QUESTIONS: alpha-helix "signals" in proteins

Mark Mark
Tue Jul 5 08:29:02 EST 1994


BACKGROUND INFO:

In a few weeks i will be giving a presentation at a literature group meeting
for the students taking the Biological Chemie Praktikum. (I am one of the 
students). I have chosen the topic of alpha-helix formation in protiens and will use several papers by G.D. Rose (Rose G.D. et al. (1994) "Rules for alpha-Helix Termination by Glycine" _Science_, 264, 1126; Rose G.D. et al. (1993) "Helix Stop Signals in Proteins and Peptides: The Capping Box" _Biochemistry_, 32, 7605; Rose G.D. et al. "Helix Signals in Proteins" _Science_ 240, 1632) as the main sources of information.



QUESTIONS:  What role do/could tertiary interactions play in stabilizing
the alpha-helix?

Does a protein first fold into its secondary structure elements and then into its tertiary structure, afterwhich the original secondary structure elements
remain as before the folding into the tertiary structure?  (If yes or no, could
you please provide references).

Rose proposes that "the folded structure of a protein is encrypted in its 
aa secquence, written in a *code* that remians obscure". (Rose, G.D. et
al. (1994) _Science_ 264, 1126).  What is the status of this obscure *code*
that he is referring to?  Is the existence of this *code* a widely held
belief?


thanks in advance,

Mark Dresser
e-mail: chs211 at stud.chem.ethz.ch



 



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