By Jo M. Holt, Michael L. Johnson, Gary K. Ackers
This quantity makes a speciality of equipment on the topic of allosteric enzymes and receptors, together with fluorescent proves, spectroscopic tools and quantitative research in addition to on cooperativity in protein folding. NMR and mass spectrometry tools are mentioned. *Allosteric Enzymes and Receptors *Cooperativity in Protein Folding and meeting
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Additional info for Energetics of Biological Macromolecules
If, for example, Hþ are bound preferentially by B, then the conversion of A to B will be promoted by low pH. Preferential Hþ binding by one of the states is determined by the pKa values of ionizable residues. The pKa values are influenced by a large variety of molecular factors, including interactions with other 2 M. Schaefer, H. W. van Vlijmen, and M. Karplus, Adv. Protein Chem. 51, 1 (1998).  electrostatic calculations with proteins 23 charges, with polar atoms, with polarizable atoms, and with water molecules.
Mol. Biol. 12, 88 (1965). See, for example, A. Fersht, ‘‘Structure and Mechanism in Protein Science,’’ p. 292. W. H. , New York, 1999. 18 allosteric enzymes and receptors  when O2 is bound, and this modified geometry is that existing in the R state. 26 However, and more importantly, widespread structural changes in the T to R transition seem possible. All noncovalent interactions within a receptor system that are coupled with negative cooperativity to ligand binding should loosen. To test this conclusion we determined27 by ESI-MS the change in dynamic behavior of the hemoglobin tetramer polypeptide backbone when it binds O2.
Positively Cooperative Binding Probed by NMR Spectroscopy Several peptide ligands, all containing the carboxyl group depicted at the lower right in Fig. 2, were separately bound to the antibiotics. In all cases, a downfield chemical shift of the antibiotic amide NH proton w2 was observed upon ligand binding. A larger limiting downfield shift of w2 indicates a shorter carboxylate to NH hydrogen bond. This hydrogen bond was found to decrease in length as the number of the adjacent hydrogen bonds that aid ligand binding was increased.