期刊
PHYSICAL REVIEW LETTERS
卷 104, 期 16, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.104.168105
关键词
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资金
- Leverhulme Trust [F10100A]
- EPSRC [EP/G026165/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/G026165/1] Funding Source: researchfish
The intrinsic property of proteins to form structural motifs such as alpha helices and beta sheets leads to a complex phase behavior in which proteins can assemble into various types of aggregates including crystals, liquidlike phases of unfolded or natively folded proteins, and amyloid fibrils. Here we use a coarse-grained protein model that enables us to perform Monte Carlo simulations for determining the phase diagram of natively folded alpha-helical and unfolded beta-sheet forming peptides. The simulations reveal the existence of various metastable peptide phases. The liquidlike phases are metastable with respect to the fibrillar phases, and there is a hierarchy of metastability.
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