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Single-molecule studies of calmoduli...

Slaughter, Brian D.

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Single-molecule studies of calmodulin conformation, dynamics, and folding.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Single-molecule studies of calmodulin conformation, dynamics, and folding./
作者:	Slaughter, Brian D.
面頁冊數:	233 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-08, Section: B, page: 4244.
Contained By:	Dissertation Abstracts International66-08B.
標題:	Chemistry, Physical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3185223
ISBN:	0542267993

Single-molecule studies of calmodulin conformation, dynamics, and folding.
Slaughter, Brian D.

Single-molecule studies of calmodulin conformation, dynamics, and folding. - 233 p.

Source: Dissertation Abstracts International, Volume: 66-08, Section: B, page: 4244.

Thesis (Ph.D.)--The University of Kansas, 2005.

Calmodulin (CaM) is a flexible, Ca2+ binding protein that interacts with diverse target enzymes, possibly due to its flexibility and structural diversity. In this dissertation, single-molecule and fluorescence methods are applied to diagnose the heterogeneity of CaM structure, the magnitude of sub-millisecond domain motion, and CaM-binding to a peptide target (C28W) that represents the CaM binding domain of the plasma membrane Ca2+ -ATPase (PMCA).

ISBN: 0542267993Subjects--Topical Terms:

560527
Chemistry, Physical.

Single-molecule studies of calmodulin conformation, dynamics, and folding.
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245 1 0 $a Single-molecule studies of calmodulin conformation, dynamics, and folding.
300 $a 233 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-08, Section: B, page: 4244.
500 $a Adviser: Carey K. Johnson.
502 $a Thesis (Ph.D.)--The University of Kansas, 2005.
520 $a Calmodulin (CaM) is a flexible, Ca2+ binding protein that interacts with diverse target enzymes, possibly due to its flexibility and structural diversity. In this dissertation, single-molecule and fluorescence methods are applied to diagnose the heterogeneity of CaM structure, the magnitude of sub-millisecond domain motion, and CaM-binding to a peptide target (C28W) that represents the CaM binding domain of the plasma membrane Ca2+ -ATPase (PMCA).
520 $a A doubly labeled CaM mutant, with fluorescence probes in opposing domains, CaM-T34C-T110C-AF488-TR, (CaM-DA) was used to examine intradomain motion using a combination of fluorescence correlation spectroscopy and fluorescence resonance energy transfer. Time constants of hundreds of microseconds and milliseconds were observed for intradomain motion. Burst-integrated FRET of freely diffusing CaM-DA molecules revealed that up to three conformations of CaM co-exist in solution. Their amplitudes vary as a function of Ca2+, ionic strength, pH, and oxidative modification of methionine residues. Single-molecule trajectories were analyzed to examine interchange among the sub-conformations.
520 $a The unfolding pathway of CaM was probed by examination of single-molecule distributions obtained at a range of urea concentrations. The distributions at intermediate urea concentrations could not be adequately described as a combination of native and denatured conformations, showing that at least a single unfolding intermediate exists for CaM. The changes in CaM conformation upon denaturation can be described by either a downhill folding model with a range of intermediate structures, or by the presence of a single unfolding intermediate that grows in amplitude upon denaturation.
520 $a The kinetics of interaction of CaM with C28W were studied by fluorescence quenching both in ensemble and single-molecule studies. A significant change in dissociation was observed for CaM that had been oxidized. A model was presented with two intermediate steps in the dissociation of CaM from C28W. The effect of oxidation on the kinetic rates was examined to lend insight into the reason for the reduced ability of oxidized-CaM to activate the PMCA.
520 $a In a computational study, the electronic transitions of the proline analogue indoline-2-carboxylic-acid were characterized by ab-initio and density functional techniques. The substitution of indoline for proline was examined by comparison of minimized blocked peptide conformations.
590 $a School code: 0099.
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650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
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710 2 0 $a The University of Kansas. $3 1288487
773 0 $t Dissertation Abstracts International $g 66-08B.
790 1 0 $a Johnson, Carey K., $e advisor
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791 $a Ph.D.
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