Characterization of Scaffolding Proteins Altered in the Ability to Perform a Critical Conformational Switch

Persistent Link:
http://hdl.handle.net/10150/195476
Title:
Characterization of Scaffolding Proteins Altered in the Ability to Perform a Critical Conformational Switch
Author:
Cherwa, Jr., James Edward
Issue Date:
2009
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:
Throughout recent history scientists have struggled to elucidate the biochemical and biophysical mechanisms that guide the assembly of macromolecular structures. The early models of "sub-assembly" or "self assembly" attempted to explain how individual components could interact in a precisely regulated manner to form higher-ordered complex biological structures. Subsequent studies, using viral systems as assembly models, demonstrated how protein-protein and protein-nucleic acid interactions assist in lowering the thermodynamic barriers that typically disfavor assembly.Due to their simplicity, viruses provide an ideal system to investigate the biophysical mechanisms that drive the assembly of complex biological structures. Proper virion assembly requires numerous macromolecular interactions that proceed along an ordered morphogenetic pathway. While structural proteins are incorporated into the final product, morphogenesis is equally dependent upon scaffolding proteins, which are not included in the mature virion. Since the identification of scaffolding proteins in the bacteriophage P22, homologues have been discovered in many systems. Scaffolding proteins play multiple roles during morphogenesis by inducing protein conformational switches and lowering the thermodynamic barriers to promote virion assembly, while ensuring the efficiency and fidelity of the final product.
Type:
text; Electronic Dissertation
Keywords:
Bacteriophage; Inhibitory proteins; Virus Assembly
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Microbiology; Graduate College
Degree Grantor:
University of Arizona
Advisor:
Fane, Bentley A.
Committee Chair:
Fane, Bentley A.

Full metadata record

DC FieldValue Language
dc.language.isoENen_US
dc.titleCharacterization of Scaffolding Proteins Altered in the Ability to Perform a Critical Conformational Switchen_US
dc.creatorCherwa, Jr., James Edwarden_US
dc.contributor.authorCherwa, Jr., James Edwarden_US
dc.date.issued2009en_US
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.abstractThroughout recent history scientists have struggled to elucidate the biochemical and biophysical mechanisms that guide the assembly of macromolecular structures. The early models of "sub-assembly" or "self assembly" attempted to explain how individual components could interact in a precisely regulated manner to form higher-ordered complex biological structures. Subsequent studies, using viral systems as assembly models, demonstrated how protein-protein and protein-nucleic acid interactions assist in lowering the thermodynamic barriers that typically disfavor assembly.Due to their simplicity, viruses provide an ideal system to investigate the biophysical mechanisms that drive the assembly of complex biological structures. Proper virion assembly requires numerous macromolecular interactions that proceed along an ordered morphogenetic pathway. While structural proteins are incorporated into the final product, morphogenesis is equally dependent upon scaffolding proteins, which are not included in the mature virion. Since the identification of scaffolding proteins in the bacteriophage P22, homologues have been discovered in many systems. Scaffolding proteins play multiple roles during morphogenesis by inducing protein conformational switches and lowering the thermodynamic barriers to promote virion assembly, while ensuring the efficiency and fidelity of the final product.en_US
dc.typetexten_US
dc.typeElectronic Dissertationen_US
dc.subjectBacteriophageen_US
dc.subjectInhibitory proteinsen_US
dc.subjectVirus Assemblyen_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineMicrobiologyen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorFane, Bentley A.en_US
dc.contributor.chairFane, Bentley A.en_US
dc.contributor.committeememberSo, Magdaleneen_US
dc.contributor.committeememberGoodrum, Feliciaen_US
dc.contributor.committeememberCollins, Jamesen_US
dc.identifier.proquest10743en_US
dc.identifier.oclc659753564en_US
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