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19F NMR evidence for interactions between the c‐AMP binding sites on the c‐AMP receptor protein from E. coli
Author(s) -
Hinds Mark G.,
King Rodney W.,
Feeney James
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80569-o
Subject(s) - chemistry , dissociation constant , dimer , titration , dissociation (chemistry) , chemical shift , fluorine 19 nmr , receptor , molecule , binding site , stereochemistry , proton nmr , nuclear magnetic resonance spectroscopy , crystallography , biochemistry , inorganic chemistry , organic chemistry
The 19 F NMR spectra of 3‐fluorotyrosine containing c‐AMP receptor protein (CRP) from E. coli have been recorded in the presence of increasing amounts of c‐AMP. One of the signals (from Tyr B) shifts upfield by 0.6 ppm in the presence of excess c‐AMP and shows both slow and fast exchange behaviour during the titration. This is evidence for interactions between the two c‐AMP binding sites on the CRP dimer leading to different dissociation rate constants (≤ 75 s −1 ; ≥ 350 s −1 ) for complexes containing one and two c‐AMP molecules.