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  5. The structural character of α-syn12 dimer in explicit water molecules by replica-exchange molecular

The structural character of α-syn12 dimer in explicit water molecules by replica-exchange molecular

来源 :第六届全国生物信息学与系统生物学学术大会暨国际生物信息学前沿研讨会 | 被引量 : 0次 | 上传用户：liyizhong1235
【摘 要】
：
Background: The typical symptom of Parkinsons disease is the presence of α-synuclein aggregates in the form of β-structure that can be soluble or insoluble.The N-terminal region (residues 1-60) of α-s
【作 者】
：
曹赞霞 刘磊 王吉华 
【机 构】
：
山东省功能大分子生物物理重点实验室,物理系,德州学院,德州,253023 山东省功能大分子生物物理
【出 处】
：
第六届全国生物信息学与系统生物学学术大会暨国际生物信息学前沿研讨会
【发表日期】
：
2014年4期
【关键词】
：
Parkinson's disease α-syn12 polypeptide dimer structural ensemble transform 
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　　Background: The typical symptom of Parkinsons disease is the presence of α-synuclein aggregates in the form of β-structure that can be soluble or insoluble.The N-terminal region (residues 1-60) of α-synuclein plays a key role in the formation of α-synuclein assemblies.Furthermore, the dimerization is important for α-synuclein conformational transition and aggregation.However, it is difficult to simulate 120 residues in explicit water sufficiency.In this study, we selected N-terminal 12 residues peptide of α-synuclein (α-syn12).
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