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Molecular recognition of protein sur...

Sprinz, Katherine Ingrid.

Molecular recognition of protein surfaces by rational and combinatorial methods.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Molecular recognition of protein surfaces by rational and combinatorial methods.
Author:	Sprinz, Katherine Ingrid.
Description:	134 p.
Notes:	Adviser: Andrew D. Hamilton.
Notes:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5967.
Contained By:	Dissertation Abstracts International66-11B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3194710
ISBN:	9780542394928

Molecular recognition of protein surfaces by rational and combinatorial methods.
Sprinz, Katherine Ingrid.

Molecular recognition of protein surfaces by rational and combinatorial methods. - 134 p.

Adviser: Andrew D. Hamilton.

Thesis (Ph.D.)--Yale University, 2005.

HIV-1 reverse transcriptase is a pseudo-heterodimer that is comprised of two subunits (p66 and p51) that share the same primary sequence until a truncation point, where one subunit is cleaved (p51) and the other (p66) contains the active site of the protein. Previously reported peptides in the literature, derived from the dimerization domain, were tested for their binding capabilities but the assay approach left it uncertain whether the peptides were binding one subunit over the other. In order to determine the binding partners, several of these previously tested peptides were analyzed in a fluorescence depolarization assay. After getting comparable results with the published literature, additional peptides were derived from the alpha-helical interaction that occurs between the two subunits. Two peptides derived from the p51 subunit bound p66 with a greater affinity than they bound p51 which agrees with new findings that the subunits have the same conformations in the monomeric form as they do in the active dimer. This assay can be used to find reverse transcriptase dimerization inhibitors that can compete with the fluorescently-labeled peptides investigated in this study.

ISBN: 9780542394928Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Molecular recognition of protein surfaces by rational and combinatorial methods.
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245 1 0 $a Molecular recognition of protein surfaces by rational and combinatorial methods.
300 $a 134 p.
500 $a Adviser: Andrew D. Hamilton.
500 $a Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5967.
502 $a Thesis (Ph.D.)--Yale University, 2005.
520 # $a HIV-1 reverse transcriptase is a pseudo-heterodimer that is comprised of two subunits (p66 and p51) that share the same primary sequence until a truncation point, where one subunit is cleaved (p51) and the other (p66) contains the active site of the protein. Previously reported peptides in the literature, derived from the dimerization domain, were tested for their binding capabilities but the assay approach left it uncertain whether the peptides were binding one subunit over the other. In order to determine the binding partners, several of these previously tested peptides were analyzed in a fluorescence depolarization assay. After getting comparable results with the published literature, additional peptides were derived from the alpha-helical interaction that occurs between the two subunits. Two peptides derived from the p51 subunit bound p66 with a greater affinity than they bound p51 which agrees with new findings that the subunits have the same conformations in the monomeric form as they do in the active dimer. This assay can be used to find reverse transcriptase dimerization inhibitors that can compete with the fluorescently-labeled peptides investigated in this study.
590 $a School code: 0265.
650 # 0 $a Chemistry, Biochemistry. $3 226900
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790 1 0 $a Hamilton, Andrew D., $e advisor
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