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Role of loop motions in enzyme catal...

Reddish, Michael J.

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Role of loop motions in enzyme catalysis.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Role of loop motions in enzyme catalysis./
Author:	Reddish, Michael J.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2015,
Description:	167 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-04(E), Section: B.
Contained By:	Dissertation Abstracts International77-04B(E).
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3736855
ISBN:	9781339258140

Role of loop motions in enzyme catalysis.
Reddish, Michael J.

Role of loop motions in enzyme catalysis. - Ann Arbor : ProQuest Dissertations & Theses, 2015 - 167 p.

Source: Dissertation Abstracts International, Volume: 77-04(E), Section: B.

Thesis (Ph.D.)--Emory University, 2015.

This item is not available from ProQuest Dissertations & Theses.

Enzymes are important paradigms for studying catalysis. They are highly effective at increasing reaction rates with strong substrate specificity while operating at moderate conditions. Despite extensive characterization over the last century, the actual process of enzyme catalysis is not well understood. Simple investigations relating protein structure to function fail. These investigations tend to fail because they consider the enzyme as a static structure, ignoring the fact that proteins are known to exist as dynamic structures. Protein dynamics can occur on the order of small vibrations or large conformational rearrangements. One such dynamic feature common to many enzymes is the movement of loops throughout the catalytic cycle. Loop motion has typically been ill-studied due to experimental limitations in studying the microsecond to millisecond timescale of these motions. In this dissertation, we develop two complimentary approaches to studying this timescale, temperature-jump spectroscopy and microfluidic fast-mixing. We then apply these methods to study three different model enzyme systems: lactate dehydrogenase, dihydrofolate reductase, and purine nucleoside phosphorylase. By studying these enzymes we are able to establish that loop motions contribute a significant amount of heterogeneity to enzyme reactions requiring a reaction landscape, as opposed to the traditional reaction pathway, to fully describe the system. We then briefly discuss the implications of this approach for understanding enzymes in general.

ISBN: 9781339258140Subjects--Topical Terms:

518028
Biochemistry.

Role of loop motions in enzyme catalysis.
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245 1 0 $a Role of loop motions in enzyme catalysis.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2015
300 $a 167 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-04(E), Section: B.
500 $a Adviser: Brian Dyer.
502 $a Thesis (Ph.D.)--Emory University, 2015.
506 $a This item is not available from ProQuest Dissertations & Theses.
520 $a Enzymes are important paradigms for studying catalysis. They are highly effective at increasing reaction rates with strong substrate specificity while operating at moderate conditions. Despite extensive characterization over the last century, the actual process of enzyme catalysis is not well understood. Simple investigations relating protein structure to function fail. These investigations tend to fail because they consider the enzyme as a static structure, ignoring the fact that proteins are known to exist as dynamic structures. Protein dynamics can occur on the order of small vibrations or large conformational rearrangements. One such dynamic feature common to many enzymes is the movement of loops throughout the catalytic cycle. Loop motion has typically been ill-studied due to experimental limitations in studying the microsecond to millisecond timescale of these motions. In this dissertation, we develop two complimentary approaches to studying this timescale, temperature-jump spectroscopy and microfluidic fast-mixing. We then apply these methods to study three different model enzyme systems: lactate dehydrogenase, dihydrofolate reductase, and purine nucleoside phosphorylase. By studying these enzymes we are able to establish that loop motions contribute a significant amount of heterogeneity to enzyme reactions requiring a reaction landscape, as opposed to the traditional reaction pathway, to fully describe the system. We then briefly discuss the implications of this approach for understanding enzymes in general.
590 $a School code: 0665.
650 4 $a Biochemistry. $3 518028
650 4 $a Physical chemistry. $3 1981412
650 4 $a Biophysics. $3 518360
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710 2 $a Emory University. $b Chemistry. $3 3281152
773 0 $t Dissertation Abstracts International $g 77-04B(E).
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