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Microsecond Dynamics of Enzymes: A S...

Akhterov, Maxim V.

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Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors./
作者:	Akhterov, Maxim V.
面頁冊數:	104 p.
附註:	Source: Dissertation Abstracts International, Volume: 77-03(E), Section: B.
Contained By:	Dissertation Abstracts International77-03B(E).
標題:	Nanotechnology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3727428
ISBN:	9781339125237

Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors.
Akhterov, Maxim V.

Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors. - 104 p.

Source: Dissertation Abstracts International, Volume: 77-03(E), Section: B.

Thesis (Ph.D.)--University of California, Irvine, 2015.

Molecular motions of proteins and their exibility determine conformational states required for enzyme catalysis, signal transduction, and protein-protein interactions. However, the mechanisms for protein transitions between conformational states are often poorly understood, especially in the milli- to microsecond ranges where conventional optical techniques and computational modeling are most limited. The goal of this work was to use single- walled carbon nanotube field-effect transistors (SWCNT-FET) as single-molecule biosensors to investigate microsecond dynamics of three enzymes. Low-noise electrical transport measurements were performed in a home-built electrochemical ow cell. To ensure that the output signal was free from external noise across a 200 kHz measurement bandwidth, parasitic capacitance was minimized by tightly integrating electrical components and constraining the liquid within a micro uidic channel. After attaching a single enzyme molecule to the SWCNT sidewall, dynamic changes of conductance through a SWCNT-FET reported con- formational motions of an enzyme with a 1.6 mus resolution. This technique was used to study microsecond dynamics of T4 Lysozyme, Klenow Fragment of DNA polymerase I (KF), and protein kinase A (PKA).

ISBN: 9781339125237Subjects--Topical Terms:

526235
Nanotechnology.

Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors.
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245 1 0 $a Microsecond Dynamics of Enzymes: A Single-Molecule Study Using Carbon Nanotube Transistors.
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500 $a Source: Dissertation Abstracts International, Volume: 77-03(E), Section: B.
500 $a Adviser: Philip G. Collins.
502 $a Thesis (Ph.D.)--University of California, Irvine, 2015.
520 $a Molecular motions of proteins and their exibility determine conformational states required for enzyme catalysis, signal transduction, and protein-protein interactions. However, the mechanisms for protein transitions between conformational states are often poorly understood, especially in the milli- to microsecond ranges where conventional optical techniques and computational modeling are most limited. The goal of this work was to use single- walled carbon nanotube field-effect transistors (SWCNT-FET) as single-molecule biosensors to investigate microsecond dynamics of three enzymes. Low-noise electrical transport measurements were performed in a home-built electrochemical ow cell. To ensure that the output signal was free from external noise across a 200 kHz measurement bandwidth, parasitic capacitance was minimized by tightly integrating electrical components and constraining the liquid within a micro uidic channel. After attaching a single enzyme molecule to the SWCNT sidewall, dynamic changes of conductance through a SWCNT-FET reported con- formational motions of an enzyme with a 1.6 mus resolution. This technique was used to study microsecond dynamics of T4 Lysozyme, Klenow Fragment of DNA polymerase I (KF), and protein kinase A (PKA).
520 $a Lysozyme closing and opening took on average 37mus. The distribution of transition dura- tions was independent of the lysozyme state: either catalytic or nonproductive. The observed symmetry in enzyme opening and closing suggests that substrate translocation occurs while lysozyme is closed. For KF and PKA, the microsecond resolution revealed that the transition duration was 3-5 mus for both enzymes, about ten times shorter than lysozyme. Additionally, the high-bandwidth recording of KF resolved fast non-catalytic closures. When KF was pro- cessing poly(dT)42 template KF stayed 2-3 times longer in a closed conformation than when it was replicating poly(dA)42. However, the open events of KF were 2-5 times shorter when it was processing poly(dT) 42 compared to poly(dA)42. The results demonstrate SWCNT-FET as a sensitive technique for studying conformational dynamics of biological molecules in the microsecond range.
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