Amyloid: Structure and Function
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Informatics".
Deadline for manuscript submissions: closed (20 September 2022) | Viewed by 9777
Special Issue Editor
Interests: prion; amyloid; liquid-liquid phase separation (LLPS); mnemon; chaperones; Sup35; yeast; proteinase K
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Amyloids and their infective form, prions, occupy a special place in molecular biology; not central, but interesting and enigmatic. While DNA, RNA, and proteins were created by nature through natural selection, amyloids were not. They result from a side property – a kind of a flaw – of protein matter. Due to this, they mainly manifest as diseases. However, the nature can find use for any property, and there is already a fairly long list of useful mechanisms based on amyloids. The structure of amyloids is another interesting issue. In contrast to 3-D crystals formed by small molecules and globular proteins, amyloids are 1-dimensional crystals. While, during formation of 3-D crystals, the spatial freedom belongs to whole molecules, amyloids are formed by unfolded polypeptides in which every residue possesses some freedom before the amyloid structure is fixed. Amyloid formation in vitro requires just amyloidogenic protein, but in vivo, it is a complex process involving many other proteins, mainly chaperones.
According to the presented considerations, the main topics that will be the focus of this Special Issue are the process of in vivo amyloid formation, the structure of amyloids, and useful or potentially useful mechanisms based on amyloids and prions.
Dr. Vitaly V. Kushnirov
Guest Editor
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Keywords
- Amyloid
- Prion
- Amyloid structure
- Amyloid formation
- Potentially useful mechanism
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