Literature DB >> 9197236

Protein folding: does diffusion determine the folding rate?

T E Creighton1.   

Abstract

A major question about protein folding is whether the coming together by diffusion of different segments of the polypeptide chain is rate-determining. This seemingly simple question has been very difficult to answer experimentally, but a positive result has now been obtained with one small model protein.

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Year:  1997        PMID： 9197236     DOI： 10.1016/s0960-9822(06)00180-1

Source DB:  PubMed          Journal:  Curr Biol        ISSN： 0960-9822            Impact factor:   10.834


  4 in total

1.  The topomer-sampling model of protein folding.

Authors:  D A Debe; M J Carlson; W A Goddard
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

2.  High viscosity and anisotropy characterize the cytoplasm of fungal dormant stress-resistant spores.

Authors:  J Dijksterhuis; J Nijsse; F A Hoekstra; E A Golovina
Journal:  Eukaryot Cell       Date:  2006-11-10

3.  Limited internal friction in the rate-limiting step of a two-state protein folding reaction.

Authors:  K W Plaxco; D Baker
Journal:  Proc Natl Acad Sci U S A       Date:  1998-11-10       Impact factor: 11.205

4.  The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding.

Authors:  S Sato; C J Sayid; D P Raleigh
Journal:  Protein Sci       Date:  2000-08       Impact factor: 6.725
  4 in total

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