Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 38, Pages 11157-11161Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201505416
Keywords
high-pressure NMR spectroscopy; kinetics; protein folding; proteins; relaxation dispersion
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Funding
- Intramural Program of NIDDK, NIH
- AIDS Targeted Antiviral Program of Office of Director of NIH
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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 N-15-relaxation dispersion NMR from 1 to 2500 bar. Changes in partial molar volumes (Delta V) and isothermal compressibilities (Delta K-T) 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 mLmol(-1) and 40 mu Lmol(-1) bar(-1), respectively, higher than those of the unfolded ensemble. Of particular interest are the findings related to the energetic and volumetric properties of the on-pathway folding intermediate. While the latter is energetically close to the unfolded state, its volumetric properties are similar to those of the folded protein. The compressibility of the intermediate is larger than that of the folded state reflecting the less rigid nature of the former relative to the latter.
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