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Relation of conformational and dynamic differences in collagen sequences to alpha2I domain integrin binding affinity
Descriptive
TitleInfo
Title
Relation of conformational and dynamic differences in collagen sequences to alpha2I domain integrin binding affinity
Name
(type = personal)
NamePart
(type = family)
Wang
NamePart
(type = given)
Jacky
NamePart
(type = date)
1991-
DisplayForm
Jacky Wang
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)
York
NamePart
(type = given)
Darrin
DisplayForm
Darrin York
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
internal member
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 = 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)
2015
DateOther
(qualifier = exact);
(type = degree)
2015-05
Place
PlaceTerm
(type = code)
xx
CopyrightDate
(encoding = w3cdtf);
(qualifier = exact)
2015
Language
LanguageTerm
(authority = ISO639-2b);
(type = code)
eng
Abstract
(type = abstract)
The α2I domain of integrin has been identified to bind to the recognition motifs in collagen, GFOGER and GAOGER, with the former having a higher binding affinity than the latter. Here we employ nuclear magnetic resonance spectroscopy and circular dichroism spectroscopy to study the structural differences between the GFOGER and GAOGER collagen model peptides (CMP) triple helices. As a consequence of the limitations from using synthetic CMPs, we have also used recombinant collagen proteins expressed from E. coli as a way to efficiently screen mutations in CMPs and provide a platform to probe binding affinities using enzyme-linked immunosorbent assay. Results from this work show that the residues in GAOGER and GFOGER triple helices have few differences in dynamics, however dynamics between strands in a collagen triple helix may play a role in modulation of binding affinity. Attempts at more efficient analysis of varying CMPs using recombinant proteins have yielded us fusion proteins that can be used with enzyme-linked immunoabsorbent assay and produce recombinant CMPs.
Subject
(authority = RUETD)
Topic
Chemistry and Chemical Biology
RelatedItem
(type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
(type = RULIB)
ETD
Identifier
ETD_6203
PhysicalDescription
Form
(authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (v, 46 p. : ill.)
Note
(type = degree)
M.S.
Note
(type = bibliography)
Includes bibliographical references
Subject
(authority = ETD-LCSH)
Topic
Nuclear magnetic resonance
Note
(type = statement of responsibility)
by Jacky Wang
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/T37D2X0B
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
Wang
GivenName
Jacky
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
(encoding = w3cdtf);
(qualifier = exact);
(point = start)
2015-03-05 22:52:08
AssociatedEntity
Name
Jacky Wang
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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Technical
RULTechMD
(ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem
(VERSION = 5.1)
windows xp
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Statistical Profile