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More compact protein globules exhibit slower folding rates
Author(s) -
Galzitskaya Oxana V.,
Reifsnyder Danielle C.,
Bogatyreva Natalya S.,
Ivankov Dmitry N.,
Garbuzynskiy Sergiy O.
Publication year - 2007
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.21619
Subject(s) - globular protein , beta (programming language) , protein folding , folding (dsp implementation) , chemistry , alpha (finance) , protein structure , residue (chemistry) , crystallography , biophysics , biochemistry , biology , mathematics , computer science , electrical engineering , engineering , construct validity , statistics , programming language , psychometrics
We have demonstrated that, among proteins of the same size, α/β proteins have on the average a greater number of contacts per residue due to their more compact (more “spherical”) structure, rather than due to tighter packing. We have examined the relationship between the average number of contacts per residue and folding rates in globular proteins according to general protein structural class (all‐α, all‐β, α/β, α+β). Our analysis demonstrates that α/β proteins have both the greatest number of contacts and the slowest folding rates in comparison to proteins from the other structural classes. Because α/β proteins are also known to be the oldest proteins, it can be suggested that proteins have evolved to pack more quickly and into looser structures. Proteins 2008. © 2007 Wiley‐Liss, Inc.