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An atomic force microscopy investiga...

Hoskins, Jessica L.

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An atomic force microscopy investigation of insulin amyloid fibril formation.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	An atomic force microscopy investigation of insulin amyloid fibril formation./
作者:	Hoskins, Jessica L.
面頁冊數:	55 p.
附註:	Source: Masters Abstracts International, Volume: 43-01, page: 0169.
Contained By:	Masters Abstracts International43-01.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1421515
ISBN:	0496262602

An atomic force microscopy investigation of insulin amyloid fibril formation.
Hoskins, Jessica L.

An atomic force microscopy investigation of insulin amyloid fibril formation. - 55 p.

Source: Masters Abstracts International, Volume: 43-01, page: 0169.

Thesis (M.S.)--California State University, Long Beach, 2004.

The aggregation of amyloid fibrils in the body is a characteristic pathology of a number of debilitating diseases, including Alzheimer's disease, Parkinson's disease, and Type II diabetes. Under certain environmental conditions, normally inert proteins will self-aggregate to form elongated amyloid fibril plaques. Understanding the aggregation of these types of fibrils may be the key to opening the door for new therapeutic techniques. Insulin amyloid fibrils are grown in vitro under acidic conditions with stirring and heating. Appropriate sample preparation methods are devised for an atomic force microscopy investigation. Atomic force microscopy techniques are used to determine the morphology of fibrils at different times during the incubation process, and trends in the physical structure of fibrils are determined. Future research directions, including force mapping and scanning in fluid, are discussed.

ISBN: 0496262602Subjects--Topical Terms:

1019105
Biophysics, General.

An atomic force microscopy investigation of insulin amyloid fibril formation.
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500 $a Source: Masters Abstracts International, Volume: 43-01, page: 0169.
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502 $a Thesis (M.S.)--California State University, Long Beach, 2004.
520 $a The aggregation of amyloid fibrils in the body is a characteristic pathology of a number of debilitating diseases, including Alzheimer's disease, Parkinson's disease, and Type II diabetes. Under certain environmental conditions, normally inert proteins will self-aggregate to form elongated amyloid fibril plaques. Understanding the aggregation of these types of fibrils may be the key to opening the door for new therapeutic techniques. Insulin amyloid fibrils are grown in vitro under acidic conditions with stirring and heating. Appropriate sample preparation methods are devised for an atomic force microscopy investigation. Atomic force microscopy techniques are used to determine the morphology of fibrils at different times during the incubation process, and trends in the physical structure of fibrils are determined. Future research directions, including force mapping and scanning in fluid, are discussed.
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