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Design, characterization of amphiphi...

University of Pennsylvania.

Design, characterization of amphiphilic proteins and potential engineering applications.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Design, characterization of amphiphilic proteins and potential engineering applications.
Author:	Ye, Shixin.
Description:	157 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2928.
Notes:	Supervisor: J. Kent Blasie.
Contained By:	Dissertation Abstracts International65-06B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3138094
ISBN:	0496852647

Design, characterization of amphiphilic proteins and potential engineering applications.
Ye, Shixin.

Design, characterization of amphiphilic proteins and potential engineering applications. - 157 p.

Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2928.

Thesis (Ph.D.)--University of Pennsylvania, 2004.

Orienting molecules as an ensemble to generate macroscopic response is the key step in realizing material applications. Based on hydrophobic concept, de novo designed maquettes have been rendered to be protein amphiphiles to create an ensemble at the air-water interface. Initially, we seek to construct a monolayer composed of four-alpha-helical bundles formed by association of di-alpha-helical peptides which are attached with hydrocarbon chains at the N-termini of peptide. Then, membrane proteins that mimic natural heme proteins, and vectorially-orient at the air-water interface as a well-ordered ensemble have been developed. A significant progress has been achieved in the area of development of transmembrane proteins that are capable of incorporating pigment cofactors required to promote light activated electron transfer. These designed membrane proteins have been demonstrated to insert into host phospholipids monolayers and to vectorially orient in the membrane. This new finding has been successfully applied to the design of model membrane proteins to understand the anesthetic binding mechanism.

ISBN: 0496852647Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Design, characterization of amphiphilic proteins and potential engineering applications.
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245 1 0 $a Design, characterization of amphiphilic proteins and potential engineering applications.
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500 $a Source: Dissertation Abstracts International, Volume: 65-06, Section: B, page: 2928.
500 $a Supervisor: J. Kent Blasie.
502 $a Thesis (Ph.D.)--University of Pennsylvania, 2004.
520 # $a Orienting molecules as an ensemble to generate macroscopic response is the key step in realizing material applications. Based on hydrophobic concept, de novo designed maquettes have been rendered to be protein amphiphiles to create an ensemble at the air-water interface. Initially, we seek to construct a monolayer composed of four-alpha-helical bundles formed by association of di-alpha-helical peptides which are attached with hydrocarbon chains at the N-termini of peptide. Then, membrane proteins that mimic natural heme proteins, and vectorially-orient at the air-water interface as a well-ordered ensemble have been developed. A significant progress has been achieved in the area of development of transmembrane proteins that are capable of incorporating pigment cofactors required to promote light activated electron transfer. These designed membrane proteins have been demonstrated to insert into host phospholipids monolayers and to vectorially orient in the membrane. This new finding has been successfully applied to the design of model membrane proteins to understand the anesthetic binding mechanism.
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773 0 # $g 65-06B. $t Dissertation Abstracts International
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790 1 0 $a Blasie, J. Kent, $e advisor
791 $a Ph.D.
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