期刊
PHYSICAL REVIEW LETTERS
卷 99, 期 2, 页码 -出版社
AMERICAN PHYSICAL SOC
DOI: 10.1103/PhysRevLett.99.028101
关键词
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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.
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