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Investigating the characteristics of collagen in protein-protein interactions through NMR relaxation experiments and indirect ELISA binding assays

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TitleInfo
Title
Investigating the characteristics of collagen in protein-protein interactions through NMR relaxation experiments and indirect ELISA binding assays
Name (type = personal)
NamePart (type = family)
Young
NamePart (type = given)
Robert T.
NamePart (type = date)
1984-
DisplayForm
Robert Young
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Baum
NamePart (type = given)
Jean
DisplayForm
Jean Baum
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Case
NamePart (type = given)
David
DisplayForm
David Case
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
York
NamePart (type = given)
Darrin
DisplayForm
Darrin York
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Nanda
NamePart (type = given)
Vikus
DisplayForm
Vikus Nanda
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
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)
2013
DateOther (qualifier = exact); (type = degree)
2013-10
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
Triple helical collagen in the most abundant protein found in the human body. It is made of three right-handed polyproline chains that supercoil together with an n-1 stagger to produce a rigid left-handed helix. Collagen has various types based on the combination of chains used to assemble the helix and each type can generate various higher order structures, such as a thick collagen fibril. Collagen’s unique G-X-Y repeated sequence and interstrand bonding network contributes to the protein’s high overall structural integrity, with the GPO triplet (GPO) being the most rigid structure and, therefore, the most often repeated sequence. A subdomain in the collagen sequence with greater internal motion and flexibility is known to be areas of molecular recognition for proteins such as the transmembrane protein integrin or the MHC-I protein subunit β2-microglobulin (B2m). As full length collagen proteins are approximately 1000 residues in length, collagen model peptides of thirty residues are often used for characterization experiments in nuclear magnetic resonance (NMR) but are not necessary in indirect ELISA binding assays. NMR relaxation experiments were conducted on a homotrimeric collagen model peptide GFOGER, designed from the high affinity integrin binding sequence in heterotrimeric type I collagen. Previous research indicated key areas of binding between the two proteins, but flexibility information about the six-residue sequence is essential for future binding studies with heterotrimer models. Experiments with longitudinal relaxation and multiple transverse relaxation experiments have indicated the flexible nature of the insert, and further work will be conducted to identify individual trimer residues and their roles in integrin binding. Indirect ELISA binding assays were conducted between full length type I collagen and B2m to first confirm reports from previous studies, and to work toward potentially identifying the binding domains on collagen that result in the initial binding and subsequent aggregation of B2m. Work in replicating the binding assays did confirm a strong binding interaction between collagen and B2m by experimenting with constant collagen concentrations and various B2m concentrations, ranging from the normal serum level to levels that are what is found in patients undergoing hemodialysis attributed to renal failure.
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_5127
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
ix, 34 p. : ill.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Robert T. Young
Subject (authority = ETD-LCSH)
Topic
Collagen
Subject (authority = ETD-LCSH)
Topic
Enzyme-linked immunosorbent assay
Subject (authority = ETD-LCSH)
Topic
Nuclear magnetic resonance
Subject (authority = ETD-LCSH)
Topic
Molecular biology--Research
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3B27SBJ
Genre (authority = ExL-Esploro)
ETD graduate
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Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Young
GivenName
Robert
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2013-10-02 09:03:52
AssociatedEntity
Name
Robert Young
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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RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
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