Literature DB >> 1184281

Theory of reversible denaturation of globular proteins.

N Go.   

Abstract

A theoretical method is developed by which the character of the process of protein denaturation (e.g., whether or not it is of the all-or-none type) can be discussed in terms of conformation of native proteins and the forces stabilizing it. An important role is played by a quantity S(H): entropy of a protein molecule in solution in the conformational states with a given value of enthalpy H. It is demonstrated that the all-or-none type denaturation of proteins is a rather direct consequence of the globularity and specificity of the native conformations. Denaturations with significant intermediate states are discussed. Denaturations induced by added denaturants are also discussed.

Mesh:

Year:  1975        PMID: 1184281

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  2 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.  Energy profile of the space of model protein sequences.

Authors:  G Tiana; R A Broglia; E I Shakhnovich
Journal:  J Biol Phys       Date:  2001-06       Impact factor: 1.365

  2 in total

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