Literature DB >> 1901804

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

D M Baldisseri1, J G Pelton, S W Sparks, D A Torchia.   

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.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 1901804     DOI: 10.1016/0014-5793(91)80352-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  Mapping the sevoflurane-binding sites of calmodulin.

Authors:  Ulrika Brath; Kelvin Lau; Filip Van Petegem; Máté Erdélyi
Journal:  Pharmacol Res Perspect       Date:  2014-02-12
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.