Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.

Abstract:

:Hydrogen/deuterium (H/D) exchange measurements in low and moderate concentrations of GuHCI 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 beta-sheet.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Jonasson P,Kjellsson A,Sethson I,Jonsson BH

doi

10.1016/s0014-5793(99)00042-3

keywords:

subject

Has Abstract

pub_date

1999-02-26 00:00:00

pages

361-5

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)00042-3

journal_volume

445

pub_type

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