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NMR conformational and dynamic characterization of triple helical peptides

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
NMR conformational and dynamic characterization of triple helical peptides
SubTitle
PartName
PartNumber
NonSort
Identifier (displayLabel = ); (invalid = )
ETD_2068
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000051923
Language (objectPart = )
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Chemistry and Chemical Biology
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Peptides
Subject (ID = SBJ-3); (authority = ETD-LCSH)
Topic
Collagen
Subject (ID = SBJ-4); (authority = ETD-LCSH)
Topic
Nuclear magnetic resonance spectroscopy
Abstract
The repeating Gly-X-Y sequences and uniform rod-like structure makes collagen-like peptides a unique system for NMR studies. In this dissertation, a number of triple helical peptides modeling biologically important regions in collagen, such as mutation sites, interruption sites and collagenase cleavage sites, are investigated by a variety of NMR techniques. Structure determination strategy combining molecular modeling and NMR spectroscopy have been developed on a classic triple helical peptide. Novel approaches capable of obtaining long-range order restraints, such as residual dipolar coupling and 15N relaxation measurements, are applied to obtain detailed information about the orientation of the N-H bonds, which are crucial in defining collagen structure.
Triple helical peptides modeling Gly mutations involved in Osteogenesis imperfecta (OI), a connective tissue disorder, are investigated to elucidate the structural bases of various OI phenotypes. The level of structural disruption by different Gly substitutions is found to correlate well with the lethality of OI, while Arg/Asp causes larger disruption and is more likely to result in lethal OI. Triple helical peptides modeling natural interruptions in a heterotrimeric rather than homotrimeric environment have been successfully obtained and special features of stability, conformation, dynamics and folding at the interruption sites are detected by NMR.
Triple helical peptides, which model natural cleavage sites and potential but noncleavable sites in collagen, are explored to understand the specific recognition of collagen by matrix metalloproteinases (MMP). A single Ile at the cleavage site shows a distinct chemical shift, an unusual J-coupling value, dramatically increased dynamics and decreased local stability, suggesting that the Ile may be released from the restricted triple helical conformation and recognized by MMPs. The distribution of neighboring imino acids is also shown to be able to affect the local conformation and dynamics at the cleavage sites. This thesis correlates collagen sequence variations to the changes in structural and dynamic features of collagen-like peptides, furthering our understanding of the molecular bases for collagen-involved diseases and recognitions.
PhysicalDescription
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electronic resource
Extent
xv, 160 p. : ill.
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Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references (p. 150-159)
Note (type = statement of responsibility)
by Jianxi Xiao
Name (ID = NAME-1); (type = personal)
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Xiao
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Jianxi
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1980-
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author
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Jianxi Xiao
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Baum
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Jean
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chair
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Advisory Committee
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Jean Baum
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Taylor
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John
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internal member
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John Taylor
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Talaga
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David
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internal member
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Advisory Committee
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David Talaga
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NamePart (type = family)
Brodsky
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Barbara
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outside member
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Advisory Committee
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Barbara Brodsky
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
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degree grantor
Name (ID = NAME-2); (type = corporate)
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Graduate School - New Brunswick
Role
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school
OriginInfo
DateCreated (point = ); (qualifier = exact)
2009
DateOther (qualifier = exact); (type = degree)
2009-10
Place
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xx
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
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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/T3222TX6
Genre (authority = ExL-Esploro)
ETD doctoral
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RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work
Copyright
Status
Copyright protected
Notice
Note
Availability
Status
Open
Reason
Permission or license
Note
RightsHolder (ID = PRH-1); (type = personal)
Name
FamilyName
Xiao
GivenName
Jianxi
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Copyright holder
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DateTime
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Name
Jianxi Xiao
Affiliation
Rutgers University. Graduate School - New Brunswick
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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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