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15 N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: sequence specific assignments of the imide 15 N resonances of the proline residues and the interaction with human immunoglobulin G
Author(s) -
Torigoe Hidetaka,
Shimada Ichio,
Waelchli Markus,
Saito Akiko,
Sato Moriyuki,
Arata Yoji
Publication year - 1990
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(90)81147-g
Subject(s) - nuclear magnetic resonance , sequence (biology) , chemistry , proline , nuclear magnetic resonance spectroscopy , resonance (particle physics) , domain (mathematical analysis) , physics , crystallography , amino acid , atomic physics , biochemistry , mathematics , mathematical analysis
15 N nuclear magnetic resonance (NMR) studies of the B domain (FB) of Staphylococcus protein A, which is uniformly labeled with 15 N, are reported. The α CH(i)‐ 15 N(i) connectivity in the 1 H‐ 15 N HMBC spectrum and the 13 C(i‐1)‐ 15 N(i) spin coupling in the 15 N spectrum of a 13 C‐, 15 N‐doubly labeled FB were used to establish the assignments of the imide 15 N resonances for all the three Pro residues that exist in FB. Addition of human IgG caused a significant downfield shift of the Pro‐39 resonance. This result is quite consistent with our previous suggestion that a significant conformation change is induced in the Ser‐42‐Ala‐55 helical region of FB when it is bound to human IgG.