欢迎您!
东篱公司
退出
申报数据库
申报指南
立项数据库
成果数据库
期刊论文
会议论文
著 作
专 利
项目获奖数据库
位置:
成果数据库
>
期刊
> 期刊详情页
Distinct Helix Propensities and Membrane Interactions of Human and Rat IAPP1-19 Monomers in Anionic
期刊名称:Journal of Physical Chemistry B
时间:2015.2.26
页码:3366-3376
相关项目:多肽自组装的多尺度分子模拟研究(四)
作者:
Cong Guo|Sebastien Cote|Normand Mousseau|Guanghong Wei|
同期刊论文项目
多肽自组装的多尺度分子模拟研究(四)
期刊论文 24
同项目期刊论文
Aβ(16–22) Peptides Can Assemble into Ordered β-Barrels and Bilayer &
Influence of Au nanoparticles on the aggregation of amyloid-beta-(25-35) peptides.
Conformational distribution and alpha-helix to beta-sheet transition of human amylin fragment dimer.
Abeta(16-22) peptides can assemble into ordered beta-barrels and bilayer beta-sheets, while substitu
Hydrophobic Interaction Drives Surface-Assisted Epitaxial Assembly of Amyloid-like Peptides
STRUCTURAL INSIGHT INTO THE POLYMORPHISM OF NNQNTF PROTOFIBRIL: IMPORTANCE OF INTERFACIAL WATER, POL
Interactions of a water-soluble fullerene derivative with amyloid-beta protofibrils: dynamics, bindi
Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer
Molecular mechanism of fullerene-inhibited aggregation of Alzheimer’s β-amyloid peptide fragment
Single Mutations in Tau Modulate the Populations of Fibril Conformers through Seed Selection
Effects of hydroxylated carbon nanotubes on the aggregation of Aβ(16-22) peptides: a combined simula
Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the na
Structural insight into tau protein’s paradox of intrinsically disordered behavior, self-acetylation
Aβ “Stretching-and-Packing” Cross-seeding Mechanism Can Trigger Tau Protein Aggregation
Amphiphilic peptides A6K and V6K display distinct oligomeric structures and self-assembly dynamics:
Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier
Atomic-Level Study of the Effects of O4 Molecules on the Structural Properties of Protofibrillar Aβ
Interactions of a water-soluble fullerene derivative with amyloid-β protofibrils: dynamics, binding