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Folding of beta‐sandwich proteins: Three‐state transition of a fibronectin type III module
Author(s) -
Cota Ernesto,
Clarke Jane
Publication year - 2000
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.9.1.112
Subject(s) - guanidine , chemistry , equilibrium unfolding , phi value analysis , protein folding , folding (dsp implementation) , kinetics , biophysics , native state , fibronectin , crystallography , biochemistry , biology , physics , quantum mechanics , electrical engineering , extracellular matrix , engineering
An analysis of the folding of the 94 residue tenth fibronectin type III (fnIII) domain of human fibronectin (FNfn10) is presented. Use of guanidine isothiocyanate as a denaturant allows us to obtain equilibrium and kinetic data across a broad range of denaturant concentrations that are unavailable in guanidine hydrochloride. Equilibrium unfolding experiments show that FNfn10 is significantly more stable than has been reported previously. Comparison of equilibrium and kinetic parameters reveals the presence of an intermediate that accumulates at low denaturant concentrations. This is the first demonstration of three‐state folding kinetics for a fnIII domain. We have previously shown that a homologous domain from human tenascin (TNfn3) folds by a two‐state mechanism, but this does not necessarily indicate that the two proteins fold by different folding pathways.