Premium
Co‐evolutionary constraints of globular proteins correlate with their folding rates
Author(s) -
Mallik Saurav,
Kundu Sudip
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.032
Subject(s) - globular protein , contact order , folding (dsp implementation) , protein folding , biophysics , native state , chemistry , polypeptide chain , globular cluster , evolutionary biology , crystallography , biology , physics , biochemistry , amino acid , galaxy , electrical engineering , engineering , quantum mechanics
Folding rates (ln k f ) of globular proteins correlate with their biophysical properties, but relationship between ln k f and patterns of sequence evolution remains elusive. We introduce ‘relative co‐evolution order’ ( rCEO ) as length‐normalized average primary chain separation of co‐evolving pairs (CEPs), which negatively correlates with ln k f . In addition to pairs in native 3D contact, indirectly connected and structurally remote CEPs probably also play critical roles in protein folding. Correlation between rCEO and ln k f is stronger in multi‐state proteins than two‐state proteins, contrasting the case of contact order ( co ), where stronger correlation is found in two‐state proteins. Finally, rCEO , co and ln k f are fitted into a 3D linear correlation.