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Order and disorder in proteins

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TitleInfo
Title
Order and disorder in proteins
Name (type = personal)
NamePart (type = family)
Ertekin
NamePart (type = given)
Asli
NamePart (type = date)
1980-
DisplayForm
ASLI ERTEKIN
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Montelione
NamePart (type = given)
Gaetano T
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Gaetano T Montelione
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Advisory Committee
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chair
Name (type = personal)
NamePart (type = family)
Nanda
NamePart (type = given)
Vikas
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Vikas Nanda
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Advisory Committee
Role
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internal member
Name (type = personal)
NamePart (type = family)
Baum
NamePart (type = given)
Jean
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Jean Baum
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Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Stock
NamePart (type = given)
Ann M
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Ann M Stock
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Anderson
NamePart (type = given)
Stephen
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Stephen Anderson
Affiliation
Advisory Committee
Role
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outside member
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NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2011
DateOther (qualifier = exact); (type = degree)
2011-10
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
In contrast to the general view that proteins should have a specific 3D structure in solution for their activity, there are many proteins which do not have a folded “native” structure for a big portion of their sequence. While these intrinsically disordered regions are essential for protein function, they cause problems in efforts for determining the 3D structures for the folded domains. It has been shown that the removal of the disordered domains improved the structure determination success both by X-ray crystallography and by NMR. As part of Northeast Structural Genomics (NESG) effort I worked on identifying the disordered and flexible parts of the protein using Hydrogen/Deuterium Exchange with Mass Spectroscopy (HDX-MS) analysis for construct optimization for high-throughput structure determination. Using this method I also studied human Smad3, which is an important part of the TGF-β-signaling pathway; and provided the first experimental data on structural features of the linker domain. During my training, I also studied human Deleted in Oral Cancer (DOC-1) protein, which was one of the proteins I studied by HDX-MS for construct optimization. We determined the solution structure of the folded region of DOC-1, which was shown to be important in cell-cycle regulation and cancer biology; and I also studied structure-function relations. Additionally, we studied the solution structure of Methionine Sulfoxide Reductase B from Bacillus subtilis, an important protein for reversing oxidative damage in cells, by NMR as a part of methods development studies for NMR for large proteins.
Subject (authority = RUETD)
Topic
Computational Biology and Molecular Biophysics
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_3559
PhysicalDescription
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electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
xvi, 119 p. : ill.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Asli Ertekin
Subject (authority = ETD-LCSH)
Topic
Proteins—Research
Subject (authority = ETD-LCSH)
Topic
Proteins—Denaturation
Subject (authority = ETD-LCSH)
Topic
Proteins--Spectra
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000063397
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/T3GH9H1P
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
ERTEKIN
GivenName
ASLI
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2011-09-14 21:28:09
AssociatedEntity
Name
ASLI ERTEKIN
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
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.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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