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Structural studies of protein-protei...

Katz, Darin Scott.

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Structural studies of protein-protein interactions in biotechnology.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structural studies of protein-protein interactions in biotechnology./
Author:	Katz, Darin Scott.
Description:	195 p.
Notes:	Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0302.
Contained By:	Dissertation Abstracts International57-01B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9615060

Structural studies of protein-protein interactions in biotechnology.
Katz, Darin Scott.

Structural studies of protein-protein interactions in biotechnology. - 195 p.

Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0302.

Thesis (Ph.D.)--University of Pennsylvania, 1995.

The work presented in this thesis is aimed at elucidating structure/function relationships for two proteins that participate in different types of protein-protein interactions. X-ray crystallography and modeling studies of these proteins have important implications for their possible roles in biotechnology. First, protease-inhibitor complexes are represented by studies of Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Structural studies of protein-protein interactions in biotechnology.
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035 $a (UnM)AAI9615060
035 $a AAI9615060
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100 1 $a Katz, Darin Scott. $3 1931833
245 1 0 $a Structural studies of protein-protein interactions in biotechnology.
300 $a 195 p.
500 $a Source: Dissertation Abstracts International, Volume: 57-01, Section: B, page: 0302.
500 $a Adviser: David W. Christianson.
502 $a Thesis (Ph.D.)--University of Pennsylvania, 1995.
520 $a The work presented in this thesis is aimed at elucidating structure/function relationships for two proteins that participate in different types of protein-protein interactions. X-ray crystallography and modeling studies of these proteins have important implications for their possible roles in biotechnology. First, protease-inhibitor complexes are represented by studies of $\ alpha\sb1 $- antichymotrypsin (ACT) and its complex with chymotrypsin. The three-dimensional structure of the P3-P3 $\ sp\prime $ variant of ACT (rACT-P3P3 $\ sp\prime $) provides the first atomic view of the reactive loop from an uncleaved and completely inhibitory serpin. Additionally, the first model of a serpin-protease complex, the ACT-chymotrypsin complex, yields significant mechanistic conclusions regarding the conformation of the serpin reactive loop in the Michaelis complex. Second, complementing these studies was the three-dimensional structure of aquomet porcine hemoglobin at 2.8 A resolution, which series as a paradigm for the study of oligomeric proteins.
520 $a The conclusions drawn from this work are as follows: (1) The reactive loops of native (uncleaved) serpins display $\ alpha $- helical properties and are not inserted into $\ beta $- sheet A, as evidenced by rACT-P3P3 $\ sp\prime $ and uncleaved ovalbumin (a non-inhibitory serpin homologue); (2) Following complexation with a protease, the helical reactive loop unwinds and insertion of residues P16-P14 into $\ beta $- sheet A occurs, as modeled in the ACT-chymotrypsin complex; (3) These studies, in accordance with numerous kinetic and biochemical analyses of serpin-protease complexes, point toward an induced fit mechanism for serpin-protease inhibition; (4) Aquomet porcine hemoglobin and oxygenated human hemoglobin were found to have similar secondary and tertiary structures, resulting in similar protein-heme environments and subunit-subunit interfaces within each hemoglobin tetramer; (5) The 20-25% reduced alkaline Bohr effect evidenced in the porcine erythrocyte results from bulk electrostatic effects within the central cavity of the porcine tetramer which displays lessened positive electrostatic potential than the human tetramer; (6) The formation of interspecies hybrids in the transgenic porcine erythrocyte results from structural and electrostatic complementarity between the porcine and human subunits. Importantly, amino acid differences in the porcine and human $\ alpha $- chains influence the overall lower thermodynamic stability of the p $\ alpha $- h $\ beta $ heterodimer.
590 $a School code: 0175.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 0 $a University of Pennsylvania. $3 1017401
773 0 $t Dissertation Abstracts International $g 57-01B.
790 1 0 $a Christianson, David W., $e advisor
790 $a 0175
791 $a Ph.D.
792 $a 1995
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9615060