Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

Annette Eva Langkilde; Bente Vestergaard

doi:10.1016/j.febslet.2009.05.040

Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

Annette Eva Langkilde, Bente Vestergaard

55 Citations (Scopus)

Abstract

Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to the nature of the process, which may be described as a dynamically evolving equilibrium between a large number of structural species. These are furthermore of highly diverging sizes and present in very uneven amounts and timeframes. Different structural methods have different strengths and limitations. These, and in particular recent advances within solution analysis of the undisturbed equilibrium using small angle X-ray scattering, are reviewed here.

Original language	English
Journal	FEBS Letters
Volume	583
Issue number	16
Pages (from-to)	2600-2609
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2009.05.040
Publication status	Published - 2009

Keywords

Former Faculty of Pharmaceutical Sciences

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10.1016/j.febslet.2009.05.040

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title = "Methods for structural characterization of prefibrillar intermediates and amyloid fibrils",

abstract = "Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to the nature of the process, which may be described as a dynamically evolving equilibrium between a large number of structural species. These are furthermore of highly diverging sizes and present in very uneven amounts and timeframes. Different structural methods have different strengths and limitations. These, and in particular recent advances within solution analysis of the undisturbed equilibrium using small angle X-ray scattering, are reviewed here.",

keywords = "Former Faculty of Pharmaceutical Sciences",

author = "Langkilde, {Annette Eva} and Bente Vestergaard",

note = "Keywords: Amyloid; Animals; Humans; Models, Chemical; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Scattering, Small Angle; X-Ray Diffraction",

year = "2009",

doi = "10.1016/j.febslet.2009.05.040",

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T1 - Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

AU - Langkilde, Annette Eva

AU - Vestergaard, Bente

N1 - Keywords: Amyloid; Animals; Humans; Models, Chemical; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Scattering, Small Angle; X-Ray Diffraction

PY - 2009

Y1 - 2009

N2 - Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to the nature of the process, which may be described as a dynamically evolving equilibrium between a large number of structural species. These are furthermore of highly diverging sizes and present in very uneven amounts and timeframes. Different structural methods have different strengths and limitations. These, and in particular recent advances within solution analysis of the undisturbed equilibrium using small angle X-ray scattering, are reviewed here.

AB - Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to the nature of the process, which may be described as a dynamically evolving equilibrium between a large number of structural species. These are furthermore of highly diverging sizes and present in very uneven amounts and timeframes. Different structural methods have different strengths and limitations. These, and in particular recent advances within solution analysis of the undisturbed equilibrium using small angle X-ray scattering, are reviewed here.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.febslet.2009.05.040

DO - 10.1016/j.febslet.2009.05.040

M3 - Journal article

C2 - 19481541

SN - 0014-5793

VL - 583

SP - 2600

EP - 2609

JO - F E B S Letters

JF - F E B S Letters

IS - 16

ER -

Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

Abstract

Keywords

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