Proton magnetic resonance studies of ribonuclease T1. Assignment of histidine-40 peak and analysis of the active site
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference21 articles.
1. The Structure and Function of the Active Site of Ribonuclease T1
2. The Identification of a Glutamic Acid Residue as Part of the Active Site of Ribonuclease T1
3. Evidence for the Implication of Histidines-40 and -92 in the Active Site of Ribonuclease T1
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1. Hydration water molecules of nucleotide-free RNase T-1 studied by NMR spectroscopy in solution;Journal of Biomolecular NMR;1998
2. Limits of NMR structure determination using variable target function calculations: ribonuclease T 1 , a case study 1 1Edited by P. E. Wright;Journal of Molecular Biology;1997-02
3. Backbone dynamics of proteins studied by two-dimensional heteronuclear NMR spectroscopy and molecular dynamics simulations;International Journal of Quantum Chemistry;1996
4. Determination of the Backbone Mobility of Ribonuclease T1 and its 2′GMP Complex Using Molecular Dynamics Simulations and NMR Relaxation Data;Journal of Biomolecular Structure and Dynamics;1994-06
5. The complex between ribonuclease T1 and 3'GMP suggests geometry of enzymic reaction path. An X-ray study;European Journal of Biochemistry;1993-12
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