Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will.

Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Research Abstract Details 

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Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Abstract Text:

Kevin Pagel,Sara C Wagner,Kerim Samedov,Hans von Berlepsch,Christoph ,Beate Koksch,

To potentially cure neurodegenerative diseases, we need to understand on a molecular level what triggers the complex folding mechanisms and shifts the equilibrium from functional to pathological isoforms of proteins. The development of small peptide models that can serve as tools for such studies is of paramount importance. We describe the de novo design and characterization of an alpha-helical coiled coil based model peptide that contains structural elements of both alpha-helical folding and beta-sheet formation. Three distinct secondary structures can be induced at will by adjustment of pH or concentration. Low concentrations at pH 4.0 yield globular particles of the unfolded peptide, while at the same pH, but at higher concentration, defined beta-sheet ribbons are formed. In contrast, at high concentrations and pH 7.4, the peptide forms highly ordered alpha-helical fibers. Thus, this system allows one to systematically study now the consequences of the interplay between peptide and protein primary structure and environmental factors for peptide and protein folding on a molecular level.

Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Publishing Authors By Initials

K Pagel,SC Wagner,K Samedov,H von Berlepsch,C ,B Koksch,

For similar proteins research abstracts see: proteins research

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Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 128

Page Numbers: 2196-7

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 22

MONTH: Feb

YEAR: 2006

Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will. Information

Substance Name: Proteins

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Grant and Affiliation Information for Random coils, beta-sheet ribbons, and alpha-helical fibers: one peptide adopting three different secondary structures at will.

AFFILIATION: Department of Chemistry and Biochemistry-Organic Chemistry, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, Germany.

Country: United States

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MEDLINETA: J Am Chem Soc

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