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Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan‐indole‐H N sites
Author(s) -
Jonasson Per,
Kjellsson Annika,
Sethson Ingmar,
Jonsson Bengt-Harald
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00042-3
Subject(s) - hydrogen–deuterium exchange , chemistry , tryptophan , deuterium , carbonic anhydrase , indole test , hydrogen , stereochemistry , biochemistry , enzyme , amino acid , organic chemistry , physics , quantum mechanics
Hydrogen/deuterium (H/D) exchange measurements in low and moderate concentrations of GuHCl were conducted on the side chain H N 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.