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Proton NMR resonance assignments and surface accessibility of tryptophan residues of a dimeric phospholipase A 2 from Trimeresurus flavoviridis
Author(s) -
Endo Toshiya,
Oya Masanao,
Kaptein Robert,
Vuister Geerten W.,
Kihara Hiroshi,
Mohri Noriko,
Tanaka Shuji,
Ohno Motonori
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80641-0
Subject(s) - tryptophan , chemistry , dimer , indole test , phospholipase a2 , stereochemistry , phospholipase a , proton nmr , crystallography , enzyme , biochemistry , amino acid , organic chemistry
Proton NMR spectra of a dimeric phospholipase A 2 from Trimeresurus flavoviridis have been recorded. N‐1 proton resonances of the tryptophan indole rings have been detected and assigned to specific positions, Trp‐3/Trp‐30, Trp‐68 and Trp‐108, by comparing the spectra of the enzyme derivatives with tryptophans oxidized to differing extents. Photo‐CIDNP experiments have revealed that Trp‐68 and Trp‐108 are exposed while Trp‐3 and Trp‐30 are buried in the molecule. This is consistent with the X‐ray crystal structure of a homologous phospholipase A 2 from Crotalus atrox where residues 3 and 30 are located at a dimer interface, but inconsistent with the results of stepwise oxidation of tryptophan residues.