Literature DB >> 4033149

Investigation of protein refolding: a special feature of native structure responsible for refolding ability.

I Simon.   

Abstract

A possible origin of the refolding ability of globular proteins is discussed. It is shown that the structure of native proteins has a special feature, namely, that this is the only structure in which the short overlapping segments of the polypeptide chain are in one of the significantly stable conformations of the oligopeptides with the same amino acid sequences as segments themselves. It is shown that this special feature is responsible for the refolding ability of proteins. A simple formula is given for the estimation of the time, t, necessary for the spontaneous formation of a refolding nucleus by a certain segment and it is shown that the segment which has the smallest t value, will serve as a refolding nucleus. It is suggested that natural selection which ensures the maintenance of the native structure of globular proteins automatically results in the refolding ability of proteins regardless of the biological relevance of this ability.

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Year:  1985        PMID: 4033149     DOI: 10.1016/s0022-5193(85)80187-9

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  1 in total

1.  Calculation of protein conformation as an assembly of stable overlapping segments: application to bovine pancreatic trypsin inhibitor.

Authors:  I Simon; L Glasser; H A Scheraga
Journal:  Proc Natl Acad Sci U S A       Date:  1991-05-01       Impact factor: 11.205

  1 in total

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