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Single-molecule investigation of rep...

Lu, Hailong.

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Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase./
作者:	Lu, Hailong.
面頁冊數:	176 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4044.
Contained By:	Dissertation Abstracts International65-08B.
標題:	Chemistry, Physical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3144049
ISBN:	0496027018

Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase.
Lu, Hailong.

Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase. - 176 p.

Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4044.

Thesis (Ph.D.)--The University of New Mexico, 2004.

The motor-like activity of Human Immunodeficiency Virus Reverse Transcriptase (HIV RT) was studied using single-molecule Atomic Force Microscopy (AFM) and single-molecule fluorescence techniques.

ISBN: 0496027018Subjects--Topical Terms:

560527
Chemistry, Physical.

Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase.
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245 1 0 $a Single-molecule investigation of replication by human immunodeficiency virus reverse transcriptase.
300 $a 176 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-08, Section: B, page: 4044.
500 $a Adviser: David J. Keller.
502 $a Thesis (Ph.D.)--The University of New Mexico, 2004.
520 $a The motor-like activity of Human Immunodeficiency Virus Reverse Transcriptase (HIV RT) was studied using single-molecule Atomic Force Microscopy (AFM) and single-molecule fluorescence techniques.
520 $a We modified an existing AFM to work in force-mode. New software was also written, in LabViewRTM, to operate the custom-built AFM. This instrument is able to detect pN of force with time-resolution of tens of milliseconds. This instruments was used to study the effects of external forces on the DNA directed DNA polymerization (DDDP) activity of HIV RT. In these experiments, the HIV RT molecules were attached to the tip of an AFM cantilever and the DNA primer/template molecules were attached to a cover glass. When the tip and the substrate were brought close, HIV RT began to polymerize a DNA primer/template. The forces and motions in this process were recorded by the AFM. By following this process, the effects of an external force on the HIV RT polymerization were studied.
520 $a The DDDP activity of HIV RT at zero force was studied using single-molecule fluorescence techniques. In these experiments, the HIV RT molecules were adsorbed on a cover-glass substrate. DNA primer/template molecules and NTP were present in the surrounding solution. When HIV RT began to polymerize the DNA primer/template, it incorporated fluorescently labeled NIP into the DNA primer/template, which was then excited by an evanescent field formed by total internal reflection. By analyzing the statistics of the fluorescence "on" time for the polymerization process, the polymerization rates for the HIV RT at zero loading force were obtained.
520 $a The results from these two single-molecule experiments show that at low load forces the polymerase is mechanically slowed, while at high forces (approximately 15 pN) it stalls. From the data of estimated polymerase turnover velocity versus load force, an approximate force-velocity curve was constructed. The shape of the curve suggests that load force strongly slows down the rate-limiting step of the polymerase turnover cycle, and that the combined effects of load on all steps involves an effective motion of about 16 A. Earlier results from pre-steady-state kinetics experiments have identified the rate-limiting step as the closing of the fingers domain to form a tight catalytic complex. Together these findings indicate that the closing of the fingers domain of the HIV RT is a major force-generating step for HIV RT and, by extension, for all DNA polymerase machines.
590 $a School code: 0142.
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650 4 $a Biophysics, General. $3 1019105
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710 2 0 $a The University of New Mexico. $3 1018024
773 0 $t Dissertation Abstracts International $g 65-08B.
790 1 0 $a Keller, David J., $e advisor
790 $a 0142
791 $a Ph.D.
792 $a 2004
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