Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar

FEBS Letters

Lubienski, Michael J.¹  Jones, David N.M.¹  Fersht, Alan R.¹  Bycroft, Mark¹ 

[1] MRC Unit for Protein Function and Design, Cambridge Centre for Protein Engineering, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK

关键词: Sequence-specific NMR assignment;    Barnase;    Barstar;    NMR;    nuclear magnetic resonance;    2D;    two-dimen-sional;    3D;    three-dimensional;    NOE;    nuclear Overhauser enhance-ment;    NOESY;    two-dimensional NOE-correlated spectroscopy;    TOCSY;    total correlated spectroscopy;    HMQC;    1H-detected hetero-nuclear multiple quantum correlation;    HSQC;    2D 1H-detected hetero-nuclear single quantum correlation;   

DOI  :  10.1016/0014-5793(93)80489-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Barstar, a polypeptide inhibitor of ribonucleases, has been studied by 2D and 3D NMR techniques using uniformly ¹⁵N-labeled protein. Backbone (¹⁵NH-C_αH-C_βH) resonances were assigned for all but 5 of the 89 residues. Dihedral angle and deuterium exchange studies were used in conjunction with medium range inter-proton NOEs to characterize the secondary structure of barstar. The protein is composed of four α-helices and three short stretches of extended strand. By further analysis of the NOE data three of the helices were found to be parallel to each other with the single disulphide bond linking the second and fourth helices at their C-terminal ends.

【 授权许可】

Unknown