Site-specific observation of the conformational change of a protein with 15N-labeled Tyr residues using NMR
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. A 1H-15N NMR study of human c-Ha-ras protein: biosynthetic incorporation of 15N-labeled amino acids;Yamasaki;J. Biomol. NMR,1992
2. Amino acid-selective isotope labeling of proteins for nuclear magnetic resonance study: proteins secreted by Brevibacillus choshinensis;Tanio;Anal. Biochem.,2009
3. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution;Pervushin;Proc. Natl. Acad. Sci. U.S.A.,1997
4. Extension of transverse relaxation-optimized spectroscopy techniques to allosteric proteins: CO- and paramagnetic fluoromet-hemoglobin [β(15N-valine)];Nocek;Proc. Natl. Acad. Sci. U.S.A.,2000
5. High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy;Peterson;Biochemistry,2001
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