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Understanding DNA-protein hybridization-dependent interactions

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TitleInfo
Title
Understanding DNA-protein hybridization-dependent interactions
Name (type = personal)
NamePart (type = family)
O'Grady
NamePart (type = given)
Laura
NamePart (type = date)
1959-
DisplayForm
Laura O'Grady
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Olson
NamePart (type = given)
Wilma K
DisplayForm
Wilma K Olson
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Das
NamePart (type = given)
Kalyan
DisplayForm
Kalyan Das
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 = 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)
2012-10
CopyrightDate (qualifier = exact)
2012
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
The study of DNA-protein interactions is important since these associations are critical to the operation of living cells. DNA-protein contacts show distinct microenvironments. Hybridization is a notable atomic feature that contributes to the distribution of charge within a protein. In order to study a manageable amount of discreet data, a dataset of 499 non-redundant structures was generated. These structures were chosen from DNA-protein structures of high resolution (> 2.5วบ), available in the Protein Data Bank up to June 2011. This research describes differences in DNA-protein interactions based upon atomic hybridization within the set of non-redundant protein structures generated. Although generalizations can be made in terms of hybridization-dependent DNA-protein interactions, the data in this research show hydrogen bond donor-acceptor relationships, as well as electrostatic (positive-negative) attractions, are the primary features regulating close contacts in the major grooves. In general, atoms with a more electropositive environment show a greater number of close contacts with sp2 hybridized atoms, and conversely atoms with a more electronegative environment show a greater number close contacts with sp3 hybridized atoms. However, for proteins comprised of amino acids with delocalized electrons, it is the charge (positive or negative) on the functional group, as well as the structure (cyclic or aliphatic) that have the greatest impact on the number and type of close contacts.
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_4288
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
xii, 243 p. : ill.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = vita)
Includes vita
Note (type = statement of responsibility)
by Laura O'Grady
Subject (authority = ETD-LCSH)
Topic
DNA-protein interactions--Research
Subject (authority = ETD-LCSH)
Topic
Cell hybridization
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000066929
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/T3GQ6WHF
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
O'Grady
GivenName
Laura
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2012-09-26 09:56:28
AssociatedEntity
Name
Laura O'Grady
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

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1710592
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application/pdf
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application/x-tar
FileSize (UNIT = bytes)
1720320
Checksum (METHOD = SHA1)
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