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Remarkably slow folding of a small protein
Author(s) -
Aronsson Göran,
Brorsson Ann-Christin,
Sahlman Lena,
Jonsson Bengt-Harald
Publication year - 1997
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/s0014-5793(97)00730-8
Subject(s) - protein folding , guanidine , chemistry , folding (dsp implementation) , peptide bond , population , phi value analysis , denaturation (fissile materials) , amino acid , proline , unfolded protein response , native state , peptide , biophysics , crystallography , biochemistry , biology , endoplasmic reticulum , demography , sociology , electrical engineering , nuclear chemistry , engineering
Equilibrium denaturation of the 72 amino acid α/β‐protein MerP, by acid, guanidine hydrochloride, or temperature, is fully reversible and follows a two‐state model in which only the native and unfolded states are populated. A cis ‐ trans equilibrium around a proline peptide bond causes a heterogeneity of the unfolded state and gives rise to a slow‐ and a fast folding population. With a rate constant of 1.2 s −1 for the major fast folding population, which has none of the common intrinsically slow steps, MerP is the slowest folding protein of this small size yet reported.