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Protein promoting vibrations: Subpi...

Mincer, Joshua S.

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Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis./
作者:	Mincer, Joshua S.
面頁冊數:	87 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-02, Section: B, page: 0761.
Contained By:	Dissertation Abstracts International66-02B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3163200
ISBN:	9780496970636

Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis.
Mincer, Joshua S.

Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis. - 87 p.

Source: Dissertation Abstracts International, Volume: 66-02, Section: B, page: 0761.

Thesis (Ph.D.)--Yeshiva University, 2006.

The coupling of protein dynamics to enzymatic reactions is explored, specifically with reference to subpicosecond quasioscillatory motions, protein promoting vibrations (PPVS), that dynamically modulate the reaction potential energy surface on the same timescale as the reaction barrier passage itself. Computational algorithms to study these motions are presented. The first identifies a PPV in a specific enzymatic reaction, if it exists. The second identifies protein residues, the motions of which drive the PPV. Application to the enzyme horse liver alcohol dehydrogenase (HLADH) explains experimental mutagenesis studies and makes predictions for the many residues as yet not studied. PPV contribution to rate enhancement in HLADH is considered in light of these studies.

ISBN: 9780496970636Subjects--Topical Terms:

1019105
Biophysics, General.

Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis.
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245 1 0 $a Protein promoting vibrations: Subpicosecond enzyme dynamics and catalysis.
300 $a 87 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-02, Section: B, page: 0761.
500 $a Adviser: Steven D. Schwartz.
502 $a Thesis (Ph.D.)--Yeshiva University, 2006.
520 $a The coupling of protein dynamics to enzymatic reactions is explored, specifically with reference to subpicosecond quasioscillatory motions, protein promoting vibrations (PPVS), that dynamically modulate the reaction potential energy surface on the same timescale as the reaction barrier passage itself. Computational algorithms to study these motions are presented. The first identifies a PPV in a specific enzymatic reaction, if it exists. The second identifies protein residues, the motions of which drive the PPV. Application to the enzyme horse liver alcohol dehydrogenase (HLADH) explains experimental mutagenesis studies and makes predictions for the many residues as yet not studied. PPV contribution to rate enhancement in HLADH is considered in light of these studies.
520 $a The reaction rate theory developed by Antoniou and Schwartz is generalized to include an electron coordinate, allowing for the modeling of enzymes that catalyze proton-coupled electron transfer (PCET) reactions. Model system calculations yield kinetic parameters and primary HID kinetic isotope effects (KIEs) in qualitative agreement with experiment and allow for insights into KIE temperature dependence as well as KIE masking when these reactions are coupled to a PPV.
520 $a Finally, PPV coupling to bond cleavage reactions in general is investigated in the specific context of PPV coupling to reaction center electron density in the enzyme purine nucleoside phosphorylase.
590 $a School code: 0266.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Physics, Molecular. $3 1018648
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