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Genetic optimization and time-resolv...

Koscielecki, Jeremy F.

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Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants./
Author:	Koscielecki, Jeremy F.
Description:	173 p.
Notes:	Adviser: Robert R. Birge.
Contained By:	Dissertation Abstracts International68-01B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249544

Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants.
Koscielecki, Jeremy F.

Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants. - 173 p.

Adviser: Robert R. Birge.

Thesis (Ph.D.)--University of Connecticut, 2006.

The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Halobacterium salinarum and can be applied to a number of biophotonic devices. Genetic changes made to BR that affect proton pumping are visualized through spectral changes to the photocycle. Changes that affect the M and O state photokinetics are promising candidates for use in a number of biophotonic devices, The spectrokinetic properties of over 3,000 variant forms of BR, encompassing 96% of the protein structure, are studied by using time-resolved UV/Visible spectroscopy at three wavelengths: 412 nm, 658 nm and 650 nm. Protein variants with altered photocycles are further studied by using time-resolved Fourier transform infrared (FT-IR) spectroscopy and Fourier transform terahertz (FT-THz) spectroscopy. Protein variants are constructed by using site-directed and semi-random mutagenesis techniques. The results endorse the use of semi-random mutagenesis combined with spectroscopic methods to identify protein variants with novel photokinetic properties.Subjects--Topical Terms:

586156
Chemistry, Analytical.

Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants.
LDR:01926nam 2200265 a 45 001 970837
005 20110921
008 110921s2006 eng d
035 $a (UMI)AAI3249544
035 $a AAI3249544
040 $a UMI $c UMI
100 1 $a Koscielecki, Jeremy F. $3 1294877
245 1 0 $a Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants.
300 $a 173 p.
500 $a Adviser: Robert R. Birge.
500 $a Source: Dissertation Abstracts International, Volume: 68-01, Section: B, page: 0274.
502 $a Thesis (Ph.D.)--University of Connecticut, 2006.
520 $a The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Halobacterium salinarum and can be applied to a number of biophotonic devices. Genetic changes made to BR that affect proton pumping are visualized through spectral changes to the photocycle. Changes that affect the M and O state photokinetics are promising candidates for use in a number of biophotonic devices, The spectrokinetic properties of over 3,000 variant forms of BR, encompassing 96% of the protein structure, are studied by using time-resolved UV/Visible spectroscopy at three wavelengths: 412 nm, 658 nm and 650 nm. Protein variants with altered photocycles are further studied by using time-resolved Fourier transform infrared (FT-IR) spectroscopy and Fourier transform terahertz (FT-THz) spectroscopy. Protein variants are constructed by using site-directed and semi-random mutagenesis techniques. The results endorse the use of semi-random mutagenesis combined with spectroscopic methods to identify protein variants with novel photokinetic properties.
590 $a School code: 0056.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0486
690 $a 0487
710 2 0 $a University of Connecticut. $3 1017435
773 0 $t Dissertation Abstracts International $g 68-01B.
790 $a 0056
790 1 0 $a Birge, Robert R., $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249544