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Characterization of a new collagen-like protein from trichodesmium erythraeum

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TitleInfo
Title
Characterization of a new collagen-like protein from trichodesmium erythraeum
Name (type = personal)
NamePart (type = family)
Shah
NamePart (type = given)
Ruchit Girishchandra
NamePart (type = date)
1987-
DisplayForm
Ruchit Shah
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Silver
NamePart (type = given)
Frederick H.
DisplayForm
Frederick H. Silver
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Shreiber
NamePart (type = given)
David I.
DisplayForm
David I. Shreiber
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Freeman
NamePart (type = given)
Joseph W.
DisplayForm
Joseph W. Freeman
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)
2012
DateOther (qualifier = exact); (type = degree)
2012-01
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
In order to meet the exponentially rising demands of collagen in the fields of tissue engineering, cosmetic surgery and drug delivery systems, there is an increasing demand to find novel sources. Recently, an intron-free collagen-like gene found in Trichodesmium erythraeum, a colonial marine cyanobacterium, was reported. This thesis aims at characterizing this new collagen-like sequence and theoretically comparing it with human collagens (especially type I human collagen) and few other bacterial proteins in terms of amino acid composition, flexibility, hydropathicity and charge density. Enzyme degradation and polarized light microscopy were utilized to support the hypothesis of presence of collagen-like protein in T. erythraeum’s cell. The initial step of analysis involved running the blastp algorithm using this new sequence as the query sequence and studying its resemblance to various proteins in RefSeq protein database. Comparison with type I human collagen revealed that the assumed homotrimer molecule of Trichodesmium erythraeum’s collagen-like protein is almost as relatively stable as the former. The alternate flexible and rigid domains in the molecular structure can be predicted to coincide and form a highly flexible fibrillar structure that may aid the aggregates to survive stresses from ocean. It is suggested that this collagen-like protein is primarily responsible for transmission of energy during loading and not as much for storage of elastic energy. This new sequence was found to be highly hydrophobic and sparsely charged unlike any of the other sequences used in analyses. Based on this unusual hydrophobic nature, this collagen-like protein may find its applications for procedures like guided tissue reconstruction in dentistry as also in hernia repair and topical wound dressings. In order to determine the potential of the collagen gene of Trichodesmium erythraeum for tissue engineering, further studies will be required that include experimentally measuring its thermal stability, enzymatic stability of the triglycine repeat region and the globular N and C termini and its ability to undergo fibrillogenesis using established methods.
Subject (authority = RUETD)
Topic
Biomedical Engineering
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_3709
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
viii, 69 p. : ill.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Ruchit Girishchandra Shah
Subject (authority = ETD-LCSH)
Topic
Cyanobacteria--Genetics
Subject (authority = ETD-LCSH)
Topic
Collagen
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000064174
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/T30R9NFS
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
Shah
GivenName
Ruchit
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2011-11-26 16:35:46
AssociatedEntity
Name
Ruchit Shah
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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1787904
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application/pdf
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application/x-tar
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