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Dynamics of biomolecular fibers.

Plewa, Joseph Steven.

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Dynamics of biomolecular fibers.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Dynamics of biomolecular fibers./
作者:	Plewa, Joseph Steven.
面頁冊數:	133 p.
附註:	Adviser: David Grier.
Contained By:	Dissertation Abstracts International62-10B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3029527
ISBN:	049341939X

Dynamics of biomolecular fibers.
Plewa, Joseph Steven.

Dynamics of biomolecular fibers. - 133 p.

Adviser: David Grier.

Thesis (Ph.D.)--The University of Chicago, 2001.

We describe theoretical and experimental investigations of biomolecular dynamics. First we demonstrate a lattice Monte Carlo simulation which conserves a topological linking number by forbidding moves through cis conformations. Unlike previous models that conserve linking number, our simulated ring chains have flexibility and the scaling properties of a lattice self-avoiding walk. A linking number of order 0.2 per bond leads to an eight-percent reduction of the radius for 128-bond chains. For ring chains evolving without the conservation of linking number, we demonstrate a substantial anti-correlation between the twist and writhe variables whose sum yields the linking number. We raise the possibility that our observed anti-correlations may have counterparts in biomolecules like DNA.

ISBN: 049341939XSubjects--Topical Terms:

1019105
Biophysics, General.

Dynamics of biomolecular fibers.
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245 1 0 $a Dynamics of biomolecular fibers.
300 $a 133 p.
500 $a Adviser: David Grier.
500 $a Source: Dissertation Abstracts International, Volume: 62-10, Section: B, page: 4600.
502 $a Thesis (Ph.D.)--The University of Chicago, 2001.
520 $a We describe theoretical and experimental investigations of biomolecular dynamics. First we demonstrate a lattice Monte Carlo simulation which conserves a topological linking number by forbidding moves through cis conformations. Unlike previous models that conserve linking number, our simulated ring chains have flexibility and the scaling properties of a lattice self-avoiding walk. A linking number of order 0.2 per bond leads to an eight-percent reduction of the radius for 128-bond chains. For ring chains evolving without the conservation of linking number, we demonstrate a substantial anti-correlation between the twist and writhe variables whose sum yields the linking number. We raise the possibility that our observed anti-correlations may have counterparts in biomolecules like DNA.
520 $a We then discuss experiments which combine digital video microscopy and total-internal reflection microscopy (TIRM) in a single technique (3DTIRM) which allows accurate measurement of the three-dimensional location of microscopic particles. We compare two methods for measuring the total scattered light intensity. The first method uses an external photodiode as in conventional TIRM, the second uses only digitized video frames. We employ 3DTIRM to study the material properties of yeast amyloid fibers, consisting of aggregates of Sup35 protein. We attach one end of a biotin-labelled fiber to a glass slide and the other end to a streptavidin-coated 4.4 μm polystyrene sphere. By studying the equilibrium fluctuations of the colloidal sphere, we determine the elastic modulus of the fibers, and set limits on the twisting persistence length.
590 $a School code: 0330.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Physics, Condensed Matter. $3 1018743
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710 2 0 $a The University of Chicago. $3 1017389
773 0 $t Dissertation Abstracts International $g 62-10B.
790 $a 0330
790 1 0 $a Grier, David, $e advisor
791 $a Ph.D.
792 $a 2001
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