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What determines the spectrum of protein native state structures?
Author(s) -
Lezon Timothy R.,
Banavar Jayanth R.,
Lesk Arthur M.,
Maritan Amos
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20869
Subject(s) - ramachandran plot , symmetry (geometry) , protein structure , state (computer science) , biological system , spectrum (functional analysis) , crystallography , chemical physics , chemistry , computational biology , geometry , computer science , statistical physics , physics , biology , mathematics , algorithm , biochemistry , quantum mechanics
We present a brief summary of the key factors underlying protein structure, as developed in the investigations of Pauling, Ramachandran, and Rose. We then outline a simplified physical model of proteins that focusses on geometry and symmetry. Although this model superficially appears unrelated to the detailed chemical descriptions commonly applied to proteins, we show that it captures the essential elements of the chemistry and provides a unified framework for understanding the common characteristics of folded proteins. We suggest that the spectrum of protein native state structures is determined by geometry and symmetry and the role of the sequence is to choose its native state structure from this predetermined menu. Proteins 2006. © 2006 Wiley‐Liss, Inc.