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 Lettjournal_title
FEBS lettersauthors
Jonasson P,Kjellsson A,Sethson I,Jonsson BHdoi
10.1016/s0014-5793(99)00042-3keywords:
subject
Has Abstractpub_date
1999-02-26 00:00:00pages
361-5issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)00042-3journal_volume
445pub_type
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