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Daniel Otzen

Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

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Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide. / Otzen, Daniel E.; Oliveberg, Mikael.

In: Protein Science, Vol. 13, No. 5, 01.05.2004, p. 1417-1421.

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Otzen, Daniel E. ; Oliveberg, Mikael. / Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide. In: Protein Science. 2004 ; Vol. 13, No. 5. pp. 1417-1421.

Bibtex

@article{7341462d22324e02b75167e87a801946,
title = "Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide",
abstract = "During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 {\AA}) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 {\AA} to 120 {\AA} diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.",
keywords = "Amyloid fibrils, Electron microscopy, Peptide aggregation, Peptide crystal, Protein aggregation",
author = "Otzen, {Daniel E.} and Mikael Oliveberg",
year = "2004",
month = may,
day = "1",
doi = "10.1110/ps.03538904",
language = "English",
volume = "13",
pages = "1417--1421",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell Publishing, Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Transient formation of nano-crystalline structures during fibrillation of an Aβ-like peptide

AU - Otzen, Daniel E.

AU - Oliveberg, Mikael

PY - 2004/5/1

Y1 - 2004/5/1

N2 - During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.

AB - During the first few minutes of fibrillation of a 14-residue peptide homologous to the hydrophobic C-terminal part of the Aβ-peptide, EM micrographs reveal small crystalline areas (100 to 150 nm, repeating unit 47 Å) scattered in more amorphous material. On a longer time scale, these crystalline areas disappear and are replaced by tangled clusters resembling protofilaments (hours), and eventually by more regular amyloid fibrils of 60 Å to 120 Å diameter (days). The transient population of the crystalline areas indicates the presence of ordered substructures in the early fibrillation process, the diameter of which matches the length of the 14-mer peptide in an extended β-strand conformation.

KW - Amyloid fibrils

KW - Electron microscopy

KW - Peptide aggregation

KW - Peptide crystal

KW - Protein aggregation

UR - http://www.scopus.com/inward/record.url?scp=1942473120&partnerID=8YFLogxK

U2 - 10.1110/ps.03538904

DO - 10.1110/ps.03538904

M3 - Journal article

C2 - 15096642

AN - SCOPUS:1942473120

VL - 13

SP - 1417

EP - 1421

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 5

ER -