The pyruvate dehydrogenase multienzyme complex (PDHc) plays crucial physiological roles in human. Structural study of this complex with traditional methods is highly challenging due to its large size (> 10 M Da). In this thesis, the Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS) method was employed to study the protein-protein interactions of the components in both E. coli and human PDHc, which successfully revealed their binding loci, as well as the active center coupling, the substrate coupling, the allosteric regulation, and the catalytic mechanisms. The findings greatly improved the current understanding of the PDHc model, creating opportunities for designing new drugs targeting protein-protein interactions.
Subject (authority = RUETD)
Topic
Chemistry
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_5250
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
xxvi, 283 p. : ill.
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = vita)
Includes vita
Note (type = statement of responsibility)
by Junjie Wang
Subject (authority = ETD-LCSH)
Topic
Pyruvates
Subject (authority = ETD-LCSH)
Topic
Escherichia coli
RelatedItem (type = host)
TitleInfo
Title
Graduate School - Newark Electronic Theses and Dissertations
Identifier (type = local)
rucore10002600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
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