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Subject: Keystone Symposia Call for Abstracts
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~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~
KEYSTONE SYMPOSIA CALL FOR ABSTRACTS
~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~

Mitochondrial Dysfunction in Pathogenesis(A4)
Organizers: John J. Lemasters and Anna-Liisa Nieminen
January 15 - January 20, 2000
Hilton of Santa Fe, Santa Fe, New Mexico

Abstract Deadline: September 15,1999
Early Registration: November 15, 1999

POSTER SESSION 1:  Inherited Mitochondrial Diseases and
Aging/Mitochondrial
Ion Permeability and Metabolic Control
POSTER SESSION 2:  Mitochondrial Permeability Transition/Mitochondrial
Regulation of Apoptosis
POSTER SESSION 3:  Mitochondria and Acute Cell Killing/Mitochondria,
Radicals and Neurodegenerative Disease/Excitotoxicity/Chemical Toxicity

For up to date programs, abstract submission instructions, on-line
registration and lodging information, go to our web site:
http://www.symposia.com 


------------------------------------------------------------------------

Keystone Symposia
Drawer 1630
Silverthorne, CO 80498

800-253-0685
970-262-1230

keystone@symposia.com 




From owner-biophysics@net.bio.net Tue Sep 14 18:14:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Biophysical Society Elects President-Elect and Council
Date: 14 Sep 1999 12:14:08 -0700
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Mary Dicky Barkley, of Case Western Reserve University, was elected
President-Elect of the Biophysical Society. She will assume that office at
the 2000 Annual Meeting in New Orleans and serve as President February
2001-February 2002.

Dorothy Beckett, Diana Bigelow, Franco Conti, Timothy Cross, Cristobal Dos
Remedios, Edward Egelman, and Jeff Gelles were elected to serve three-year
terms (2000-2002) on Council.

The changes in bylaws affecting subgroup formation and dissolution were
approved. The Society thanks the 1,110 members who voted. This number
represents 24% of eligible voters.

From owner-biophysics@net.bio.net Thu Sep 16 16:54:00 1999
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From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: New Orleans 2000 Annual Meeting
Date: 16 Sep 1999 10:53:16 -0700
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The entire Call for Papers for the 2000 Annual Meeting
can be found online at:
http://www.biophysics.faseb.org/biophys/society/annmtg


Symposia

Sensational Molecules: Mechanisms of Sensory Transduction 
Anita L. Zimmerman (Organizer), Brown University 
Marie Burns, Stanford University
Deactivation Mechanisms of Retinal Rods
Anna Menini, Istituto di Cibernetica e Biofisica, CNR, Genova 
Transduction and Adaptation in Olfactory Sensory Neurons
Padinjat Raghu, Cambridge University
Activation of the Light Sensitive Channels, TRP and TRPL, in Drosophila
David Corey, Harvard University
Dancing on the Head of a Pin: Motor Proteins in Hair-Cell Adaptation


Membrane Trafficking & Vesicle Fusion 
Wolfhard Almers (Organizer), Vollum Institute
Insights from Studying Single Exo- and Endocytic Events
Jennifer Lippincott-Schwartz, National Institutes of Health 
Kinetic Analysis of Secretory Protein Traffic
Reinhard Jahn, Max Planck Institute for Biophysical Chemistry 
Mechanism of SNARE Proteins in Membrane Fusion
Axel Brunger, Yale University
Structural and Functional Insights in the Mechanism of  Synaptic Exocytosis


Membrane Transport Proteins: Schlepping through the Bilayer
H. Ronald Kaback (Organizer), University of California, Los Angeles 
What to Do While Awaiting Crystals of a Membrane Transport Protein and Thereafter
Peter Dimroth, ETH-Zentrum, Zurich
Sodium Pumping Oxaloacetate Decarboxylase
Robert Fillingame, University of Wisconsin
Structure of the Fo Sector of the H+-Transporting Rotary ATP Synthase
Ernest Wright, University of California, Los Angeles 
Symport by Conformational Change


Muscle Crossbridges: Stepping into the Millennium
Hugh Huxley (Organizer), 
Brandeis University 
What X-rays Have Shown Us: 
Then and Now
Michael Reedy, Duke University
The Millennium Bug and its Crossbridges
Malcolm Irving, King's College London
The Motions of Myosin Heads that Drive Muscle Contraction; Structure-Function Studies on Isolated Fibers
Kathy Trybus, University of Vermont
Conventional and Unconventional Myosins: Variations on a Theme


Transmitter-gated Channel Structure and Function
Mark Mayer (Organizer), National Institutes of Health
Allosteric Modulation and Pore Block in Ionotropic Glutamate Receptors
Eric Gouaux, Columbia University
Biochemical and Crystallographic Studies of Ionotropic Glutamate Receptors
Nigel Unwin, MRC Laboratory of Molecular Biology, Cambridge
Acetylcholine Receptor at 4.6Å Resolution
Arthur Karlin, Columbia University
Gating and Electrostatics in the Acetylcholine Receptor Channel



Molecular Motors: Design and Performance 
David M. Warshaw  (Organizer), University of Vermont
Myosin Molecular Motors: Design and Performance
Jonathon Howard, 
University of Washington
The ATP Hydrolysis Cycle of Kinesin and its Coupling to Molecular Force
Robert Fletterick, University of California, San Francisco 
Structural Mechanisms of Kinesins
Mark Mooseker, Yale University
Unconventional Myosins: 
Structural and Functional Diversity


Structural Biology in Genomic Analysis
Gaetano T. Montelione (Organizer), Rutgers University 
Protein NMR and Structural Genomics
Peer Bork, European Molecular Biology Laboratory,  Heidelberg 
Predicting Targets for Structural Genomics
Stephen Burley, The Rockefeller University
X-ray Crystallography and Structural Genomics
Barry Honig, Columbia University
Structure-based Analysis of Sequence and Function



Protein Folding: An Urgent Problem in the Postgenomic Era
Lila Gierasch (Organizer), University of Massachusetts 
The Roles of Local Sequence and Global Interactions in the Folding of Predominantly b-sheet Protein
Eugene Shakhnovich, Harvard University
Listening to the Music of Evolution: 
Folding Theme with Functional Variations
Ernesto Freire, The Johns Hopkins University 
Global and Local Cooperativity in Protein Folding and Function
Jean Baum, Rutgers University
Folding of the Collagen Triple Helix and Misfolding in Disease

Folding, Form and Function of RNA and DNA molecules 
Anna Marie Pyle (Organizer), 
Columbia University 
Active-Site Structure and Catalytic Mechanism of a Large Ribozyme:  
The Group II Intron
Tobin Sosnick, University of Chicago
Thermodynamics and the Fast, 
Error-free Folding of a Large Ribozyme
Steve Schultz, University of Colorado
Structures and Assembly of O. nova Telomeric Protein-ssDNA Complexes

Fred Lewis, Northwestern University
Structure and Electron Transfer in Synthetic DNA Hairpins


G Protein Signaling: From Receptor to Effector
Heidi E. Hamm (Organizer), Northwestern University
Insight into G Protein Function and Regulation from Structural Studies
Wayne Hubbell, University of California, Los Angeles
Structural Origin of Rhodopsin Activation
Steve Sprang, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center
Conformational Control of GTP Hydrolysis by G Proteins
Lily Jan, Howard Hughes Medical Institute, University of California, San Francisco  
K+ Channels as Effectors of G 
Protein-coupled Receptors

Phosphatidylinositides in Cell Signaling 
Donald Hilgemann (Organizer), University of Texas 
Southwestern Medical Center 
Regulation of Ion Transporters and Channels by Phosphatidylinositides
Tobias Meyer, Duke University
Visualizing Signaling in the Phosphatidylinositol Pathway
James H. Hurley, National Institutes of Health
Of FYVEs, Flounders, and Flattened Folds: Structural Biology of Phosphoinositide Signaling
Christopher L. Carpenter, 
Harvard University
Phosphatidylinositol Phosphate Kinases Regulate PtdInsP2-dependent Signaling

Hybrid Crystallography and Electron Cryomicroscopy: Elucidating Macromolecular Complexes
Wah Chiu (Organizer), Baylor College of Medicine 
Stephen Harrison, Harvard University
Synergy of X-ray Crystallography and Electron Microscopy for the Structural Biology of Macromolecular Assemblies
Amy McGough, Baylor College of Medicine
New Twists in Actin Structure and Regulation Revealed by Electron Cryomicroscopy and X-ray Crystallography
Eva Nogales, University of California, Berkeley
High Resolution Model of the Microtubule by Electron Crystallography
Jack Johnson,The Scripps Research Institute
The Chemical Basis of Virus Polymorphism Determined by X-ray Crystallography and Electron Cryomicroscopy


Awards Symposium
Helen Berman, Rutgers University
Distinguished Service Award
Carolyn Cohen, Brandeis University
Elisabeth Roberts Cole Award 
Elizabeth Komives, University of California, San Diego
Michael and Kate Bárány Award for Young Investigators 

Public Policy Symposium 
Science for All Americans in the New Millennium
Jonathan King (Organizer), Massachusetts Institute of Technology
(Speakers to be announced.)


Workshops

Single Molecule Experiments: Revealing the Role of Protein Fluctuations
Shimon Weiss (Organizer), University of California Berkeley  
Sunney Xie, Pacific Northwest National Laboratory
Single-Molecule Enzymology
Carlos Bustamante, University of California, Berkeley
Steps, Arrests, and Pauses in Elongation
David Bensimon, Ecole Normale Superieure
Studying the Action of Single Enzymes on DNA
Kazuhiko Kinosita, Keio University
Stepping Rotation in a Protein Machine Revealed by Single Molecule Imaging
Fred Sigworth, Yale University
The Voltage-sensing Machinery of Potassium Channels

New Approaches to Measuring and Manipulating Intracellular Messengers
Richard H. Kramer (Organizer), University of Miami 
Real-Time Patch-Cram Detection of Cyclic GMP in Intact Cells
Elizabeth A. Finch, Duke University
Local Signaling by IP3 and Ca2+ in Dendrites of Purkinje Neurons 
Roger Y. Tsien, University of California, San Diego
New Molecules for Peeking at or Poking Intracellular Messengers
Hagan Bayley, Texas A & M Health Science Center
Engineered Channels and Enzymes for Monitoring and Controlling Cell Signalling


Closing the Reductionist Loop: Going from Biophysics to Network Dynamics
Eve Marder (Organizer), Brandeis University
Going from the Biophysics of Currents to the Dynamics of  Rhythmic Circuits
Ravi Iyengar, Mt. Sinai Medical School
Modeling Signaling Pathways
Yoram Rudy, Case Western Reserve University
Integrative Models of Cardiac Excitation and Arrhythmias
Gilles Laurent, California Institute of Technology
Circuit Dynamics and Neural Codes

From owner-biophysics@net.bio.net Thu Sep 16 19:34:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: New Orleans 2000 Annual Meeting CORRECTION
Date: 16 Sep 1999 13:34:25 -0700
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The correct URL for the Biophysical Society
Annual Meeting information and Call for Papers is:

http://www.biophysics.org/biophys/society/annmtg 

This year we are offering online registration (for 
several programs and awards) as well as a 
new online abstract submission program.

From owner-biophysics@net.bio.net Fri Sep 17 19:25:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Society Fellows Named
Date: 17 Sep 1999 13:25:24 -0700
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The Biophysical Society is proud to announce the Society Fellows for the
year 2000.  This first class of Fellows consists of 39 distinguished
Society
members who have contributed to the highest level of the science of
biophysics.

Gary K. Ackers for his fundamental studies of biomolecule association and
cooperativity, particularly in hemoglobin, and for pioneering the
application of the methods and principles of equilibrium thermodynamics to
the study and dissection of function and organization in complex
macromolecular assemblies.

Richard  W. Aldrich for his elegant and insightful work on gating of
sodium, potassium and calcium-activated potassium channels.

Clay M. Armstrong for the impact of his experimentation and original
thinking on the development of channel biophysics.

Daniel Axelrod for his pioneering research that helped develop the field
of
Total Internal Reflection Fluorescence (TIRF) microscopy.  This work has
impacted biophysical research broadly from cell biology to single molecule
detection.

Robert  L. Baldwin  for his seminal contributions to the field of protein
folding.

Francisco Bezanilla for his work in channel biophysics that includes a
rare
combination of state-of-the-art techniques in molecular biology,
electrophysiology and spectroscopy.

Rodney L. Biltonen for his many original and significant contributions to
our understanding of fundamental biological thermodynamics and 
of the kinetic basis of regulation of interacting biological systems.

Kevin P. Campbell for his research on the dystrophin-glycoprotein complex
of muscle and its role in normal skeletal muscle and in Duchenne muscular
dystrophy and his research in the field of voltage-dependent calcium
channels.

Charles R. Cantor for major contributions to the Genome project including
the development of methods for separating large DNA molecules,studies on
structural relationships in complex assemblies of proteins and nucleic
acids, and for sensitive detection of proteins and nucleic acids.

Donald  L. D. Caspar for his pioneering research in structural biology
including determination of the first viral structures by x-ray
diffraction,and for his insightful work on viruses and structures of
crystals.

Carolyn Cohen for her structural studies of fibrous and contractile
proteins.

Donald  M. Crothers for contributions to molecular biophysics and for his
pioneering contributions on the problems of RNA folding.

David Eisenberg  for his unique contributions to the understanding of
protein structure and stability using x-ray crystallography and
computational modelling, and for relating structure to function by
biochemical and genetic methods.

S. Walter Englander  for the development of models and methods that have
contributed to a much deeper understanding of the dynamic structural
processes of protein folding and hydrogen exchange rates. 

Bertil Hille for his many seminal discoveries in the fields of ion
channels
and second messengers including studies on the mechanism of permeability
of
the acetylcholine receptor ion channel.

Barry Honig for his many seminal contributions in biophysics including
quantum chemistry, biophysics of color vision, protein folding,
electrostatics of proteins in DNA and protein structure prediction and
bioinformatics.
Wayne Hubbell  for his development and application of site-directed spin
labeling.

Hugh E. Huxley for establishing the structural basis for muscle
contraction
using x-ray diffraction and electron microscopy.

William P. Jencks for his deep fundamental contributions to our
understanding of the basic chemistry underlying the mechanisms of enzyme
action.

Jack H. Kaplan for his highly significant contributions to the fields of
transport, membrane permeability and active transport and the introduction
of photorelease strategies.

Peter S. Kim  for his outstanding contributions to our understanding of
fundamental aspects of protein folding and macromolecular recognition.

Susan Lowey for dissecting and characterizing the functional domains of
muscle myosins, including the effects of light chain phosphorylation on
the
structure and activity of smooth muscle myosin.

J. Andrew McCammon for his pioneering work in the development of
biomolecular dynamics, and computer models and simulation methods, and for
his work on motion in biomolecules, which provides a foundation for modern
theoretical understanding of protein dynamics.

Harden M. McConnell for fundamental contributions in molecular orbital
theory to explain electron distributions in aromatic radicals and in
kinetic
analysis of NMR spectra, for defining the range of motions possible for
membrane components, and for developing biological applications of spin
labeling.

Gerhard Meissner for his identification and characterization of the
ryanpodine receptors, which have been instrumental in opening a new era in
excitation-coupling studies and for seminal contributions to the field of
intracellular calcium signaling.

Peter B. Moore for pioneering the development of novel biophysical
approaches for obtaining structural information on macromolecular
assemblies.

V. Adrian Parsegian  for his fundamental contributions to intermolecular
forces in biological systems through  measuring, formulating, computing
and,
gauging the consequences of forces that organize biomolecules.

Thomas D. Pollard  for major contributions in his research of the
biophysics and cell biology of the cytoskeleton.

Frederic M. Richards  for seminal contributions to methods of protein
structure determination, for a long history of contributions to protein
structures, and for deep insights into the forces of organization,
packing,
and geometries in proteins. 

Michael G. Rossmann for his fundamental contributions towards the
determination of the 3-D structure of viruses accomplished over many years
by his methodical and creative development of mathematical procedures,
unique biochemical and crystallographic techniques, and for identifying
the
Rossman fold.

Harold A. Scheraga for his pioneering development of theory and
experiments
that have led to a deeper understanding of protein structure and
properties.

Andrew P. Somlyo for his seminal contributions in collaboration with Avril
V. Somlyo to the understanding of the mechanism of contraction and its
regulation in smooth muscle as well as of excitation-coupling in skeletal
muscle. 

Avril V. Somlyo for her seminal contributions in collaboration with Andrew
P. Somlyo to the understanding of the mechanism of contraction and its
regulation in smooth muscle as well as of excitation-coupling in skeletal
muscle. 

Robert M. Stroud  for his leadership for many years in shaping the field
of
x-ray structural studies of structure-function relationships in
macromolecules and for his mentoring an extraordinarily successful group
of
graduate students and postdoctoral fellows.

Andrew G. Szent-Gyorgyi for pivotal discoveries in the field of
contractile
protein biophysics including the demonstration that myosin can be
proteolytically cleaved into distinct domains, for the discovery of
myosin-dependent regulation of muscle contraction, and for the definition
of
a critical regulatory fragment of the scallop myosin.

Thomas E. Thompson for his many lasting contributions to research on
bilayer membranes and his impact throughout the field of membrane
biophysics.

Richard W. Tsien  For his major contributions to understanding both the
fundamental biophysical and molecular properties of calcium channels, as
well as the clarification of the physiological function of the calcium
fluxes produced by these channels in important cellular and organismic
processes.  

Watt W. Webb for his work in physical measurements that illuminate
cellular
events including an exhaustive and instructive set of FRAP measurements on
lateral movement in cells and in artificial lipid preparations and for a
breathtaking set of studies on live cells.

Annemarie Weber for her fundamental contributions towards understanding
the
regulation of muscle contraction and the dynamics of actin polymerization.


From owner-biophysics@net.bio.net Tue Sep 21 15:15:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Nominations for the K.S. Cole Award
Date: 21 Sep 1999 09:15:44 -0700
Organization: BIOSCI International Newsgroups for Molecular Biology
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The Membrane Biophysics Subgroup is calling for nominations for the K.S.
Cole award for "exceptional contributions to the field of membrane
biophysics".  If you would like to nominate someone, please include an
updated CV for the nominee along with a letter explaining why you believe
that the candidate should be considered for the Cole Award and send it to:

Dr. Linda Kenney, 
Department of Molecular Microbiology & Immunology, L-220, 
Oregon Health Sciences University, 
3181 SW Sam Jackson Park Road, Portland, OR  97201, 

or by e-mail to KenneyL@ohsu.edu.  The deadline is November 1, 1999.



From owner-biophysics@net.bio.net Tue Sep 21 15:17:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Public Affairs Update
Date: 21 Sep 1999 09:16:55 -0700
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NSF Budget Struggles

The House Appropriations Subcommittee on VA, HUD and Independent agencies marked up the FY 2000 appropriations bill for the various agencies under its jurisdiction.  These include NSF, NASA, VA, HUD, and many other agencies.  

Faced with substantial reduction in its discretionary allocation because of the caps on spending imposed by the Balanced Budget Act, the Subcommittee recommended $3.647 billion for NSF in FY 2000.  This amount is $24.3 million below the FY 1999 appropriation and $274.6 million below the President¢s budget request for FY 2000.

The amount recommended for NSF¢s research and related activities was $2778.5 million, which is $8.5 million above the FY 1999 level and $225.5 million below the budget request. In that amount, the Subcommittee recommended $35 million for information technology research in the computer and information science and engineering directorate and $35 million for the Biocomplexity Initiative.The chart on the right provides recommendations for directorates.



Circular A-110 Update

On August 5, the Office of Management & Budget (OMB) published its amended Circular A-110 in the Federal Register and issued a Request for Comments on Clarifying Changes to Proposed Revision on Public Access to Research Data. 
The OMB¢s regulations are in response to the provision introduced by Representative Richard Shelby (R-AL) in the FY 1999 appropriations bill requiring all data generated under federal research grants to be available for release through the Freedom of Information Act (FOIA). The revised Circular A-110 may be accessed on the web at 
http://www.whitehouse.gov/omb/fedreg/2ndnotice-a110.html 
Comments should be addressed to 
F. James Charney, OMB Policy Analyst, and e-mailed to: grants@omb.eop.gov 


Boundaries Panel Invites Comments 

The Panel on Scientific Boundaries for Review is inviting comments on its phase 1 draft report. The Panel is conducting a comprehensive examination of the organization and function of the review process managed by NIH¢s Center for Scientific Review (CSR). 

The draft report presents a set of proposed Integrated Review Groups (IRGs), clusters of scientifically related study sections that serve as the functional units of review in CSR, some cultural norms they believe are needed to make the system operate optimally, and the procedures and principles to be followed in phase 2 when the study sections that populate the IRGs will be created. 
The draft report is posted at http://www.csr.nih.gov/bioopp/select.htm A summary is published in the Policy Forum of Science (cover date: 30 July 1999). Bruce Alberts, President of the National Academy of Sciences, is chair of the panel, an ad hoc working group of the CSR Advisory Committee. Names and affiliations of the panel are also available at the website posted above. 
JSC-CLC Grad Students and Postdocs Day on the Hill

Anatomy of a Hill Day

Achievements in public policy are similar to lab experiments.  Often the perfect approach to success is a result of a mixture of different compounds.  That was the case June 16, 1999, when the Joint Steering Committee for Public Policy (JSC) coordinated the visit of 15 graduate students and postdoctoral fellows from seven states to Washington, D.C., to advocate for biomedical research. 

June 15, 7:00 pm
The group met on the previous evening at an informal dinner in what became a wonderful networking opportunity.  The camaraderie continued the next day, making the group more cohesive and effective during the Capitol Hill visit.

9:00 am
Following breakfast, JSC staff explained what participants needed to do during their visits with Members of Congress:
Thank Members for their unprecedented 15% increase in NIH funding for FY 1999

Explain their research to Members of Congress in simple, human terms that relate to health implications

Stress the importance of federal funding of that research 

Answer Members¢ questions
Invite them to join the Biomedical Research Caucus (if they have not already joined) 
	
Encourage them to continue their support of biomedical research
	
Ask them to sign on to House Resolution 89, which calls for a $2 billion increase in Federal investment in biomedical research in fiscal year 2000.  

After some role-playing, which led to spirited interaction and a sense of what was to come, the group was ready to storm the Hill.

10:00 am
Participants split into groups to meet with various Representatives.  In all, four congressional meetings were conducted  in the morning with Representatives Sonny Callahan (R-AL), David Price (D-NC), Joe Moakley (D-MA), and Connie Morella (R-MD).  While each discussed the FY 2000 budget priorities, grad students and postdocs ably made the case for increased funding for the NIH and the NSF.

12:00 pm
The group reunited at the Congressional Biomedical Research Caucus lunch to hear Solomon Snyder of The Johns Hopkins University discuss Nitric Oxide: The Serious Side of Laughing Gas.  During the lunch, Hill Day participants sat among the Congressional staff members, who do much of the preparation work for the Members of Congress on a variety of issues, often health related.  This proved to be an ideal setting for the scientists to meet with policy makers to discuss science policy at length and in depth. 

1:00 pm 
Representative George Gekas (R-PA), Co-Chair of the Congressional Biomedical Research Caucus, met with the entire group and commended them for their participation.  He stressed the importance of scientists taking an active role in advocating for federal increases in funding for biomedical research and urged them to continue with their message in each subsequent visit.  

2:00 pm
The group met with Representative John Porter (R-IL), Chairman of the Labor/Health and Human Services Subcommittee, which controls the funding for the NIH.  Congressman Porter is a passionate supporter of biomedical research and has led the effort for doubling the NIH. He explained the legislative process and gave a realistic assessment of the FY 2000 budget battles that will take place and the difficulties ahead in garnering a substantial increase for biomedical research this year.  Many Hill Day participants reported that this meeting, with Representative Porter, was the most informative of the day. 

3:00 pm
Participants again split into smaller groups to meet with their respective Members of Congress.  Representatives Spencer Bachus (R-AL), Anna Eschoo (D-CA), Elijah Cummings (D-MD), Shelley Berkely (D-NV), Ben Cardin (D-MD), Michael Capuano (D-MA), and Steny Hoyer (D-MD) were all visited.  In addition, a few Hill Day participants met Maryland Senator Paul Sarbanes¢ staff. 

4:00 pm
Debriefing.  Participants gave their impressions of the day and received feedback.  They were told that the group¢s activities made a lasting impression.  Congressman David Price (D-NC) had noted that while he knows that many groups bring their members to Capitol Hill, this was the first time he had heard of any group specifically bringing in graduate students.  He had been impressed by their enthusiasm and the quality of their comments and questions. 
This is the strength of Hill days:  letting members advocate for biomedical research.  The day was so successful that the JSC is making it an annual event.

¯Alec Stone, JSC-CLC National Field     
   Coordinator




FASEB 

Breakthroughs

The latest Breakthroughs in Bioscience article has been published.  Copies of the eight-page Cloning: Past, Present, and the Exciting Future, by Marie Di Berardino, are now available. The Breakthroughs in Bioscience series features articles that describe and explain basic biomedical research and its impact on disease prevention and treatment. Other topics in the series include Science, Serendipity, and a Hew Hantavirus, Blood Safety in the Age of AIDS, The Polymerase Chain Reaction, Cardiovascular Diseases and the Endothelium, Unraveling the Mystery of Protein Folding, and Helicobacter pylori and Ulcers. 

For more information, contact FASEB Office of Public Affairs, 301-571-3657.	

From owner-biophysics@net.bio.net Thu Sep 23 21:09:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: The New Protein DataBank
Date: 23 Sep 1999 15:09:47 -0700
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On July 1, 1999, the Research Collaboratory for Structural Bioinformatics
(RCSB) became fully responsible for the operation of the Protein Data Bank
(PDB). Throughout the nine-month transition period, which began when the
National Science Foundation announced the award on October 1, 1998, a
concentrated effort was made to ensure that the transition of management
between Brookhaven National Laboratory (BNL) and the RCSB was as seamless
and non-disruptive as possible.  Users who went to the PDB site on June
30,
1999, were automatically redirected to the new home of the PDB at
http://www.rcsb.org/ 

During the transition period, the RCSB phased in many new features of the
PDB. A Web-based tool, the AutoDep Input Tool (ADIT;
http://pdb.rutgers.edu/adit/), was introduced for the easy deposition of
data. The BNL-developed tool, AutoDep, was ported to the RCSB site to
allow
people to complete depositions started at the BNL site and to provide
continuity.  For all data deposited, the RCSB has developed a much faster
data processing system that reduces the processing time by a factor of ten
to assure the timely access of information by the community of users. The
RCSB also began accepting data collected and processed at remote sites,
the
first one being at the European Bioinformatics Institute in Hinxton,
England. 

The RCSB has released two new search engines: SearchLite and SearchFields.
SearchLite allows simple text-based searches while SearchFields allows
searches to be done on specific data items stored in the database. Both
have
very rich reporting capabilities that include a Structure Explorer page
with
summary information about each structure, reports about the geometric
features of the structures, and structure neighboring. Cross-links to
other
databases are also provided.

The RCSB supports two ftp archives: ftp://ftp.rcsb.org, a reorganized and
more logical organization of all PDB data, software, and documentation;
and
ftp://bnlarchive.rcsb.org, a near-identical copy  of the original BNL
archive for BNL-style PDB mirrors. The new RCSB-style mirrors being
established around the world will contain the flat file data as well as
the
full database of information.
The RCSB is a consortium composed of Rutgers, the State University of New
Jersey; the University of California at San Diego (UCSD); and the National
Institute of Standards and Technology (NIST). The project runs under a
Cooperative Agreement from the National Science Foundation (NSF), with
funding from that agency as well as the Department of Energy, and two
units
of the National Institutes of Health: the National Institute of General
Medical Sciences and the National Library of Medicine.  The
responsibilities
of the three sites have been divided according to experience and
expertise.


Principal investigator Helen Berman, a member of the Biophysical Society
and Rutgers professor of chemistry, was part of the original team that
developed the PDB at Brookhaven in 1971. She is responsible for the
development of the  Nucleic Acid Database (NDB) at Rutgers, which
assembles
and distributes structural information about nucleic acids and contains an
atlas, an archive and a sophisticated search engine to access the data. In
collaboration with John Westbrook, who has played a key role in the
development of the mmCIF dictionary, they have drawn on the experiences
with
the NDB and have led a team of people who have created a new data
deposition
and processing system for all macromolecules.

At the San Diego Supercomputer Center (SDSC) at UCSD, senior principal
scientist and adjunct professor Phil Bourne leads a group of scientists in
the Biological Data Representation and Query Initiative. The group has
developed locally a number of databases containing derived data on protein
structures and maintains a mirror site of Berman's NDB. Recent work
produced a database of structure comparisons for the more than 10,000
structures in the PDB. Together with Peter Arzberger, a computational
biologist and Executive Director of NPACI, this group will be responsible
for all aspects of data query and distribution.

Gary L. Gilliland, chief of the Biotechnology Division in NIST's Chemical
Science and Technology Laboratory, will lead the NIST effort. He has
maintained an active research program in protein crystallography for more
than 20 years. Gilliland also played a key role in establishing the Center
for Advanced Research in Biotechnology (CARB), a joint effort of NIST and
the University of Maryland Biotechnology Institute, where he served as the
Associate Director until 1996. Phoebe Fagan, who has worked for many years
in the NIST Standard Reference Data program, is responsible for the
technical aspects of the project at that site. NIST will establish data
uniformity of the old and new structures in order to improve the
accessibility and reliability of queries and will also manage the Master
Archive. 

The creation of this resource was both exciting and demanding.  The
successful culmination of the transition of the PDB from BNL to the RCSB
required the dedication and cooperation of the members of the RCSB team,
the
staff at Brookhaven National Laboratory led by Joel Sussman, and the
federal
agencies who fund the PDB. 

From owner-biophysics@net.bio.net Thu Sep 23 21:31:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Subgroup Activities
Date: 23 Sep 1999 15:31:18 -0700
Organization: BIOSCI International Newsgroups for Molecular Biology
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Bioenergetics 
We are happy to report that attendance at the annual programs presented by the Bioenergetics Subgroup has been steadily increasing in past years.  In part, the increase in attendance is a consequence of the timely and provocative topics chosen for the symposia. The subgroups have the unique organizational opportunity to assemble programs of depth and diversity within the larger annual meeting of the Biophysical Society. While the Bioenergetics Subgroup is comprised of approximately 110 registered members, our annual Subgroup symposia attract approximately 300-500 participants to both the morning and the afternoon sessions. The Bioenergetics Subgroup Symposia have become increasingly attractive to participants with a wide range of scientific interests.  The unique scheduling of the Subgroup meetings a day prior to the formal Biophysical Society program offers meeting attendees the opportunity to participate fully in the organized program. 
The day-long format for the Bioenergetics Subgroup 2000 program was chosen from program topics that were originally raised at the Bioenergetics Subgroup Business Meeting in Baltimore.  The choice was made to assemble the morning, afternoon and roundtable sessions under the unifying scope of membrane protein structural analyses.  This format was realized as a consequence of fruitful communication within the Subgroup constituency,  with added input and direction from experts in the field including. William Cramer  and Shelagh Ferguson-Miller.
The program for 2000 reflects our interest to (re)explore the classical aspects of bioenergetics (oxidative phosphorylation, electron transport, and vectorial metabolite transport) from a structural vantage point.
While the primary focus of this program is on mitochondrial proteins and processes, this full-day session is anticipated to be of interest to the broader scientific community. In the past years, the three-dimensional structures of more than 25 membrane proteins have been solved.  The vast majority of these proteins are from energy-transducing membranes. While it is important to review the structures of these solved proteins within the context of their substrate or electron-transporting function, it is even more important to consider these proteins as forming the foundation for the hundreds of proteins whose structures are not yet solved. Therefore, we assembled the symposia to represent a progression from the known structures of the electron transport protein(s) bc1 and b6f to the inferred structures of the mitochondrial transporters and finally to the discussion of principles of protein structure and modeling in the roundtable session.   It is our hope that this day-long prog!
!
ram, which is both timely and f
The program Structural Analysis Of Membrane Proteins: Realizing The Mitochondriaós Potential reunites the fundamental and classical principles of modern Bioenergetics with the atomic structures of the proteins that mediate the processes. This full-day program will be offered by the Bioenergetics Subgroup on Saturday, February 12, 2000, in the New Orleans Convention Center at the Societyós Annual Meeting. The program for the 2000 meeting marks the first time that two areas of research have been integrated with the objective of provoking comparisons between membrane proteins whose structures have been determined and transmembrane proteins whose structures are being eagerly pursued. 
The morning session is dedicated to the process of electron transport (E. Berry  and C. Yu, Co-chairs) and is focused upon cytochrome bc1 and b6f complexes, multi-subunit membrane proteins whose three-dimensional structures have been solved by crystallization and X-ray diffraction. This session will address the questions of mechanisms of electron transport highlighting the kinetics (C. Yu), substrate binding sites (E. Berry and S. Iwata) and structures of bc1 (C. Hunte) and b6f (C. Breyton and W.A. Cramer) complexes. 
The afternoon session will explore metabolite transport through structural and functional studies of mitochondrial transporters (R. Kaplan, Chair), a family of membrane proteins that represent model systems for passive transport, yet have resisted crystallization. This session will address the historic aspects of mitochondrial transport (M. Klingenberg), and questions pertaining to mechanisms of transmembrane metabolite transport through the identification of novel carriers (J.E. Walker), the structure and functional studies of the citrate (R. Kaplan) and phosphate (H. Wohlrab) carriers, and a structural analysis of the proteins that comprise the mitochondrial contact sites. 
The problems»practical, hypothetical, and philosophical»raised in the morning and afternoon sessions will be given a voice in the roundtable session scheduled at the end of the day. The roundtable discussion (Sir John Walker, Chair) is an essential feature of this program and will be composed of platform speakers from the two sessions. The goal of the roundtable is to discuss 1) the major concepts of protein structure and folding using the solved structures as a conceptual scaffold and 2) the practical application of these global lessons that have been gleaned about protein structure towards protein purification, crystallization, and structural modeling. We anticipate that the information in this day-long meeting will provoke discussion and ultimately facilitate future studies whose goals are to solve the three- dimensional structure of membrane proteins. 
The Bioenergetics Subgroup Symposium  is supported by a generous contribution from Anatrace, Inc.
»M.W. McEnery, Subgroup Chair 
==========
Biological Fluorescence - 2000 Meeting Program
Arrangements are well underway for the Biological Fluorescence Subgroup February 2000 Meeting in New Orleans, which will feature new and exciting research presentations, our subgroup awards, and roundtable discussion.  Roger Tsien, of the University of California, San Diego, and Antonie Visser, of  Wageningen University, The Netherlands, have agreed to present talks on their research interests, tentatively entitled, Genetically Encoded Physiological Indicators and Fluorescence and Molecular Dynamics of Flavoproteins, respectively. Of course, the last two speakers of the session will be the winners of the Biological Fluorescence Subgroupós prestigious and coveted Jablonski and Young Fluorescence Investigator Awards. 
Awards - Spectronic Unicam will again cosponsor the Jablonski Award, presented annually to an established investigator for outstanding fundamental accomplishments in the principles and applications of fluorescence spectroscopy.  The awardee receives a $2,500 cash prize. In addition, the awardeeós name will join former recipients Professors Gregorio Weber (1997), Michael Kasha (1998), and Lenny Brand  (1999) on the beautiful wood carved Jablonski plaque (http://www.phys.uni.torun.pl/~lum98/ 
award.html).
SPEX/JY/Horiba has generously agreed to continue its support of the Young Fluorescence Investigator Award.  This award is based on novel applications of fluorescence spectroscopy to current work in biology and biophysics by a pre-tenure faculty member, and is accompanied by a cash prize of $1,000. Call for nominations will be announced formally in the fall. The deadline  for receipt of nominations for these awards is Friday, December 10, 1999. For more information about the nomination procedure, please check our subgroup web page or email me directly (see following page).
Roundtable - Our subgroup roundtable topic is focused on Protein/Nucleic Acid Interactions, and promises to be a lively and interesting discussion.  Panel participants include: 
Mary Hawkins, NCI/NIH, Pteridine Nucleoside Analogues*Properties and Applications; 
Robert Clegg, University of Illinois, Probing the Structures and Functions of Nucleic Acids with Photons
David  Millar, Scripps Research Institute, Dissecting the Mechanism of DNA Polymerase Proofreading Using Time-Resolved Fluorescence Spectroscopy
Subgroup Web Page - Other news is that the Biological Fluorescence Subgroup web page will be updated (http://www.biophysics.org/biophys/society/subgrps/subgrps.htm). Check out the subgroupós web page for information about the subgroup awards, upcoming fluorescence meetings, including the complete Biophysical Society subgroup 2000 program, subgroup members, and useful links for the fluorescence community.  If you have any information that you would like to post, please let me know.
Finally, for your information, at a meeting of subgroup chairs held at the last Biophysical Society meeting in Baltimore, it was decided to feature a booth at the Annual Meeting to promote the various subgroups by displaying their mission statements, officers, list of awards, etc., and material encouraging membership (still only $10 for the Biological Fluorescence subgroup - so donót forget to renew your membership!). This booth will be located adjoining the BJ/Society booth, in the exhibit hall. Be sure to come by and bring your fluorescence friends. All suggestions, news of upcoming meetings, and general information valuable to the fluorescence community are welcome.  
*Lesley Davenport, Chair   LDvnport@brooklyn.cuny.edu 
============
Membrane Biophysics - K.S. Cole Award Nominations
The Membrane subgroup welcomes nominations for the K.S. Cole Award.  The deadline for nominations is September 1, 1999.  If you have a suggestion for a future symposium topic or K.S. Cole awardee, please present it to a member of the Advisory Committee: David Dawson, University of Michigan; Sarah Garber, Allegheny University for the Health Sciences; Linda J. Kenney, Oregon Health Sciences University; Joe Hume, University Nevada-Reno; Carol Vandenberg, University of California,Santa Barbara; Doug Eaton, Emory University
»David Dawson, 1999/2000 Chair
=============
Membrane Structure and Assembly - Member Alert
The Membrane Structure and Assembly Subgroup sent an e-mail to subgroup members (past and present) in late July to remind them to include Subgroup dues with their Society dues payments.  If you have not yet renewed your membership in the Subgroup or are a past member who has lost his/her way, please renew ASAP.  The goal is to increase our member base to include all Society members whose intellectual interests are served by the Subgroup.  The Subgroupós purpose is to foster and advance knowledge about the physical properties of lipids and of lipid-protein complexes in biomembranes.  As such, its mission should be to provide an intellectual home base for its members in a Biophysical Society that is rapidly growing and expanding its realm of interests. If the Subgroup is at least one of your intellectual homes in the Society, please reaffirm your commitment to this mission both by renewing your membership and by becoming actively involved in your subgroupós activities.  The subg!
!
roup depends on its members to 
2000 Symposium - Again this year, the Subgroup will sponsor an exciting Symposium at the Society meeting entitled Phospholipases and Sphingomyelinases: Enzymology at a Surface with Mike Gelb, John Bell, Rod Biltonen, Mary Roberts, and  Felix Goni presenting talks. Following the Symposium, we will have our usual boring business meeting and a new exciting Members Only Mixer.  The subgroup will provide refreshments and snacks in the hope of giving us all a chance to renew acquaintances and start discussions that will lead to a more productive meeting.  I welcome your input on how to make our mixer a success.
Call for Nominations - Finally, members should submit nominations for chair and chair-elect of the subgroup as soon as possible to me (uncbrl@med.unc.edu).  Please check with the person whom you plan to nominate before making a nomination.  I encourage you to volunteer even!  Please participate in this important aspect of the life of your subgroup. The MSAS is its members.  Join us and get involved!
»Barry Lentz,1999 MSAS Chair
============
Motility
The Motility Subgroup will meet in New Orleans on Saturday, February 12 during the Societyós Annual Meeting.  An exciting program is being planned entitled Molecular Motors and Their Supporting Cast: Past and Future. Speakers will include: Marie-France Carlier, CNRS, France (Title to be announced); Christine Cremo, Washington State University, Regulation of smooth muscle and nonmuscle myosin II; Lynn Coluccio
Boston Biomedical Research Institute, Mechanism of the small mammalian molecular motors, myosins I; Miklos Kellermayer, Pecs University Medical School, The muscular brake: mechanisms of regulating sarcomeric extensibility by titin; Toshio Yanagida, Osaka University Medical School, Myosin neck region does not act as a lever arm but controls velocity and directionality of motion; Steve Block, Stanford University, Nanomechanical studies of single kinesin motors: old and new perspectives
Evening speaker - Hugh Huxley, Brandeis University, Trying to understand how muscles contract
»Henk Granzier, Program Chair 

From owner-biophysics@net.bio.net Mon Sep 27 20:42:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: On-Line Textbook
Date: 27 Sep 1999 14:42:17 -0700
Organization: BIOSCI International Newsgroups for Molecular Biology
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Two additional chapters have been added to the On-Line Textbook of
Biophysics.   

Membranes
Membrane Proteins and Bilayers, Stephen White

Computational Biology 
Molecular Modeling, (Spring 99, course homework assignments),Tamar Schlick

These latest chapters include examples of web-related resources that will
become part of each volume and are designed to aid in the teaching and
learning of biophysics. If you have discovered useful sites in your
journeys
through cyberspace, ones you feel would add value to the On-Line Textbook
of
Biophysics, please send them to: 

Victor Bloomfield (victor@tc.umn.edu) or Carol Gross (cgross@cbs.umn.edu)

The Textbook may be accessed through the Biophysical Society web site:
http://www.faseb.org/biophys/society/biohome.htm
or at the textbook's URL:
http://biosci.umn.edu/biophys/OLTB/

From owner-biophysics@net.bio.net Tue Sep 28 20:07:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: PRAT Postdoctoral Fellowships
Date: 28 Sep 1999 14:07:33 -0700
Organization: BIOSCI International Newsgroups for Molecular Biology
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The Pharmacology Research Associate (PRAT) Program of the National
Institute
of General Medical Sciences (NIGMS) sponsors postdoctoral fellows
conducting
research at the NIH in the pharmacological sciences.  This can include
research in the areas of signal transduction, drug metabolism,
immunopharmacology, chemistry and drug design, structural biology,
endocrinology, neuroscience, clinical pharmacology, among other areas. 
Potential fellows make an application together with a preceptor to the
PRAT
Program.  Selected fellows receive a two-year appointment, salary,
supplies,
and travel funds from the NIGMS to support research in the preceptors'
laboratories.  Candidates may apply prior to coming to NIH or FDA, or they
may have started postdoctoral research at NIH or FDA within the 12-month
period prior to the application receipt deadline.  Applications are due on
or before January 5, 2000, for fellowships starting in October of that
year.
 Only U.S. citizens or permanent residents are eligible.  Contact the PRAT
Program Assistant at (301) 594-3583 or prat@nigms.nih.gov to request a
PRAT
Fact Sheet and an application kit, or visit the NIGMS home page at
http://www.nih.gov/nigms/about_nigms/prat.html to view the PRAT Fact
Sheet.


From owner-biophysics@net.bio.net Thu Sep 30 19:37:00 1999
Path: biosci!biosci!not-for-mail
From: DMCGAVIN@biophysics.faseb.org
Newsgroups: bionet.prof-society.biophysics
Subject: Upcoming Events
Date: 30 Sep 1999 13:37:37 -0700
Organization: BIOSCI International Newsgroups for Molecular Biology
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November 14-18, 1999
AAPS Annual Meeting & Exposition, 
Quest for the Magic Bullet: An Astounding Century
New Orleans, LA
Contact: AAPS, 1650 King Street, Suite 200, 
Alexandria, VA  22314
Phone: 703-548-3000, http://www.aaps.org/annualmeet.html 

December 11-15, 1999
American Society for Cell Biology 39th Annual Meeting,  Washington, DC  
Contact: ASCB, 9650 Rockville Pike, Bethesda, MD 20814 Phone:
301-530-7153,
Fax: 301-530-7139, 
E-mail: ascbinfo@ascb.org, http://www.ascb.org/ascb 

December 20-21, 1999
The British Biophysical Society Annual Meeting
Biophysics - Past & Future, Birkbeck College London, 
Contact: Miss Sylvia Ertelt, Biochemistry & Molecular Biology Department,
University College London, Gower Street, London WC1E 6BT Phone: +44 0171
380
7048 http://www.cryst.bbk.ac.uk/BBS/meetings_forth.html 

February 12-16, 2000
Biophysical Society 44th Annual Meeting, New Orleans, LA Contact:   The
Biophysical Society, 9650 Rockville Pike, Bethesda, MD  20814
Phone: 301-530-7114 Fax: 301-530-7133, 
E-mail: society@biophysics.faseb.org 
http://www.biophysics.org/biophys/society/annmtg 

April 12-14, 2000
High-Frequency Electron Paramagnetic Resonance: 
Technology and Applications, 
Amsterdam, The Netherlands, Contact: Mr. R. des Bouvrie
Royal Netherlands Academy of Arts and Sciences
P.O. Box 19121, 1000 GC Amsterdam, The Netherlands Phone: +31 20 55 10
730,
Fax: +31 20 62 04 941
E-mail: roy.des.bouvrie@bureau.knaw.nl  http://www.knaw.nl/hfepr 

July 16-20, 2000
18th International Congress of Biochemistry and Molecular Biology: Beyond
the Genome,  Birmingham, UK. 
Contact: The Biochemical Society, 59 Portland Place, London W1N 3AJ  UK, 
Phone: +44 171 580 3481, Fax: +44 171 637 7626
E-mail: info@iubmb2000.org;  http://www.iubmb2000.org

