摘要
描述了从虎纹捕鸟蛛毒液分离的凝集素ＳＨＬ－Ｉ的核磁共振氢谱谱峰的完全归属。通过分析二维ＤＱＦ－ＣＯＳＹ，ＣＯＳＹ，ＴＯＣＳＹ和ＮＯＥＳＹ谱，鉴别出全部３２个氨基酸残基自旋体系。然后由ＣＯＳＹ，ＮＯＥＳＹ谱指纹区的ｄαＮ连系推测出序列专一归属，并得到了ＴＯＣＳＹ和ＮＯＥＳＹ谱中ｄαＮ，ｄＮＮ的验证。从而明确分辨了除Ｃｙｓ２外所有主链质子和大于９６％的侧链质子。这一结果为最终确定ＳＨＬ－Ｉ的溶液构象奠定了基础。
The complete sequence-specific assignments of proton resonances in the 1H-NMR spectra of SHL-I, a lectin isolated from the Chinese bird spider Selenocosmia huwena, is described. By using two-dimensional DQF-COSY, COSY, TOCSY and NOESY spectroscopies, all the backbone protons except Cys2 and >96% of the side-chain protons are identified without ambiguity based on intra- and inter-molecular connectivities. These studies provide a basis for further determination of the solution conformation of SHL-I.
出处
《生物物理学报》
CAS
CSCD
北大核心
1999年第2期269-276,共8页
Acta Biophysica Sinica
