Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.633148
Title: The design, synthesis, characterisation and understanding of highly a-helical peptides
Author: Baker, Emily Grace
Awarding Body: University of Bristol
Current Institution: University of Bristol
Date of Award: 2013
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Abstract:
Despite considerable effort in understanding electrostatic interactions in proteins, namely a-helices, the literature contains many conflicting descriptions. The loss of conformational entropy associated with helix ~ coil equilibrium is balanced, in part, by electrostatic contributions to enthalpy such as backbone a-helical H-bonds; i->i+3 and i->i+4 side chain H-bonds and salt bridges; side chain-main chain H-bonds and salt bridges, and through-space electrostatic interactions of side chains with the helix-macrodipole. Peptide bonds are 'micro' dipoles which are aligned (97%) with the helix axis resulting in the so-called helix-macrodipole and local dipole effects result at the termini due to dissatisfied H-bond donor and acceptors there.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.633148  DOI: Not available
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