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The Coupling of Conformational Excha...

Whittier, Sean Kenneth.

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The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases./
作者:	Whittier, Sean Kenneth.
面頁冊數:	145 p.
附註:	Source: Dissertation Abstracts International, Volume: 75-09(E), Section: B.
Contained By:	Dissertation Abstracts International75-09B(E).
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3580901
ISBN:	9781321063660

The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases.
Whittier, Sean Kenneth.

The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases. - 145 p.

Source: Dissertation Abstracts International, Volume: 75-09(E), Section: B.

Thesis (Ph.D.)--Yale University, 2014.

This item must not be sold to any third party vendors.

Many studies have shown that dynamic protein motions play a role in the enzyme catalytic cycle. However, while motions have been implicated in events prior to and subsequent to enzyme chemistry, very few studies have found such an involvement in the chemical step itself. To address this issue, active site loop motions in two orthologous protein tyrosine phosphatases (PTPs) have been quantified using solution NMR relaxation dispersion experiments. These PTPs, PTP1B and YopH, are identical in chemical mechanism and active site structure, yet they have drastically different chemical rates. The results presented in this show that in both enzymes an active site loop containing the catalytic acid closes into its catalytically competent conformation at rates that are nearly identical to the rate of phosphotyrosine cleavage. This result explains the differing chemical kinetics of PTP1B and YopH, and suggests that loop closure is coupled to leaving group protonation in protein tyrosine phosphatases.

ISBN: 9781321063660Subjects--Topical Terms:

518360
Biophysics.

The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases.
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245 1 4 $a The Coupling of Conformational Exchange Motions and Phosphoryl Transfer in Protein Tyrosine Phosphatases.
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500 $a Source: Dissertation Abstracts International, Volume: 75-09(E), Section: B.
500 $a Adviser: Joseph Patrick Loria.
502 $a Thesis (Ph.D.)--Yale University, 2014.
506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a Many studies have shown that dynamic protein motions play a role in the enzyme catalytic cycle. However, while motions have been implicated in events prior to and subsequent to enzyme chemistry, very few studies have found such an involvement in the chemical step itself. To address this issue, active site loop motions in two orthologous protein tyrosine phosphatases (PTPs) have been quantified using solution NMR relaxation dispersion experiments. These PTPs, PTP1B and YopH, are identical in chemical mechanism and active site structure, yet they have drastically different chemical rates. The results presented in this show that in both enzymes an active site loop containing the catalytic acid closes into its catalytically competent conformation at rates that are nearly identical to the rate of phosphotyrosine cleavage. This result explains the differing chemical kinetics of PTP1B and YopH, and suggests that loop closure is coupled to leaving group protonation in protein tyrosine phosphatases.
590 $a School code: 0265.
650 4 $a Biophysics. $3 518360
650 4 $a Biochemistry. $3 518028
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710 2 $a Yale University. $3 515640
773 0 $t Dissertation Abstracts International $g 75-09B(E).
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792 $a 2014
793 $a English
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