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The distribution of structures in evolving protein populations
Author(s) -
Taverna Darin M.,
Goldstein Richard A.
Publication year - 2000
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(200001)53:1<1::aid-bip1>3.0.co;2-x
Subject(s) - statistical physics , distribution (mathematics) , biological system , population , sequence (biology) , protein structure , physics , chemistry , topology (electrical circuits) , mathematics , biology , mathematical analysis , combinatorics , biochemistry , demography , nuclear magnetic resonance , sociology
Proteins exhibit a nonuniform distribution of structures. A number of models have been advanced to explain this observation by considering the distribution of designabilities, that is, the fraction of all sequences that could successfully fold into any particular structure. It has been postulated that more designable structures should be more common, although the exact nature of this relationship has not been addressed. We find that the nonuniform distribution of protein structures found in nature can be explained by the interplay of evolution and population dynamics with the designability distribution. The relative frequency of different structures has a greater‐than‐linear dependence on designability, making the distribution of observed protein structures more uneven than the distribution of designabilities. The distribution of structures is also affected by additional factors such as the topology of the sequence space and the similarity of other structures. © 2000 John Wiley & Sons, Inc. Biopoly 53: 1–8, 2000