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Branching in the sequential folding pathway of cytochrome c
Author(s) -
Krishna Mallela M.G.,
Maity Haripada,
Rumbley Jon N.,
Englander S. Walter
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072922307
Subject(s) - branching (polymer chemistry) , folding (dsp implementation) , computational biology , chemistry , biophysics , biology , stereochemistry , engineering , organic chemistry , electrical engineering
Previous results indicate that the folding pathways of cytochrome c and other proteins progressively build the target native protein in a predetermined stepwise manner by the sequential formation and association of native‐like foldon units. The present work used native state hydrogen exchange methods to investigate a structural anomaly in cytochrome c results that suggested the concerted folding of two segments that have little structural relationship in the native protein. The results show that the two segments, an 18‐residue omega loop and a 10‐residue helix, are able to unfold and refold independently, which allows a branch point in the folding pathway. The pathway that emerges assembles native‐like foldon units in a linear sequential manner when prior native‐like structure can template a single subsequent foldon, and optional pathway branching is seen when prior structure is able to support the folding of two different foldons.