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Experimental and theoretical studies...

Kapp, Gregory Thomas.

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Experimental and theoretical studies of protein folding.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Experimental and theoretical studies of protein folding./
Author:	Kapp, Gregory Thomas.
Description:	155 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0205.
Contained By:	Dissertation Abstracts International65-01B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3120187
ISBN:	0496675591

Experimental and theoretical studies of protein folding.
Kapp, Gregory Thomas.

Experimental and theoretical studies of protein folding. - 155 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0205.

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

Despite over 40 years of experimental and theoretical studies, the mechanism of protein folding is not well understood. In this thesis we study the small, fast folding model proteins monomeric lambda repressor and the B domain of protein A. The forces and events involved in the folding mechanism of these fast folding proteins should also be important forces and early events in the folding of larger, biologically important proteins.

ISBN: 0496675591Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Experimental and theoretical studies of protein folding.
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100 1 $a Kapp, Gregory Thomas. $3 1932338
245 1 0 $a Experimental and theoretical studies of protein folding.
300 $a 155 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0205.
500 $a Supervisor: Terrence G. Oas.
502 $a Thesis (Ph.D.)--Duke University, 2003.
520 $a Despite over 40 years of experimental and theoretical studies, the mechanism of protein folding is not well understood. In this thesis we study the small, fast folding model proteins monomeric lambda repressor and the B domain of protein A. The forces and events involved in the folding mechanism of these fast folding proteins should also be important forces and early events in the folding of larger, biologically important proteins.
520 $a We used a combination of experimental studies and theoretical work to investigate the folding mechanism. Our experimental work examined how substitutions in the amino acid sequence affect the kinetic rates and folding mechanism of monomeric lambda repressor. In order to examine the role of helix capping motifs on the folding mechanism, we used substitutions to introduce the inter-residue interactions characteristic of helix capping motifs. The results indicate that helix N-caps increase folding rate constants by stabilizing nascent helices. The interesting results of substitutions to helix C-cap motifs of interior helices suggest that C-cap motifs may have an important role in geometrically positioning the elements of secondary structure during the folding reaction.
520 $a We also made a series of substitutions at a single position in the monomeric lambda repressor sequence. Careful analysis has shown that the global stability of the protein is affected by the hydrophobicity and helicity of this residue. The amino acid also has substantial effects on the kinetic rate constants for folding and unfolding. The kinetic effects indicate that the residue loses entropy in folding to the transition state and then makes enthalpic interactions during folding from the transition state to the native state.
520 $a Our theoretical studies involved the improvement of the diffusion-collision model for protein folding. This model describes the folding events and makes specific predictions of folding rate constants. We improved the model to account for the thermodynamic effect of amino acid substitutions. This new model is able to predict folding rate constants and folding pathways for monomeric lambda repressor protein and the B domain of protein A. The model also predicts the kinetic effects of single amino acid substitutions in both proteins.
590 $a School code: 0066.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
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710 2 0 $a Duke University. $3 569686
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Oas, Terrence G., $e advisor
790 $a 0066
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3120187