کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1979783 | 1061701 | 2010 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Principles governing oligomer formation in amyloidogenic peptides Principles governing oligomer formation in amyloidogenic peptides](/preview/png/1979783.png)
Identifying the principles that describe the formation of protein oligomers and fibrils with distinct morphologies is a daunting problem. Here we summarize general principles of oligomer formation gleaned from molecular dynamics simulations of Aβ-peptides. The spectra of high free energy structures sampled by the monomer provide insights into the plausible fibril structures, providing a rationale for the ‘strain phenomenon.’ Heterogeneous growth dynamics of small oligomers of Aβ16–22, whose lowest free energy structures are like nematic droplets, can be broadly described using a two-stage dock-lock mechanism. In the growth process, water is found to play various roles depending on the oligomer size, and peptide length, and sequence. Water may be an explicit element of fibril structure linked to various fibril morphologies.
Journal: Current Opinion in Structural Biology - Volume 20, Issue 2, April 2010, Pages 187–195