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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.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants./
作者:	Koscielecki, Jeremy F.
面頁冊數:	173 p.
附註:	Adviser: Robert R. Birge.
Contained By:	Dissertation Abstracts International68-01B.
標題:	Chemistry, Analytical. -
電子資源:	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.
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245 1 0 $a Genetic optimization and time-resolved spectroscopy of bacteriorhodopsin variants.
300 $a 173 p.
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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.
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650 4 $a Chemistry, Biochemistry. $3 1017722
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