Keller R M, Baumann R, Hunziker-Kwik E H, Joubert F J, Wüthrich K
J Mol Biol. 1983 Feb 5;163(4):623-46. doi: 10.1016/0022-2836(83)90115-8.
The assignment of the 1H nuclear magnetic resonance (n.m.r.) spectrum of the trypsin inhibitor homologue K from the venom of Dendroaspis polylepis polylepis is described and documented. The assignments are based entirely on the amino acid sequence and on 2-dimensional n.m.r. experiments at 360 and 500 M Hz. Individual assignments were obtained for the backbone and C beta protons of all 57 residues of the inhibitor homologue K, with the exceptions of the N-terminal amino group, the amide protons of Arg16, Gly37 and Gly40 and the C beta protons of Arg16 and Pro19. The assignments for the non-labile protons of the amino acid side-chains are complete, with the exception of Gln29, Glu49 and all the proline, lysine and arginine residues. For Asn and Trp the labile side-chain protons have also been assigned. The chemical shifts for the assigned resonances are listed for an aqueous solution at 50 degrees C and pH 3.4.
描述并记录了来自多鳞树眼镜蛇毒液的胰蛋白酶抑制剂同系物K的1H核磁共振（n.m.r.）谱的归属。这些归属完全基于氨基酸序列以及在360和500兆赫兹下进行的二维n.m.r.实验。除了N端氨基、Arg16、Gly37和Gly40的酰胺质子以及Arg16和Pro19的Cβ质子外，抑制剂同系物K的所有57个残基的主链和Cβ质子都获得了各自的归属。氨基酸侧链的非不稳定质子的归属已完成，但Gln29、Glu49以及所有脯氨酸、赖氨酸和精氨酸残基除外。对于Asn和Trp，其不稳定的侧链质子也已被归属。列出了在50℃和pH 3.4的水溶液中已归属共振峰的化学位移。
