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Atom depth in protein structure and function

Authors
Publisher
Elsevier Ltd
Publication Date
Volume
28
Issue
11
Identifiers
DOI: 10.1016/j.tibs.2003.09.004
Disciplines
  • Biology
  • Mathematics

Abstract

Abstract Atom depth, originally defined as the distance between a protein atom and the nearest water molecule surrounding a protein, is a simple but valuable geometrical descriptor of the protein interior. It can be easily computed from the 3D structure of a protein, thus complementing the information provided by the calculation of the solvent accessible surface area and buried surface area. Depth has been found to be correlated with several molecular, residue and atomic properties, such as average protein domain size, protein stability, free energy of formation of protein complexes, amino acid type hydrophobicity, residue conservation and hydrogen/deuterium amide proton exchange rates.

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