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

Millisecond and submillisecond foldi...

Sabelko, Jobiah John.

Linked to FindBook

Google Book

Amazon

博客來

Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase./
Author:	Sabelko, Jobiah John.
Description:	197 p.
Notes:	Source: Dissertation Abstracts International, Volume: 61-10, Section: B, page: 5317.
Contained By:	Dissertation Abstracts International61-10B.
Subject:	Inorganic chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9990127
ISBN:	9780599977433

Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase.
Sabelko, Jobiah John.

Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase. - 197 p.

Source: Dissertation Abstracts International, Volume: 61-10, Section: B, page: 5317.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.

The folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase were monitored over the 20 ns to 10 ms time scale using a temperature jump fluorescence instrument. Cold denatured protein was rapidly temperature jumped by a 10 ns laser pulse initiating refolding. A UV pulse train generated by a tripled Ti:Sapphire laser system was used to excite tryptophan fluorescence and both lifetime and dispersed fluorescence data were collected.

ISBN: 9780599977433Subjects--Topical Terms:

3173556
Inorganic chemistry.

Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase.
LDR:02954nmm a2200301 4500 001 2076133
005 20161101084249.5
008 170521s2000 ||||||||||||||||| ||eng d
020 $a 9780599977433
035 $a (MiAaPQ)AAI9990127
035 $a AAI9990127
040 $a MiAaPQ $c MiAaPQ
100 1 $a Sabelko, Jobiah John. $3 3191565
245 1 0 $a Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase.
300 $a 197 p.
500 $a Source: Dissertation Abstracts International, Volume: 61-10, Section: B, page: 5317.
500 $a Adviser: Martin Gruebele.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.
520 $a The folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase were monitored over the 20 ns to 10 ms time scale using a temperature jump fluorescence instrument. Cold denatured protein was rapidly temperature jumped by a 10 ns laser pulse initiating refolding. A UV pulse train generated by a tripled Ti:Sapphire laser system was used to excite tryptophan fluorescence and both lifetime and dispersed fluorescence data were collected.
520 $a Horse apomyoglobin contains two tryptophans in the A-helix which were used to probe the formation of the complete AGH hydrophobic core. The protein cold denatures resulting in solvation of the A-helix and disruption of the main AGH hydrophobic core but with considerable structure remaining in the G and H helices. Two distinct kinetic phases, a roughly 300 ns protective phase and 10 mus quenching phase, were observed. The initial ns phase was tentatively assigned to the formation of the A-helix. Furthermore, through a series of experiments on both the wild-type protein and several sperm whale apomyoglobin mutants, the microsecond phase was definitely assigned to the docking of the A and H helices. More specifically, this quenching phase is the result of tryptophan 14 (A-helix) moving into close proximity to M131 (H-helix).
520 $a Yeast phosphoglycerate kinase is a 415 residue dual domain protein which contains two tryptophans located in the C-terminus. PGK readily cold denatures yielding a state generally devoid of stable secondary structure. Kinetic measurements indicated the molecule collapses to a molten globule type state on the sub-ms time scale. Measurements on the wild-type protein and a series of single tryptophans mutants also showed vastly different folding times indicating considerable folding heterogeneity both interdomain and intradomain. Furthermore, by varying the final folding temperature and thereby adjusting the native bias, the kinetics were successfully tuned between type 1 (activated) and type 0 (downhill).
590 $a School code: 0090.
650 4 $a Inorganic chemistry. $3 3173556
650 4 $a Biochemistry. $3 518028
690 $a 0488
690 $a 0487
710 2 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 61-10B.
790 $a 0090
791 $a Ph.D.
792 $a 2000
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9990127