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Millisecond and submillisecond foldi...

Sabelko, Jobiah John.

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

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Millisecond and submillisecond folding kinetics of horse apomyoglobin and yeast phosphoglycerate kinase./
作者:	Sabelko, Jobiah John.
面頁冊數:	197 p.
附註:	Source: Dissertation Abstracts International, Volume: 61-10, Section: B, page: 5317.
Contained By:	Dissertation Abstracts International61-10B.
標題:	Inorganic chemistry. -
電子資源:	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.
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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
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792 $a 2000
793 $a English
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