Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer

We have used coarse-grained (CG) and united atom (UA) molecular dynamics simulations to explore the mechanisms of protein orientational transition of a model peptide (Aβ42) in a phosphatidylcholine/cholesterol (PC/CHO) lipid bilayer. We started with an inserted state of Aβ42 containing a folded (I)...

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Veröffentlicht in:	Biophysical chemistry 2015-11, Vol.206, p.22-39
Hauptverfasser:	Cheng, Kwan Hon, Qiu, Liming, Cheng, Sara Y., Vaughn, Mark W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid beta-Peptides - chemistry Cholesterol - chemistry Humans Lipid Bilayers - chemistry Molecular Dynamics Simulation Molecular Sequence Data Peptide Fragments - chemistry Phosphatidylcholines - chemistry Protein Structure, Tertiary Protein Unfolding
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