Capturing the interaction potential of amyloidogenic proteins.

Capturing the interaction potential of amyloidogenic proteins. Research Abstract Details 

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Capturing the interaction potential of amyloidogenic proteins. Abstract Text:

Nadeem Javid,Karsten Vogtt,Christina Krywka,Metin Tolan,Roland Winter,Nadeem Javid,Karsten Vogtt,Christina Krywka,Metin Tolan,Roland Winter,

Experimentally derived static structure factors obtained for the aggregation-prone protein insulin were analyzed with a statistical mechanical model based on the Derjaguin-Landau-Verwey-Overbeek potential. The data reveal that the protein self-assembles into equilibrium clusters already at low concentrations. Furthermore, striking differences regarding interaction forces between aggregation-prone proteins such as insulin in the preaggregated regime and natively stable globular proteins are found.

Capturing the interaction potential of amyloidogenic proteins. Publishing Authors By Initials

N Javid,K Vogtt,C Krywka,M Tolan,R Winter,N Javid,K Vogtt,C Krywka,M Tolan,R Winter,

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Capturing the interaction potential of amyloidogenic proteins. Journal Published:

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

Journal: Physical review letters

VOLUME: 99

Page Numbers: 028101

Journal Abbreviation: Phys. Rev. Lett.

ISSN: 0031-9007

DAY: 13

MONTH: 07

YEAR: 2007

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LANGUAGE: eng

NlmUniqueID: 401141

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AFFILIATION: University of Dortmund, Department of Chemistry, Physical Chemistry I-Biophysical Chemistry, Otto-Hahn Strasse 6, D-44227 Dortmund, Germany.

Country: United States

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MEDLINETA: Phys Rev Lett

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