QUESTIONS: alpha-helix "signals" in proteins

Toshiya Endo d43162a at nucc.cc.nagoya-u.ac.jp
Thu Jul 14 05:19:26 EST 1994


In article <Pine.3.89.9407121006.A5334-0100000 at fox.cce.usp.br>, 
szeinfel at FOX.CCE.USP.BR (Rafael N Szeinfeld) writes:
> 
> 	First how proteins solve the Levinthal paradox that is, how a
> protein folds so fast with so many configurations to be tested in order to
> find out the energy minimun (this minimun being or not path dependent). 
> This seems to be sequence independent since all proteins folds fast (in 
> comparison to the time it would take to search the whole configurational 
> space).

The tendency of proteins to fold fast to native conformations may not be 
sequence independent.  Nature may well have selected proteins that can 
fold fast, since polypeptides that remain unfolded in the cells are degraded 
by specific proteases.  Recent works by Karplus' group (Nature 369, 248-
251) suggest that such fast-folding sequences may give structures that 
are thermodynamically stable. 


Toshiya Endo
Department of Chemistry, Faculty of Science
Nagoya University, Chikusa-ku, Nagoya 464-01, Japan
e-mail: d43162a at nucc.cc.nagoya-u.ac.jp       



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