Conformation and Interaction with Small Molecules of Cyclic Hexa-Peptides as Studied by Nuclear Magnetic Resonance Spectroscopy and Circular Dichroism
Enzymes and other biopolymers exhibit many exquisite functions, resulting from the cooperation of several elemental factors. The most important factor must be the selection and the recognition of a substrate by proteins. In enzyme reactions, this is important as the pre-rate-determining step in the catalysis as well as this is related to the allosteric control of the action. It is also important in the hormone — receptor interaction. Therefore, the substrate-recognition could be the basis of all life phenomena. To investigate the substrate-recognition, cyclic peptides are very useful protein models. Cyclic peptides have been shown to bind metal cations and ammonium compounds by the intramolecular cooperation of carbonyl groups(1). Furthermore, they are so suitable for the detailed analysis of conformation by spectroscopy (2) that we can discuss the function of cyclic peptides in relation to their conformational properties.
KeywordsEthyl Benzene Chloroform Catalysis Phenyl
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- 2.D.W. Urry and M. Ohnishi, “Spectroscopic Approaches to Biomolecular Conformation,” Amer. Med. Ass., Chicago, Ill., Ch. VII, pp. 263 – 303.Google Scholar