Literature DB >> 9269572

The Levinthal paradox: yesterday and today.

M Karplus1.   

Abstract

A change in the perception of the protein folding problem has taken place recently. The nature of the change is outlined and the reasons for it are presented. An essential element is the recognition that a bias toward the native state over much of the effective energy surface may govern the folding process. This has replaced the random search paradigm of Levinthal and suggests that there are many ways of reaching the native state in a reasonable time so that a specific pathway does not have to be postulated. The change in perception is due primarily to the application of statistical mechanical models and lattice simulations to protein folding. Examples of lattice model results on protein folding are presented. It is pointed out that the new optimism about the protein folding problem must be complemented by more detailed studies to determine the structural and energetic factors that introduce the biases which make possible the folding of real proteins.

Mesh:

Year:  1997        PMID: 9269572     DOI: 10.1016/s1359-0278(97)00067-9

Source DB:  PubMed          Journal:  Fold Des        ISSN: 1359-0278


  43 in total

Review 1.  Folding funnels, binding funnels, and protein function.

Authors:  C J Tsai; S Kumar; B Ma; R Nussinov
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

Review 2.  Folding and binding cascades: shifts in energy landscapes.

Authors:  C J Tsai; B Ma; R Nussinov
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-31       Impact factor: 11.205

3.  Understanding beta-hairpin formation.

Authors:  A R Dinner; T Lazaridis; M Karplus
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-03       Impact factor: 11.205

Review 4.  The hydrogen exchange core and protein folding.

Authors:  R Li; C Woodward
Journal:  Protein Sci       Date:  1999-08       Impact factor: 6.725

5.  Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model.

Authors:  D J Bicout; A Szabo
Journal:  Protein Sci       Date:  2000-03       Impact factor: 6.725

Review 6.  Folding and binding cascades: dynamic landscapes and population shifts.

Authors:  S Kumar; B Ma; C J Tsai; N Sinha; R Nussinov
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

7.  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

8.  Observation of strange kinetics in protein folding.

Authors:  J Sabelko; J Ervin; M Gruebele
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

9.  Fast protein folding on downhill energy landscape.

Authors:  Andrea Cavalli; Urs Haberthür; Emanuele Paci; Amedeo Caflisch
Journal:  Protein Sci       Date:  2003-08       Impact factor: 6.725

10.  Funnel sculpting for in silico assembly of secondary structure elements of proteins.

Authors:  Boris Fain; Michael Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  2003-08-18       Impact factor: 11.205

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