Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.493599
Title: A comparison of the thermodynamics of hydrophobic and hydrophilic ligand-protein interactions
Author: Syme, Neil Robert
Awarding Body: University of Leeds
Current Institution: University of Leeds
Date of Award: 2008
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Abstract:
A better understanding of the factors that determine the affinity for ligand-protein interactions remains an important goal in biophysical and medicinal chemistry. Three-dimensional structures reveal a significant amount of information about a complex, but these static structures only represent the lowest energy conformation. Molecules are mobile. Their conformational changes and internal dynamics are an integral part of their function. Linking these motions with architecture is not always straightforward, but is essential to understanding what drives the association between two molecules.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.493599  DOI: Not available
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