Literature DB >> 14499890

Hydrophobicity--getting into hot water.

Arthur M Lesk1.   

Abstract

In his famous 1959 review, Walter Kauzmann clarified important features of the thermodynamic stabilities of proteins. The hydrophobic effect is recognised as an important contributor to the stability of proteins and an important determinant of their structural patterns. As generally understood, it depends on the unusual properties of cold water and its interactions with nonpolar solutes. Here we comment on the relationship between this paradigm and the stabilities and structures of proteins from thermophilic organisms.

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Year:  2003        PMID: 14499890     DOI: 10.1016/s0301-4622(03)00086-3

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures.

Authors:  Mingjie Han; Sanhui Liao; Xiong Peng; Xiaoqun Zhou; Quan Chen; Haiyan Liu
Journal:  Protein Sci       Date:  2019-05-23       Impact factor: 6.725

  1 in total

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