Multinuclear magnetic resonance studies of Escherichia coli adenylate kinase in free and bound forms . Resonance assignment, secondary structure and ligand binding
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چکیده
منابع مشابه
Proton-nuclear magnetic resonance studies of the aromatic spin systems of Escherichia coli adenylate kinase.
Escherichia coli adenylate kinase has a very well resolved proton nuclear magnetic resonance spectrum in the region containing signals from aromatic amino acid side-chains. We found that the protein is structurally stable over a wide pH range and renatures spontaneously after acidic as well as basic denaturation. Only one out of the three histidyl imidazole rings titrates on changing the pH and...
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The 'H NMR spectrum of the 65-residue protein hirudin is assigned in a sequential manner by using a combination of two-dimensional nuclear magnetic resonance techniques to demonstrate through-bond and through-space (<5-i() connectivities. The secondary structure of hirudin is deduced from a qualitative interpretation of the nuclear Overhauser effects involving the backbone NH, CaH, and CPH prot...
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With the use of appropriately chosen solvent pairs it is demonstrated that solvent dependence of peptide carbonyl carbon resonances can be correlated with polypeptide secondary structure. Solvent titrations show the peptide carbonyl which is intramolecularly hydrogen bonded to exhibit less chemical shift on going from a dimethylsulfoxide solution to a solution containing a solvent which is a go...
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Magnetic resonance and relative enzymatic velocity studies with the use of the paramagnetic manganese ion were carried out on creatine kinase inactivated by the specific -SH reagents iodoacetic acid and dinitrofluorobenzene and by the nonspecific reagents urea and decyl sulfate. Modification of creatine kinase at the two essential --SH groups by iodoacetic acid or dinitrofluorobenzene affected ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1999
ISSN: 0014-2956,1432-1033
DOI: 10.1046/j.1432-1327.1999.00633.x