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Structure of partially denatured bac...

Krishnamani, Venkatramanan.

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Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding./
Author:	Krishnamani, Venkatramanan.
Description:	120 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-10, Section: B, page: 5988.
Contained By:	Dissertation Abstracts International71-10B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3422155
ISBN:	9781124208350

Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding.
Krishnamani, Venkatramanan.

Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding. - 120 p.

Source: Dissertation Abstracts International, Volume: 71-10, Section: B, page: 5988.

Thesis (Ph.D.)--University of California, Irvine, 2010.

The partially denatured state of bacteriorhodopsin (bR), a model hepta-helical integral membrane protein that acts as a proton pump in the membranes of Halobacterium salinarum, in SDS micelles was studied to understand the sequence dependent structural perturbations. Two-frequency pulsed electron paramagnetic resonance (EPR) (double electron-electron spin resonance, DEER) investigation combined with molecular dynamics (MD) of denaturation of individual helices of bR was used in an attempt to unravel the structural details of bR in sodium dodecyl sulfate (SDS) micelles. The results from the DEER experiments reveal a discrete heterogeneous ensemble of structures of bR in the detergent. The MD simulations show the role of charged residues in unfolding and the partitioning preference of the helices in SDS micelles. The refolding kinetics from this partially denatured starting state to a functional regenerated state using stopped flow continuous wave EPR measurements revealed that the secondary structure formation is faster than 140 msec and further helix association events followed a two step process. Majority of the structural changes happen before the functional recovery of the protein in the first step with a time constant of 3-5 sec followed by minor structural changes occurring in concert with the retinal chromophore recovery with varying association time constants for each helix pair.

ISBN: 9781124208350Subjects--Topical Terms:

1019105
Biophysics, General.

Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding.
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020 $a 9781124208350
035 $a (UMI)AAI3422155
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100 1 $a Krishnamani, Venkatramanan. $3 1678234
245 1 0 $a Structure of partially denatured bacteriorhodopsin in detergent micelles and structural changes during its refolding.
300 $a 120 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-10, Section: B, page: 5988.
500 $a Adviser: Janos K. Lanyi.
502 $a Thesis (Ph.D.)--University of California, Irvine, 2010.
520 $a The partially denatured state of bacteriorhodopsin (bR), a model hepta-helical integral membrane protein that acts as a proton pump in the membranes of Halobacterium salinarum, in SDS micelles was studied to understand the sequence dependent structural perturbations. Two-frequency pulsed electron paramagnetic resonance (EPR) (double electron-electron spin resonance, DEER) investigation combined with molecular dynamics (MD) of denaturation of individual helices of bR was used in an attempt to unravel the structural details of bR in sodium dodecyl sulfate (SDS) micelles. The results from the DEER experiments reveal a discrete heterogeneous ensemble of structures of bR in the detergent. The MD simulations show the role of charged residues in unfolding and the partitioning preference of the helices in SDS micelles. The refolding kinetics from this partially denatured starting state to a functional regenerated state using stopped flow continuous wave EPR measurements revealed that the secondary structure formation is faster than 140 msec and further helix association events followed a two step process. Majority of the structural changes happen before the functional recovery of the protein in the first step with a time constant of 3-5 sec followed by minor structural changes occurring in concert with the retinal chromophore recovery with varying association time constants for each helix pair.
590 $a School code: 0030.
650 4 $a Biophysics, General. $3 1019105
690 $a 0786
710 2 $a University of California, Irvine. $b Biological Sciences - Ph.D. $3 1675588
773 0 $t Dissertation Abstracts International $g 71-10B.
790 1 0 $a Lanyi, Janos K., $e advisor
790 1 0 $a White, Stephen H. $e committee member
790 1 0 $a Haigler, Harry H. $e committee member
790 1 0 $a Luo, Ray $e committee member
790 $a 0030
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3422155