Ontology highlight
ABSTRACT:
SUBMITTER: Tugarinov V
PROVIDER: S-EPMC4692720 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Angewandte Chemie (International ed. in English) 20150901 38
The energetic and volumetric properties of a three-state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been investigated using pressure-dependent (15) N-relaxation dispersion NMR from 1 to 2500 bar. Changes in partial molar volumes (ΔV) and isothermal compressibilities (ΔκT ) between all the states along the folding pathway have been determined to reasonable accuracy. The partial volume and isothermal compressibility of the folded state are 100 mL mol( ...[more]