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Direct detection of lysine side chain NH3+ in protein-heparin complexes using NMR spectroscopy.
Sepuru, Krishna Mohan; Iwahara, Junji; Rajarathnam, Krishna.
Afiliação
  • Sepuru KM; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA. krrajara@utmb.edu and Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, USA.
  • Iwahara J; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA. krrajara@utmb.edu and Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, USA.
  • Rajarathnam K; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA. krrajara@utmb.edu and Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, USA.
Analyst ; 143(3): 635-638, 2018 Feb 07.
Article em En | MEDLINE | ID: mdl-29292440
ABSTRACT
Two NMR observables, the NζH3+ peak in the HISQC spectrum and Nζ chemical shift difference between the free and heparin-bound forms, can identify binding-interface lysines in protein-heparin complexes. Unlike backbone chemical shifts, these direct probes are stringent and are less prone to either false positives or false negatives.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Heparina / Espectroscopia de Ressonância Magnética / Lisina Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Heparina / Espectroscopia de Ressonância Magnética / Lisina Idioma: En Ano de publicação: 2018 Tipo de documento: Article