Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan‐indole‐HN sites

FEBS Letters

Kjellsson, Annika¹  Sethson, Ingmar²  Jonasson, Per¹  Jonsson, Bengt-Harald¹ 

[1] Department of Biochemistry, Umeå University, S-901 87 Umeå, Sweden;Department of Organic Chemistry, Umeå University, S-901 87 Umeå, Sweden

关键词: Protein folding;    Hydrogen/Deuterium exchange;    NMR;    Folding intermediate;    Carbonic anhydrase;    Molten globule;    GuHCl;    guanidine hydrochloride;    HCAIIpwt;    pseudo wild-type human carbonic anhydrase II;    H/D exchange;    hydrogen/deuterium exchange;   

DOI  :  10.1016/S0014-5793(99)00042-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown