Nuclear magnetic resonance probes of membrane biophysics: Structure and dynamics

Persistent Link:
http://hdl.handle.net/10150/305369
Title:
Nuclear magnetic resonance probes of membrane biophysics: Structure and dynamics
Author:
Leftin, Avigdor
Issue Date:
2010
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
The phospholipid membrane is a self-assembled, dynamic molecular system that may exist alone in association with only water, or in complex systems comprised of multiple lipid types and proteins. In this dissertation the intra- and inter-molecular forces responsible for the atomistic, molecular and collective equilibrium structure and dynamics are studied by nuclear magnetic resonance spectroscopy (NMR). The multinuclear NMR measurements and various experimental techniques are able to provide data that enable the characterization of the hierarchical spatio-temporal organization of the phospholipid membrane. The experimental and theoretical studies conducted target membrane interactions ranging from model systems composed of only water and lipids, to multiple component domain forming membranes that are in association with peripheral and trans-membrane proteins. These measurements consisit of frequency spectrum lineshapes and nuclear-spin relaxation rates obtained using 2 H NMR, 13 C NMR, 31 P NMR and 1 H NMR. The changes of these experimental observables are interpreted within a statistical thermodynamic framework that allows the membrane structure, activation energies, and correlation times of motion to be determined. The cases presented demonstrate how fundamental principles of NMR spectroscopy may be applied to a host of membranes, leading to the biophysical characterization of membrane structure and dynamics.
Type:
text; Electronic Dissertation
Keywords:
Osmotic Stress; Peripheral Protein; Phospholipid Membrane; Solid-State Nuclear Magnetic Resonance; Chemistry; Biophysics; Nuclear Spin Relaxation
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Chemistry and Biochemistry
Degree Grantor:
University of Arizona
Advisor:
Brown, Michael
Committee Chair:
Brown, Michael

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleNuclear magnetic resonance probes of membrane biophysics: Structure and dynamicsen_US
dc.creatorLeftin, Avigdoren_US
dc.contributor.authorLeftin, Avigdoren_US
dc.date.issued2010-
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractThe phospholipid membrane is a self-assembled, dynamic molecular system that may exist alone in association with only water, or in complex systems comprised of multiple lipid types and proteins. In this dissertation the intra- and inter-molecular forces responsible for the atomistic, molecular and collective equilibrium structure and dynamics are studied by nuclear magnetic resonance spectroscopy (NMR). The multinuclear NMR measurements and various experimental techniques are able to provide data that enable the characterization of the hierarchical spatio-temporal organization of the phospholipid membrane. The experimental and theoretical studies conducted target membrane interactions ranging from model systems composed of only water and lipids, to multiple component domain forming membranes that are in association with peripheral and trans-membrane proteins. These measurements consisit of frequency spectrum lineshapes and nuclear-spin relaxation rates obtained using 2 H NMR, 13 C NMR, 31 P NMR and 1 H NMR. The changes of these experimental observables are interpreted within a statistical thermodynamic framework that allows the membrane structure, activation energies, and correlation times of motion to be determined. The cases presented demonstrate how fundamental principles of NMR spectroscopy may be applied to a host of membranes, leading to the biophysical characterization of membrane structure and dynamics.en_US
dc.typetexten_US
dc.typeElectronic Dissertationen_US
dc.subjectOsmotic Stressen_US
dc.subjectPeripheral Proteinen_US
dc.subjectPhospholipid Membraneen_US
dc.subjectSolid-State Nuclear Magnetic Resonanceen_US
dc.subjectChemistryen_US
dc.subjectBiophysicsen_US
dc.subjectNuclear Spin Relaxationen_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineChemistry and Biochemistryen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorBrown, Michaelen_US
dc.contributor.chairBrown, Michaelen_US
dc.contributor.committeememberSanov, Andreien_US
dc.contributor.committeememberVisscher, Koenen_US
dc.contributor.committeememberCordes, Matthewen_US
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