Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan‐indole‐HN sites
- 26 February 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 445 (2-3) , 361-365
- https://doi.org/10.1016/s0014-5793(99)00042-3
Abstract
Hydrogen/deuterium (H/D) exchange measurements in low and moderate concentrations of GuHCl were conducted on the side chain HN atoms of the seven tryptophans of pseudo wild-type human carbonic anhydrase II. Tryptophans 5, 16 and 245, situated in or close to the N-terminal domain were found to have little protection against exchange. The H/D exchange results for Trp-123, Trp-192 and Trp-209 showed that a previously identified molten globule and the native state gave a similar protection against exchange. Global unfolding of the protein is necessary for the efficient exchange at Trp-97, which is located in the central part of the β-sheet.Keywords
This publication has 26 references indexed in Scilit:
- Formation of Local Native-like Tertiary Structures in the Slow Refolding Reaction of Human Carbonic Anhydrase II as Monitored by Circular Dichroism on Tryptophan MutantsBiochemistry, 1997
- Alternative conformations of amyloidogenic proteins govern their behaviorCurrent Opinion in Structural Biology, 1996
- Mapping the Folding Intermediate of Human Carbonic Anhydrase II. Probing Substructure by Chemical Reactivity and Spin and Fluorescence Labeling of Engineered Cysteine ResiduesBiochemistry, 1995
- Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonanceBiophysical Journal, 1995
- Contribution of Individual Tryptophan Residues to the Fluorescence Spectrum of Native and Denatured Forms of Human Carbonic Anhydrase IIBiochemistry, 1995
- Assignment of the Contribution of the Tryptophan Residues to the Circular Dichroism Spectrum of Human Carbonic Anhydrase IIBiochemistry, 1994
- Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of sulfhydryl groups introduced by site-directed mutagenesisBiochemistry, 1993
- Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependenceBiochemistry, 1991
- Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chlorideBiochemistry, 1982
- Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase BBiochemistry, 1980