Complexes of Ribonuclease A with 2'-Deoxy-2'-Fluororibose Substrate Analogues Studied by Nuclear Magnetic Resonance
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12350.x/fullpdf
Reference22 articles.
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4. NUCLEAR MAGNETIC RESONANCE STUDIES OF A RIBONUCLEASE-DINUCLEOSIDE PHOSPHONATE COMPLEX AND THEIR IMPLICATIONS FOR THE MECHANISM OF THE ENZYME
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1. Studies on polypeptides XLI1H NMR studies of non-covalent, semi-synthetic ribonuclease A analogues in which histidine-119 has been replaced by L-homohistidine, Nτ-methyl-L-histidine, Nπ-methyl-L-histidine and 3-(3-pyrazolyl)-L-alanine, respectively;Recueil des Travaux Chimiques des Pays-Bas;2010-09-02
2. 1H-n.m.r. studies on the specificity of the interaction between bovine pancreatic ribonuclease A and dideoxynucleoside monophosphates;International Journal of Peptide and Protein Research;2009-01-12
3. Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases;FEBS Letters;1997-03-10
4. A history of biological applications of NMR spectroscopy;Progress in Nuclear Magnetic Resonance Spectroscopy;1995-12
5. The occupancy of two distinct conformations by active-site histidine-119 in crystals of ribonuclease is modulated by pH;FEBS Letters;1994-07-25
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