Structure of the Pressure-Assisted Cold Denatured State of Ubiquitin
- 18 September 1997
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 238 (2) , 289-291
- https://doi.org/10.1006/bbrc.1997.7308
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labellingFolding and Design, 1996
- Hydrogen-exchange kinetics in the cold denatured state of ribonuclease ABiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
- Structure of a Hydrophobically Collapsed Intermediate on the Conformational Folding Pathway of Ribonuclease A Probed by Hydrogen−Deuterium ExchangeBiochemistry, 1996
- Determination of the Activation Volume of the Uncatalyzed Hydrogen Exchange Reaction between N-Methylacetamide and WaterJournal of the American Chemical Society, 1996
- NMR Study of the Cold, Heat, and Pressure Unfolding of Ribonuclease ABiochemistry, 1995
- Energetics of Protein StructurePublished by Elsevier ,1995
- High-Resolution NMR Spectroscopy at High PressuresJournal of Magnetic Resonance, Series B, 1993
- Primary structure effects on peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Hydrogen exchange in thermally denatured ribonucleaseBiochemistry, 1991
- Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOHJournal of Solution Chemistry, 1987