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Mass spectrometry based methods for studies of component assembly and structure/dynamics of thiamin diphosphate dependent enzymes
Descriptive
TitleInfo
Title
Mass spectrometry based methods for studies of component assembly and structure/dynamics of thiamin diphosphate dependent enzymes
Name
(type = personal)
NamePart
(type = family)
Zhou
NamePart
(type = given)
Jieyu
NamePart
(type = date)
1979-
DisplayForm
Jieyu Zhou
Role
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(authority = RULIB)
author
Name
(type = personal)
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(type = family)
Jordan
NamePart
(type = given)
Frank
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Frank Jordan
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Advisory Committee
Role
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chair
Name
(type = personal)
NamePart
(type = family)
Huskey
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(type = given)
Phil
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Phil Huskey
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Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Sheridan
NamePart
(type = given)
John
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John Sheridan
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Lee
NamePart
(type = given)
Jeehiun Katherine
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Jeehiun Katherine Lee
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
outside member
Name
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NamePart
Rutgers University
Role
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(authority = RULIB)
degree grantor
Name
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Graduate School - Newark
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school
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Text
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theses
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2016
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2016-10
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2016
Place
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xx
Language
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eng
Abstract
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For the metabolism of a cell, most of the proteins function as complexes rather than by themselves. Understanding not only how proteins behave in isolation but also how they recognize their binding partners is therefore critical for understanding the functions of proteins. In recent decades, our understanding of protein-protein or protein-ligand interactions have moved beyond rigid binding to conformational changes upon binding, multistep ordered assembly, and structural fluctuations occurring within fully assembled complexes. In this thesis, the Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) and Chemical Cross-Linking Mass Spectrometry (CX-MS) methods were employed to study the assembly of human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc). Our experiments revealed the binding loci, which is essential to the assembly of human OGDHc. Our findings provide a new insight to understand the structure, organization and assembly of the human OGDHc. Moreover, we have used HDX-MS to explore the protein-ligand interactions of 1-deoxy-D-xylulose 5-phosphate synthase (DXPS). The unique peptides exhibiting EX1-type HDX kinetics found in this thiamin diphosphate (ThDP) dependent enzyme enable us to understand how DXPS structure and dynamics respond to different ligands. A better picture of ligand induced DXPS conformational changes can be provided to help elucidate the mechanism of catalysis, and enable structure-based inhibitor design.
Subject
(authority = RUETD)
Topic
Chemistry
Subject
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Topic
Mass spectrometry
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Title
Rutgers University Electronic Theses and Dissertations
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ETD_7575
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electronic resource
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application/pdf
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Extent
1 online resource (xvi, 150 p. : ill.)
Note
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Ph.D.
Note
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Includes bibliographical references
Note
(type = statement of responsibility)
by Jieyu Zhou
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TitleInfo
Title
Graduate School - Newark Electronic Theses and Dissertations
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rucore10002600001
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(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
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doi:10.7282/T3FB559K
Genre
(authority = ExL-Esploro)
ETD doctoral
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Rights
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The author owns the copyright to this work.
RightsHolder
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Name
FamilyName
Zhou
GivenName
Jieyu
Role
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RightsEvent
Type
Permission or license
DateTime
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2016-09-14 21:59:12
AssociatedEntity
Name
jieyu zhou
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Affiliation
Rutgers University. Graduate School - Newark
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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.
RightsEvent
DateTime
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2016-10-31
DateTime
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2018-10-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after October 31st, 2018.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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