Protein aggregation processes: In search of the mechanism.

Protein aggregation processes: In search of the mechanism. Research Abstract Details 

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Protein aggregation processes: In search of the mechanism. Abstract Text:

Carl Frieden,Carl Frieden,

Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered-collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and 19F-NMR methods are discussed.

Protein aggregation processes: In search of the mechanism. Publishing Authors By Initials

C Frieden,C Frieden,

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Protein aggregation processes: In search of the mechanism. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Protein science : a publication of the Protein Soc

VOLUME: 16

Page Numbers: 2334-44

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 26

MONTH: Nov

YEAR: 2007

Protein aggregation processes: In search of the mechanism. Information

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LANGUAGE: eng

NlmUniqueID: 9211750

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Grant and Affiliation Information for Protein aggregation processes: In search of the mechanism.

AFFILIATION: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA. frieden@biochem.wustl.edu

Country: United States

AGENCY: United States NIDDK

GRANT: DK 13332

ACRONYM: DK

MEDLINETA: Protein Sci

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