Protein stability parameters measured by hydrogen exchange
- 1 September 1994
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 20 (1), 4-14
- https://doi.org/10.1002/prot.340200103
Abstract
The hydrogen exchange (HX) rates of the slowest peptide group NH hydrogens in oxidized cytochrome c (equine) are controlled by the transient global unfolding equilibrium. These rates can be measured by one‐dimensional nuclear magnetic resonance and used to determine the thermodynamic parameters of global unfolding at mild solution conditions well below the melting transition. The free energy for global unfolding measured by hydrogen exchange can differ from values found by standard denaturation methods, most notably due to the slow cis‐trans isomerization of the prolyl peptide bond. This difference can be quantitatively calculated from basic principles. Even with these corrections, HX experiments at low denaturant concentration measure a free energy of protein stability that rises above the usual linear extrapolation from denaturation data, as predicted by the denaturant binding model of Tanford.This publication has 40 references indexed in Scilit:
- Structural Characterization of the FK506 Binding Protein Unfolded in Urea and Guanidine HydrochlorideJournal of Molecular Biology, 1994
- Formation of a Hydrophobic Cluster in Denatured Bovine Pancreatic Trypsin InhibitorJournal of Molecular Biology, 1994
- Protein interactions with urea and guanidinium chlorideJournal of Molecular Biology, 1992
- Stable submolecular folding units in a non-compact form of cytochrome cJournal of Molecular Biology, 1991
- Comparison of amide proton exchange in reduced and oxidizedRhodobacter capsulatus cytochrome c2: A1H−15N NMR studyJournal of Biomolecular NMR, 1991
- THE THERMODYNAMIC STABILITY OF PROTEINSAnnual Review of Biophysics and Biophysical Chemistry, 1987
- Mechanisms of hydrogen exchange in proteins from NMR studies of individual tryptophan indole amine hydrogens in lysozymeBiochemistry, 1982
- A novel application of nuclear Overhauser enhancement (NOE) in proteins: Analysis of correlated events in the exchange of internal labile protonsBiochemical and Biophysical Research Communications, 1980
- Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteinsJournal of Molecular Biology, 1979
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974