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Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.
Author:	Willis, Mark Ashton.
Description:	113 p.
Notes:	Directors: Lynne Regan; Axel T. Brunger.
Notes:	Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4926.
Contained By:	Dissertation Abstracts International64-10B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3109484
ISBN:	0496570269

Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.
Willis, Mark Ashton.

Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. [electronic resource] - 113 p.

Directors: Lynne Regan; Axel T. Brunger.

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

A biophysical characterization of Ala2IIe2-6 demonstrates that this repacked protein has native-like folding properties and is dimeric, like the wild-type protein. It differs from Rop in two major ways: Ala 2IIe2-6 is more thermally stable, and it lacks the capacity to bind an RNA stem-loop complex.

ISBN: 0496570269Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.
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100 0 $a Willis, Mark Ashton. $3 227429
245 1 0 $a Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. $h [electronic resource]
300 $a 113 p.
500 $a Directors: Lynne Regan; Axel T. Brunger.
500 $a Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4926.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 # $a A biophysical characterization of Ala2IIe2-6 demonstrates that this repacked protein has native-like folding properties and is dimeric, like the wild-type protein. It differs from Rop in two major ways: Ala 2IIe2-6 is more thermally stable, and it lacks the capacity to bind an RNA stem-loop complex.
520 # $a A structural and thermodynamic analysis of a variant of the four-helix bundle protein Rop has been undertaken to investigate the consequences of systematically repacking the hydrophobic core of a protein. This variant, Ala2IIe2-6, was created by systematically replacing Rop's hydrophobic core residues with alanines and isoleucines.
520 # $a To investigate the causes for these changes, a detailed structural and thermodynamic analysis of Ala2IIe2-6 has been performed. The crystal structure of Ala2IIe2-6 reveals a dramatic change in topology from that of wild-type Rop; the dimeric interface of Ala 2IIe2-6 has been transformed by a 180° rotation of one protomer around an axis perpendicular to this interface. There is a large difference in the thermodynamic parameters of Ala2IIe2-6 and Rop as well. Although the overall stability of the two proteins are similar, the balance of enthalpic and entropic contributions to the free energy of folding has changed considerably, shifting the stability profile of Ala 2IIe2-6 to higher temperatures. It is proposed that much of the change in the thermodynamic parameters can be explained by the increased disorder of residues at the helix termini of Ala2IIe2-6. A modeling analysis of Ala2IIe2-6 and Rop reveals the importance of side chain rotomers and stereochemistry in the packing of the hydrophobic core, and how this may influence the fold of the four-helix bundle. These results demonstrate how subtle changes to the stereochemistry of residues in the hydrophobic core can have dramatic structural and thermodynamic consequences.
590 $a School code: 0265.
650 # 0 $a Chemistry, Biochemistry. $3 226900
650 # 0 $a Biophysics, General. $3 226901
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790 1 0 $a Brunger, Axel T., $e advisor
790 1 0 $a Regan, Lynne, $e advisor
791 $a Ph.D.
792 $a 2003
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