Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
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.
Jonasson
P
P
Department of Biochemistry, Umeå University, Sweden.
Kjellsson
A
A
Sethson
I
I
Jonsson
B H
BH
D002256:Carbonic Anhydrases / Q000737:chemistry*; D003903:Deuterium / Q000737:chemistry; D006801:Humans; D006859:Hydrogen; D007211:Indoles / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D014364:Tryptophan / Q000737:chemistry
D007211:Indoles; D006859:Hydrogen; C030374:indole; D014364:Tryptophan; D003903:Deuterium; D002256:Carbonic Anhydrases