NMR paper Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e

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[NMR paper] Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e

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08-21-2010, 04:03 PM

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Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e

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

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

FEBS Lett. 1999 Feb 26;445(2-3):361-5

Authors: Jonasson P, Kjellsson A, Sethson I, Jonsson BH

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.

PMID: 10094490 [PubMed - indexed for MEDLINE]

Source: PubMed

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