Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500995
Title: A study of the folding and topology of VDAC isoforms from Saccharomyces cerevisiae
Author: McDonald, Beth
Awarding Body: University of Newcastle Upon Tyne
Current Institution: University of Newcastle upon Tyne
Date of Award: 2008
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Abstract:
VDAC (voltage-dependent anion channel) is a eukaryotic pore-forming β-barrel protein. It is found in abundance in the outer membrane of mitochondria, and is involved in mitochondrial homeostasis and function. A plethora of evidence also suggests the involvement of VDAC in programmed cell death, often referred to as apoptosis. However, despite its importance, the exact molecular structure of VDAC remains unsolved, with only 2D crystals of low resolution being available. Published topology models based upon experimental data suggest a β-barrel conformation comprising an N-terminal a-helix and between 12 and 19 membrane spanning p-sheets. This thesis describes the study of the topology of VDAC 1 from Saccharomyces cerevisiae with an aim to resolve the many contradictions between published topology models.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.500995  DOI: Not available
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