國立高雄大學圖資館 |

Language: English

Back

Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library.
Author:	Wei, Yinan.
Description:	211 p.
Notes:	Adviser: Michael H. Hecht.
Notes:	Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4343.
Contained By:	Dissertation Abstracts International64-09B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3102230
ISBN:	0496498002

Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library.
Wei, Yinan.

Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library. [electronic resource] - 211 p.

Adviser: Michael H. Hecht.

Thesis (Ph.D.)--Princeton University, 2003.

Binary patterning of polar and nonpolar amino acids has been used as the key design feature for constructing large combinatorial libraries of de novo proteins. To assess whether the binary code strategy can produce well-folded de novo proteins, recently a second-generation library of 102 residues four helix bundle proteins was constructed. This thesis concentrates on structural and functional studies of proteins from this library.

ISBN: 0496498002Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library.
LDR:03140nmm _2200301 _450 001 162132
005 20051017073414.5
008 230606s2003 eng d
020 $a 0496498002
035 $a 00148633
035 $a 162132
040 $a UnM $c UnM
100 0 $a Wei, Yinan. $3 227245
245 1 0 $a Structural and functional studies of well-folded alpha helical proteins from a designed combinatorial library. $h [electronic resource]
300 $a 211 p.
500 $a Adviser: Michael H. Hecht.
500 $a Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4343.
502 $a Thesis (Ph.D.)--Princeton University, 2003.
520 # $a Binary patterning of polar and nonpolar amino acids has been used as the key design feature for constructing large combinatorial libraries of de novo proteins. To assess whether the binary code strategy can produce well-folded de novo proteins, recently a second-generation library of 102 residues four helix bundle proteins was constructed. This thesis concentrates on structural and functional studies of proteins from this library.
520 # $a Chapter 1 of this thesis introduces the field of protein design and the binary code strategy. Chapter 2 describes the characterization of five proteins from the second generation library. All five proteins are monomeric, highly alpha-helical and much more stable compared to proteins from an earlier library. Four of the five proteins displayed properties consistent with well-ordered and/or native-like structures. Chapter 3 describes the solution structure of one protein, S-824, which was solved by NMR. The structure is indeed a four helix bundle as specified in the design. These results suggest that proteins with well-folded structures occur frequently in binary patterned library.
520 # $a Finally in chapter 6, the feasibility of using phage display to screen our combinatorial library for proteins with enhance stability was assessed.
520 # $a The ultimate goal of protein design is to make functional proteins. In the combinatorial approach, the frequency of occurrence of proteins with putative function is a critical factor. This issue is addressed in chapter 5 by testing selected proteins from both four helix bundle libraries for esterase activity. All seven proteins examined displayed catalytic activity for the hydrolysis of p-nitrophenyl esters with rate enhancements comparable to other artificial proteins.
520 # $a With the knowledge of the structure of S-824, mutational studies were carried out in chapter 4 to probe the roles of individual residues. Mutants were made to investigate the influence of the turn length, the coexistence of bulky aromatic residues in local proximity, and the hydrophobic plugging effect of a Trp residue in the first turn.
590 $a School code: 0181.
650 # 0 $a Chemistry, Biochemistry. $3 226900
710 0 # $a Princeton University. $3 212488
773 0 # $g 64-09B. $t Dissertation Abstracts International
790 $a 0181
790 1 0 $a Hecht, Michael H., $e advisor
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3102230 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3102230