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Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH-COSY and HCCH-TOCSY 3D NMR spectroscopy.

作者信息

Baldisseri D M, Pelton J G, Sparks S W, Torchia D A

机构信息

Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.

出版信息

FEBS Lett. 1991 Apr 9;281(1-2):33-8. doi: 10.1016/0014-5793(91)80352-4.

Abstract

Complete proton and carbon sidechain assignments are reported for 22 lysine and 11 leucine residues in staphylococcal nuclease, an enzyme with 149 residues. These assignments are readily obtained in a direct manner from the correlations observed in the 3D HCCH-COSY and HCCH-TOCSY spectra and the known protein backbone assignments. These assignments open the way to detailed studies of the sidechain structure and dynamics at the active site, in the hydrophobic core and on the surface of the protein.

摘要

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