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Title: High resolution nuclear magnetic resonance studies of biologically significant molecules
Author: Leworthy, David Paul
Awarding Body: University of London
Current Institution: Imperial College London
Date of Award: 1972
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Fluorine magnetic resonance has been used to study the interaction of N-trifluoroacetyl-X-phenyl alanines with the enzyme α-chymotrypsin with varying pH and buffer systems. The aromatic and aliphatic binding sites of the enzyme were studied simultaneously using N-trifluoroacetylfluoro phenyl alanines as the enzyme inhibitors, the aromatic fluorine spectra being simplified by heteronuclear decoupling. The specific nature of the interaction between α-chymotrypsin and the N-trifluoroacetyl-X-phenyl alanines was demonstrated using N-trans cinnamoyl imidazole as a competitive inhibitor. A new method for the estimation of α-chymotrypsin is suggested. The inherent limitations of n.m.r. for studying these types of interaction are discussed.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available