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Secondary structure of globular proteins at the early and the final stages in protein folding
Author(s) -
Kuwajima Kunihiro,
Semisotnov Gennady V,
Finkelstein Alexei V,
Sugai Shintaro,
Ptitsyn Oleg B
Publication year - 1993
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 - 10.1016/0014-5793(93)80691-m
Subject(s) - globular protein , protein secondary structure , circular dichroism , folding (dsp implementation) , protein folding , chemistry , protein structure , biophysics , crystallography , biochemistry , biology , electrical engineering , engineering
The ellipticities for an early transient intermediate in refolding observed by kinetic circular dichroism measurements at 220–225 nm for 14 different proteins are summarized, and the ellipticity values are compared with those for the final native proteins and also with the ellipticities expected from a physical theory of protein and polypeptide secondary structure. The results show that a substantial part of the protein secondary structure is in general formed in the earliest detectable intermediate in refolding and that the ellipticities in both the native and the intermediate states are consistent with the physical theory of protein secondary structure.