期刊
PROTEIN SCIENCE
卷 13, 期 7, 页码 1939-1941出版社
WILEY
DOI: 10.1110/ps.04663504
关键词
amyloid; prion; aggregation rate; Alzheimer; protein deposit; mutation
The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of natural sequences. Furthermore, the results of the parameter-free model correlate well with the aggregation propensities of a set of peptides designed by computer simulations.
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