東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Part I. Bacteriorhodopsin-related ma...

Stuart, Jeffrey Alan.

Linked to FindBook

Google Book

Amazon

博客來

Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site./
Author:	Stuart, Jeffrey Alan.
Description:	229 p.
Notes:	Source: Dissertation Abstracts International, Volume: 59-07, Section: B, page: 3291.
Contained By:	Dissertation Abstracts International59-07B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9842231
ISBN:	0591964732

Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site.
Stuart, Jeffrey Alan.

Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site. - 229 p.

Source: Dissertation Abstracts International, Volume: 59-07, Section: B, page: 3291.

Thesis (Ph.D.)--Syracuse University, 1998.

Part I. A protocol for the routine isolation and purification of purple membrane sheets containing the integral membrane protein, bacteriorhodopsin, was developed based upon modifications of protocols already in the literature. This simplified protocol is geared toward the facile isolation of protein for use in molecular electronic devices. Methods for the incorporation of bacteriorhodopsin into various polymeric supports were also developed, primarily in the form of dried films and hydrated cubes. This work also represents the first reported production of dried films of the deionized protein, or blue membrane.

ISBN: 0591964732Subjects--Topical Terms:

1019105
Biophysics, General.

Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site.
LDR:03478nmm 2200325 4500 001 1839264
005 20050627125012.5
008 130614s1998 eng d
020 $a 0591964732
035 $a (UnM)AAI9842231
035 $a AAI9842231
040 $a UnM $c UnM
100 1 $a Stuart, Jeffrey Alan. $3 1927661
245 1 0 $a Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site.
300 $a 229 p.
500 $a Source: Dissertation Abstracts International, Volume: 59-07, Section: B, page: 3291.
500 $a Adviser: Robert R. Birge.
502 $a Thesis (Ph.D.)--Syracuse University, 1998.
520 $a Part I. A protocol for the routine isolation and purification of purple membrane sheets containing the integral membrane protein, bacteriorhodopsin, was developed based upon modifications of protocols already in the literature. This simplified protocol is geared toward the facile isolation of protein for use in molecular electronic devices. Methods for the incorporation of bacteriorhodopsin into various polymeric supports were also developed, primarily in the form of dried films and hydrated cubes. This work also represents the first reported production of dried films of the deionized protein, or blue membrane.
520 $a Part II. An architecture for a volumetric optical memory based on the branched-photocycle of bacteriorhodopsin is presented. The branching reaction circumvents problems associated with destructive reading and writing processes and allows access to a stable, long-lived state, separated both temporally and energetically from the main photocycle, thereby making long-term data storage possible. The state, denoted as Q, can only be accessed by exposing the protein to two different wavelengths of light in the proper sequence, with the appropriate temporal separation (roughly 2 ms between the light pulses). The Q-state (assigned as a binary one) is transparent to both writing and reading processes, making them rigorously non-destructive. Bacteriorhodopsin in its resting state is assigned as a binary zero. A differential absorption reading process is used to determine the state of each volumetric binary element. Preliminary results are reported.
520 $a Part III. The nature of the chromophore binding site of light-adapted bacteriorhodopsin is analyzed by using all-valence electron MNDO and MNDO-PSDCI molecular orbital theory to interpret previously reported linear and nonlinear optical spectroscopic measurements. It is concluded that the unique two-photon properties of the chromophore are due in part to the electrostatic field associated with a Ca $\ sp{2+} $ ion near the chromophore. Four amino acids and three water molecules contribute significantly to the assigned chromophore adjacent calcium binding site, and two conformational minima are predicted. The cation binding site described is identified as the second high affinity binding site for calcium, and the chromophore binding site is, to a first approximation, positively charged.
590 $a School code: 0659.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Engineering, Materials Science. $3 1017759
650 4 $a Engineering, Chemical. $3 1018531
690 $a 0786
690 $a 0487
690 $a 0794
690 $a 0542
710 2 0 $a Syracuse University. $3 1017440
773 0 $t Dissertation Abstracts International $g 59-07B.
790 1 0 $a Birge, Robert R., $e advisor
790 $a 0659
791 $a Ph.D.
792 $a 1998
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9842231