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Characterization ofaPP derived minia...

Woronowicz, Kamil.

Characterization ofaPP derived miniature proteins.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Characterization ofaPP derived miniature proteins.
作者:	Woronowicz, Kamil.
面頁冊數:	134 p.
附註:	Director: Alanna Schepartz.
附註:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5969.
Contained By:	Dissertation Abstracts International66-11B.
標題:	Chemistry, Biochemistry.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3194726
ISBN:	9780542395062

Characterization ofaPP derived miniature proteins.
Woronowicz, Kamil.

Characterization ofaPP derived miniature proteins. - 134 p.

Director: Alanna Schepartz.

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

Chapter two addresses an alanine scanning of EVH1-binding protein pGolemi. Actin cytoskeletal rearrangements needed for cellular motility, axon guidance and other processes are controlled in part by paralogous, EVH1-containing proteins Mena, Vasp and Evl. Novel binding partners that perturb the system in a specific manner can promote understanding of molecular interactions that drive these events. Recently, our lab has generated such a novel EVH1-binding protein, pGolemi, which has unprecedented paralog specificity. In this work, an alanine scanning mutagenesis study is described in which the contributions of 14 pGolemi residues to EVH1 affinity, specificity, and miniature protein secondary structure were examined. It was found that pGolemi binds Mena-EVH1 domain in a fashion similar to Listeria monocytogenes' derived ActA peptide. Additionally, folding residues contribute to Mena EVH1 binding, and this effect diminishes with proximity to peptide's terminus. There is a correlation between alpha-helical content and affinity among variants, suggesting that pGolemi is structurally preorganized for binding to Mena EVH1 domain. No such correlation is observed for specificity among EVH1 domains of the Mena paralogs, VASP and Evl. This evidence suggests a model where pGolemi folding is required for EVH1 domain binding, but paralog specificity is dictated by the residue identity within a functional epitope.

ISBN: 9780542395062Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Characterization ofaPP derived miniature proteins.
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500 $a Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5969.
502 $a Thesis (Ph.D.)--Yale University, 2005.
520 # $a Chapter two addresses an alanine scanning of EVH1-binding protein pGolemi. Actin cytoskeletal rearrangements needed for cellular motility, axon guidance and other processes are controlled in part by paralogous, EVH1-containing proteins Mena, Vasp and Evl. Novel binding partners that perturb the system in a specific manner can promote understanding of molecular interactions that drive these events. Recently, our lab has generated such a novel EVH1-binding protein, pGolemi, which has unprecedented paralog specificity. In this work, an alanine scanning mutagenesis study is described in which the contributions of 14 pGolemi residues to EVH1 affinity, specificity, and miniature protein secondary structure were examined. It was found that pGolemi binds Mena-EVH1 domain in a fashion similar to Listeria monocytogenes' derived ActA peptide. Additionally, folding residues contribute to Mena EVH1 binding, and this effect diminishes with proximity to peptide's terminus. There is a correlation between alpha-helical content and affinity among variants, suggesting that pGolemi is structurally preorganized for binding to Mena EVH1 domain. No such correlation is observed for specificity among EVH1 domains of the Mena paralogs, VASP and Evl. This evidence suggests a model where pGolemi folding is required for EVH1 domain binding, but paralog specificity is dictated by the residue identity within a functional epitope.
520 # $a This dissertation describes the characterization of aPP derived miniature proteins. The first chapter discusses an attempt to reassemble the DNA-binding miniature protein p007 from two fragments. Several in vivo protein complementation assays (PCA) were initially explored, but dihydrofolate reductase (DHFR) PCA was chosen for screening large libraries. To further organize the alpha-helix fragment of p007, peptide-DNA conjugate was synthesized resulting in a DNA binding alpha-helix of p007 bound to its target hsCRE sequence. Phage display was utilized to screen library members that would interact with such peptide-DNA conjugate.
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