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X-ray and atomic force microscopy st...

Lucas, Robert Wayne.

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X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus./
作者:	Lucas, Robert Wayne.
面頁冊數:	166 p.
附註:	Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1175.
Contained By:	Dissertation Abstracts International63-03B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048056
ISBN:	0493623361

X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus.
Lucas, Robert Wayne.

X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus. - 166 p.

Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1175.

Thesis (Ph.D.)--University of California, Irvine, 2002.

The three dimensional structure of Tomato Aspermy virus (TAV) has been solved by X-ray crystallography using 33 crystals at room temperature. Large amphipathic helices were observed near the n-termini loosely connected to the beta-barrels of the protein subunits by hinge regions of six amino acids. Segments of about three nucleotides of ordered RNA interact with the capsid protein, primarily through arginine residues, at the interfaces between the A and B subunits. Cys 106, which is a conserved arginine residue in related viruses, forms a disulfide bond with cys 64 that is unique amongst wild type T3 viruses. A putative Mg++ ions lies at the quasi-threefold axis coordinated by three glutamate side chains contributing to virion stability.

ISBN: 0493623361Subjects--Topical Terms:

1017719
Biology, Molecular.

X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus.
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245 1 0 $a X-ray and atomic force microscopy structure studies of the plant viruses brome mosaic virus, tomato aspermy virus and turnip yellow mosaic virus.
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500 $a Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1175.
500 $a Chair: Alexander McPherson.
502 $a Thesis (Ph.D.)--University of California, Irvine, 2002.
520 $a The three dimensional structure of Tomato Aspermy virus (TAV) has been solved by X-ray crystallography using 33 crystals at room temperature. Large amphipathic helices were observed near the n-termini loosely connected to the beta-barrels of the protein subunits by hinge regions of six amino acids. Segments of about three nucleotides of ordered RNA interact with the capsid protein, primarily through arginine residues, at the interfaces between the A and B subunits. Cys 106, which is a conserved arginine residue in related viruses, forms a disulfide bond with cys 64 that is unique amongst wild type T3 viruses. A putative Mg++ ions lies at the quasi-threefold axis coordinated by three glutamate side chains contributing to virion stability.
520 $a Brome Mosaic Virus (BMV), a T = 3 icosahedral plant virus, can be dissociated into coat protein subunits and subunit oligomers at pH 7.5 in the presence of concentrated salts. During salt dissociation some unknown protease cleaves the subunits between amino acids 35 and 36. The truncated protein subunits will then reorganize into crystalline lattice T = 1 icosahedral particles in sodium malonate. Atomic force microscopy and quasi-elastic light scattering were used to study these crystals.
520 $a The structure of native BMV was determined from a single rhombohedral crystal by X-ray diffraction, and refined to 3.4 A resolution. Putative Mg++ ions at the quasi threefold and fivefold axis were observed and are believed to play a role in maintaining capsid stability. PEG was modeled into density that is contiguous with the viral interior on the threefold axis in a pore of about 6 A diameter.
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