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Open Access Open Badges Research

Rate and breadth of protein evolution are only weakly correlated

Sergey A Naumenko12* and Alexey S Kondrashov23

Author Affiliations

1 Institute for Information Transmission Problems, Russian Academy of Sciences, Bolshoi Karetny pereulok 19, Moscow 127994, Russia

2 Department of Bioengineering and Bioinformatics, M. V. Lomonosov Moscow State University, Vorbyevy Gory 1-73, Moscow 119992, Russia

3 Life Sciences Institute and Department of Ecology and Evolutionary Biology, University of Michigan, Ann Arbor, Michigan 48109, USA

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Biology Direct 2012, 7:8  doi:10.1186/1745-6150-7-8

Published: 15 February 2012



Evolution at a protein site can be characterized from two different perspectives, by its rate and by the breadth of the set of acceptable amino acids.


There is a weak positive correlation between rates and breadths of evolution, both across individual amino acid sites and across proteins.


Rate and breadth are two distinct, and only weakly correlated, characteristics of protein evolution. The most likely explanation of their positive correlation is heterogeneity of selective constraint, such that less functionally important sites evolve faster and can accept more amino acids.


This article was reviewed by Eugene V. Koonin, Arcady R. Mushegyan, and Eugene I. Shakhnovich.