Literature DB >> 12144347

Loop fold structure of proteins: resolution of Levinthas paradox.

Igor N Berezovsky1, Edward N Trifonov.   

Abstract

According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins - 25-30 residues.

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Year:  2002        PMID: 12144347     DOI: 10.1080/07391102.2002.10506817

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


  5 in total

1.  Understanding the determinants of stability and folding of small globular proteins from their energetics.

Authors:  Guido Tiana; Fabio Simona; Giacomo M S De Mori; Ricardo A Broglia; Giorgio Colombo
Journal:  Protein Sci       Date:  2004-01       Impact factor: 6.725

2.  Self-inflicted fear of evolution.

Authors:  Edward N Trifonov
Journal:  Orig Life Evol Biosph       Date:  2006-12       Impact factor: 1.950

3.  Organization of the multiaminoacyl-tRNA synthetase complex and the cotranslational protein folding.

Authors:  Igor N Berezovsky; Zejun Zheng; Atsushi Kurotani; Alexander A Tokmakov; Igor V Kurochkin
Journal:  Protein Sci       Date:  2015-07-14       Impact factor: 6.725

4.  Paradoxes of early stages of evolution of life and biological complexity.

Authors:  Alexey V Melkikh
Journal:  Orig Life Evol Biosph       Date:  2015-03-11       Impact factor: 1.950

5.  Statistics of knots, geometry of conformations, and evolution of proteins.

Authors:  Rhonald C Lua; Alexander Y Grosberg
Journal:  PLoS Comput Biol       Date:  2006-05-19       Impact factor: 4.475

  5 in total

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