[NMR paper] NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
Chemistry. 2014 Dec 17;
Authors: Shenderovich IG, Lesnichin SB, Tu C, Silverman DN, Tolstoy PM, Denisov GS, Limbach H
Abstract
By using a combination of liquid and solid-state NMR spectroscopy,...
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12-19-2014 11:42 AM
[NMR paper] NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
Adv Protein Chem Struct Biol. 2013;93:37-80
Authors: Zandarashvili L, Esadze A, Iwahara J
Abstract
Hydrogen bonds and ion pairs involving side chains play vital roles in protein functions such as...
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The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
Abstract The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal...
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Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-St
Oxidation of Histidine Residues in Copper-Zinc Superoxide Dismutase by Bicarbonate-Stimulated Peroxidase and Thiol Oxidase Activities: Pulse EPR and NMR Studies
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1010305/aop/images/medium/bi-2010-010305_0006.gif
Biochemistry
DOI: 10.1021/bi1010305
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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11-24-2010 07:12 AM
[NMR paper] pH-induced structural changes in human serum apotransferrin. pKa values of histidine
pH-induced structural changes in human serum apotransferrin. pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles pH-induced structural changes in human serum apotransferrin. pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy.
Eur J Biochem. 1994 Mar 15;220(3):781-7
Authors: Kubal G, Sadler PJ, Tucker A
...
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08-22-2010 03:33 AM
[NMR paper] Structural consequences of histidine phosphorylation: NMR characterization of the pho
Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli.
Related Articles Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli.
Biochemistry. 1994 Dec 27;33(51):15271-82
Authors: Rajagopal P, Waygood EB, Klevit RE
The bacterial phosphoenolpyruvate:sugar phosphotransferase system involves a series...
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08-22-2010 03:29 AM
[NMR paper] Are the histidine residues of glutathione S-transferase important in catalysis? An as
Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
Related Articles Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
J Biol Chem. 1991 Oct 15;266(29):19475-9
Authors: Zhang PH, Graminski GF, Armstrong RN
To test the proposition that a histidine residue is essential in the catalytic mechanism of glutathione S-transferase, rat liver isoenzyme 3-3...
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08-21-2010 11:12 PM
[NMR paper] Are the histidine residues of glutathione S-transferase important in catalysis? An as
Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
Related Articles Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.
J Biol Chem. 1991 Oct 15;266(29):19475-9
Authors: Zhang PH, Graminski GF, Armstrong RN
To test the proposition that a histidine residue is essential in the catalytic mechanism of glutathione S-transferase, rat liver isoenzyme 3-3...
N–H···N Hydrogen Bonds Involving Histidine Imidazole Nitrogen Atoms: A New Structural Role for Histidine Residues in Proteins
Linear Mode
