Binding modes of inhibitors to ribonuclease T1 as studied by nuclear magnetic resonance
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00325a031
Reference38 articles.
1. Proton magnetic resonance studies of ribonuclease T1. Assignment of histidine-40 peak and analysis of the active site
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3. Binding of purine nucleoside monophosphates by ribonuclease T1 a model system for protein nucleic acid interaction
4. Nucleoside conformations
5. Ribonucleases in Taka-Diastase: Properties, Chemical Nature, and Applications
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1. Professor Tatsuo Miyazawa: from molecular structure to biological function;Journal of Biochemistry;2010-12-01
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. Initial state of an enzymic reaction. Theoretical prediction of complex formation in the active site of RNase T1;Journal of the American Chemical Society;1995-10
4. pH Dependence of binding reactions from free energy simulations and macroscopic continuum electrostatic calculations: Application to 2′GMP/3′GMP binding to ribonuclease T1 and implications for catalysis;Journal of Molecular Biology;1995-04
5. Crystal structure of RNase T1 complexed with the product nucleotide 3‘-GMP. Structural evidence for direct interaction of histidine 40 and glutamic acid 58 with the 2‘-hydroxyl group of the ribose;Journal of Biological Chemistry;1994-07
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