Unique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin Fibrils

Yoav Atsmon-Raz; Vered Wineman-Fisher; Michal Baram; Yifat Miller

doi:10.1021/acschemneuro.8b00554

Unique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin Fibrils

Yoav Atsmon-Raz
, Vered Wineman-Fisher
, Michal Baram
, Yifat Miller

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross-seeding amylin-Aβ and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.

Original language	English
Pages (from-to)	1209-1213
Number of pages	5
Journal	ACS Chemical Neuroscience
Volume	10
Issue number	3
DOIs	https://doi.org/10.1021/acschemneuro.8b00554
State	Published - 20 Mar 2019
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2018 American Chemical Society.

Funding

This project is funded by the Israel Science Foundation (Grant 532/15). Notes The authors declare no competing financial interest.

Funders	Funder number
Israel Science Foundation	532/15

Keywords

Amyloid
peptide-plane in proteins
polymorphism
self-assembly
structural interconversion

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10.1021/acschemneuro.8b00554

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abstract = "Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross-seeding amylin-Aβ and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.",

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AU - Wineman-Fisher, Vered

AU - Baram, Michal

AU - Miller, Yifat

PY - 2019/3/20

Y1 - 2019/3/20

N2 - Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross-seeding amylin-Aβ and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.

AB - Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross-seeding amylin-Aβ and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.

KW - Amyloid

KW - peptide-plane in proteins

KW - polymorphism

KW - self-assembly

KW - structural interconversion

UR - https://www.scopus.com/pages/publications/85059432451

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Unique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin Fibrils

Abstract

Bibliographical note

Funding

Keywords

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