dimer formation enhances structural differences between amyloid β-protein (1–40) and (1–42) an explicit-solvent molecular dynamics study二聚体的形成增强了淀粉样蛋白结构差异β-protein第1 - 40()和(1-42)explicit-solvent分子动力学研究.pdfVIP

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2017-09-12 发布于上海
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dimer formation enhances structural differences between amyloid β-protein (1–40) and (1–42) an explicit-solvent molecular dynamics study二聚体的形成增强了淀粉样蛋白结构差异β-protein第1 - 40()和(1-42)explicit-solvent分子动力学研究.pdf

dimer formation enhances structural differences between amyloid β-protein (1–40) and (1–42) an explicit-solvent molecular dynamics study二聚体的形成增强了淀粉样蛋白结构差异β-protein第1 - 40()和(1-42)explicit-solvent分子动力学研究

Dimer Formation Enhances Structural Differences between Amyloid b-Protein (1–40) and (1–42): An Explicit-Solvent Molecular Dynamics Study Bogdan Barz, Brigita Urbanc* Physics Department, Drexel University, Philadelphia, Pennsylvania, United States of America Abstract Amyloid b-protein (Ab) is central to the pathology of Alzheimer’s disease. A 5% difference in the primary structure of the two predominant alloforms, Ab1{40 and Ab1{42 , results in distinct assembly pathways and toxicity properties. Discrete molecular dynamics (DMD) studies of Ab

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dimer formation enhances structural differences between amyloid β-protein (1–40) and (1–42) an explicit-solvent molecular dynamics study二聚体的形成增强了淀粉样蛋白结构差异β-protein第1 - 40()和(1-42)explicit-solvent分子动力学研究.pdfVIP