Proton nuclear magnetic resonance study of the histidine residues of the Escherichia coli adenosine cyclic 3',5'-phosphate receptor protein. pH titration behavior, deuterium exchange, and partial assignments
- 17 August 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (17) , 4048-4053
- https://doi.org/10.1021/bi00260a021
Abstract
No abstract availableThis publication has 5 references indexed in Scilit:
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- Isolation and characterization of the amino and carboxyl proximal fragments of the adenosine cyclic 3',5'-phosphate receptor protein of Escherichia coliBiochemistry, 1981
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- The kinetics and thermodynamics of the reaction of solid-state fully reduced membrane-bound cytochrome oxidase with carbon monoxide as studied by dual-wavelength multichannel spectroscopy and flash photolysisBiochemical Journal, 1978
- Production and properties of the α core derived from the cyclic adenosine monophosphate receptor protein of Escherichia coliBiochemistry, 1978