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Time-resolved fluorescence studies of protein aggregation leading to amyloid formation

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TitleInfo (displayLabel = Citation Title); (type = uniform)
Title
Time-resolved fluorescence studies of protein aggregation leading to amyloid formation
Name (ID = NAME001); (type = personal)
NamePart (type = family)
Giurleo
NamePart (type = given)
Jason Thomas
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Jason Thomas Giurleo
Role
RoleTerm (authority = RUETD)
author
Name (ID = NAME002); (type = personal)
NamePart (type = family)
Talaga
NamePart (type = given)
David
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Advisory Committee
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David S Talaga
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chair
Name (ID = NAME003); (type = personal)
NamePart (type = family)
Levy
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Ronald
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Advisory Committee
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Ronald M Levy
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internal member
Name (ID = NAME004); (type = personal)
NamePart (type = family)
Castner
NamePart (type = given)
Edward
Affiliation
Advisory Committee
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Edward W Castner
Role
RoleTerm (authority = RULIB)
internal member
Name (ID = NAME005); (type = personal)
NamePart (type = family)
Brodsky
NamePart (type = given)
Barbra
Affiliation
Advisory Committee
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Barbra Brodsky
Role
RoleTerm (authority = RULIB)
outside member
Name (ID = NAME006); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (ID = NAME007); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2008
DateOther (qualifier = exact); (type = degree)
2008-10
Language
LanguageTerm
English
PhysicalDescription
Form (authority = marcform)
electronic
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application/pdf
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text/xml
Extent
xxxiii, 312 pages
Abstract
Aggregation of soluble polypeptides or proteins into insoluble amyloid fibrils containing the cross-beta structural motif has been observed in the progression of over 20 diseases. Self-assembly mechanisms have been proposed but are not well-established. Recent evidence has shifted some of the focus from amyloid fibrils to prefibrillar amyloidogenic aggregates as the cause of disease symptoms. We used time-resolved non-covalent fluorescence labeling to follow the conformational changes occurring in a model protein (beta-lactoglobulin) during amyloid aggregation. The data was analyzed using a novel model-free globally regularized fitting technique. This reduction of model space allowed for stable fitting and the ability to identify intermediate species. An aggregation model was then proposed. In the second half of this thesis, our attention is shifted to alpha-synuclein (aSyn). aSyn is the majority protein component of the fibrillar inclusion bodies found in brains of Parkinson's disease patients. We have begun a set of fluorescence lifetime experiments using covalent and non-covalent labeling schemes to elucidate the dynamic, conformational and aggregation properties of aSyn.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references.
Subject (ID = SUBJ1); (authority = RUETD)
Topic
Chemistry and Chemical Biology
Subject (ID = SUBJ2); (authority = ETD-LCSH)
Topic
Cell aggregation
Subject (ID = SUBJ3); (authority = ETD-LCSH)
Topic
Protein folding
Subject (ID = SUBJ4); (authority = ETD-LCSH)
Topic
Amyloidosis
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17477
Identifier
ETD_1304
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T33R0T67
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
Jason Giurleo
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
Detail
Non-exclusive ETD license
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Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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application/x-tar
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