Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins

Lovatt, Michelle (1997) Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins. PhD thesis, University of Glasgow.

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Abstract

Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins The interaction of a range of cyclodextrins with amino acids, both free and in proteins has been investigated using sensitive microcalorimetry and spectroscopic techniques. With a view towards possible applications in chiral separation technologies, isothermal titration calorimetry (ITC) was used to study the complexation of cyclodextrins with the enantiomers of ?-amino acids by competition with p-nitrophenolate or p-aminobenzoic acid under various pH conditions. It was found the majority of amino acids showed no complexation. However, complexes of alpha-cyclodextrin with phenylalanine, and tryptophan demonstrated small, but distinct, differences in dissociation constants for their separate enantiomers. Thermodynamic parameters (Kd, DeltaH

Item Type: Thesis (PhD)
Qualification Level: Doctoral
Additional Information: Adviser: Alan Cooper
Keywords: Biochemistry
Date of Award: 1997
Depositing User: Enlighten Team
Unique ID: glathesis:1997-74847
Copyright: Copyright of this thesis is held by the author.
Date Deposited: 27 Sep 2019 15:52
Last Modified: 27 Sep 2019 15:52
URI: http://theses.gla.ac.uk/id/eprint/74847

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