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A NMR investigation of structure and...

Bhattacharya, Akash.

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A NMR investigation of structure and allostery in the Hsp70 chaperone system.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	A NMR investigation of structure and allostery in the Hsp70 chaperone system./
Author:	Bhattacharya, Akash.
Description:	226 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2882.
Contained By:	Dissertation Abstracts International71-05B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3406414
ISBN:	9781109731620

A NMR investigation of structure and allostery in the Hsp70 chaperone system.
Bhattacharya, Akash.

A NMR investigation of structure and allostery in the Hsp70 chaperone system. - 226 p.

Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2882.

Thesis (Ph.D.)--University of Michigan, 2010.

The Hsp70 Chaperone system is a complex molecular machine composed of proteins. It is responsible for assisting in protein folding/refolding/processing and transport. Hsp70 proteins have been historically associated with the 'stress' or 'heatshock' response of cells. They function in association with several co-chaperones in a delicately balanced and regulated two stage functional cycle. This system and its component molecules has been the subject of intensive efforts in structural biophysics for the last two decades.

ISBN: 9781109731620Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

A NMR investigation of structure and allostery in the Hsp70 chaperone system.
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020 $a 9781109731620
035 $a (UMI)AAI3406414
035 $a AAI3406414
040 $a UMI $c UMI
100 1 $a Bhattacharya, Akash. $3 1683863
245 1 2 $a A NMR investigation of structure and allostery in the Hsp70 chaperone system.
300 $a 226 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-05, Section: B, page: 2882.
500 $a Adviser: Erik R.P. Zuiderweg.
502 $a Thesis (Ph.D.)--University of Michigan, 2010.
520 $a The Hsp70 Chaperone system is a complex molecular machine composed of proteins. It is responsible for assisting in protein folding/refolding/processing and transport. Hsp70 proteins have been historically associated with the 'stress' or 'heatshock' response of cells. They function in association with several co-chaperones in a delicately balanced and regulated two stage functional cycle. This system and its component molecules has been the subject of intensive efforts in structural biophysics for the last two decades.
520 $a In this dissertation we present an analysis of the allosteric machinery, which operates in this molecular system. Using residual dipolar coupling analysis, a state-of-the-art method in solution nuclear magnetic resonance (NMR) spectroscopy, we have been able to detect distinct changes in the T.th-DnaK (the thermophilic Hsp70 protein) as the protein switches between the different stages of its 'two-stroke' functional cycle. Specifically, we have seen an opening of the nucleotide binding cleft in the ADP.PI state, without any exchange factor involved. Furthermore, we observed an opening of the IA/IIA interface cleft which would account for the linker being structured in the ATP state and explain how the interdomain allostery works in Hsp70s. Such changes have been observed for the first time in this field. We have also refined new methods to detect residual dipolar couplings and scrutinized our results with the most stringent possible statistical analysis.
520 $a In the second stage of this dissertation, we have studied the interaction of E. coli DnaK (the bacterial Hsp70 molecule) with DnaJ (the equivalent bacterial co-chaperone) using paramagnetic relaxation enhancement in solution NMR. Based on this analysis, we propose a model for the interaction of DnaK with DnaJ, where DnaJ lies transversely across both domains of DnaK and might act as a 'molecular crowbar' in wedging the two domains apart. This study sheds new light on how the DnaJ co-chaperone system structurally interacts with the primary Hsp70 system and suggests a possible mechanical model which explains how the allosteric machinery operates in the complex.
590 $a School code: 0127.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 $a University of Michigan. $3 777416
773 0 $t Dissertation Abstracts International $g 71-05B.
790 1 0 $a Zuiderweg, Erik R.P., $e advisor
790 $a 0127
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3406414