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University of Illinois at Urbana-Champaign
Structural Studies of Lipid-Bound Apolipoprotein A-I and Nanodisc-Embedded Cyp3A4 by SSNMR
Abstract
dc:descriptionMembrane proteins constitute more than half of all drug targets in the pharmaceutical industry today, which is not surprising given that a third of human genome codes for membrane proteins, and that they perform a large number and variety of cellular functions. However, membrane proteins to date have been structurally under-characterized as a consequence of the technical difficulties encountered by solution NMR and x-ray crystallography in solving atomic-resolution structures of these proteins. Work presented here focused on development of the Nanodisc platform for structural studies of membrane proteins using solid-state NMR (SSNMR).
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biophysics and Computational Biology
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2014
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Kijac, Aleksandra Z.
- Contributors dc:contributor
-
- Sligar, Stephen G.
- Rienstra, Chad M.
Subjects
dc:subject × 2Identifiers
dc:identifier.*- Identifier
- (UMI)AAI3395572
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/72402