Methods for structural characterization of prefibrillar intermediates and amyloid fibrils

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Methods for structural characterization of prefibrillar intermediates and amyloid fibrils. / Langkilde, Annette Eva; Vestergaard, Bente.

In: FEBS Letters, Vol. 583, No. 16, 2009, p. 2600-2609.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Langkilde, AE & Vestergaard, B 2009, 'Methods for structural characterization of prefibrillar intermediates and amyloid fibrils', FEBS Letters, vol. 583, no. 16, pp. 2600-2609. https://doi.org/10.1016/j.febslet.2009.05.040

APA

Langkilde, A. E., & Vestergaard, B. (2009). Methods for structural characterization of prefibrillar intermediates and amyloid fibrils. FEBS Letters, 583(16), 2600-2609. https://doi.org/10.1016/j.febslet.2009.05.040

Vancouver

Langkilde AE, Vestergaard B. Methods for structural characterization of prefibrillar intermediates and amyloid fibrils. FEBS Letters. 2009;583(16):2600-2609. https://doi.org/10.1016/j.febslet.2009.05.040

Author

Langkilde, Annette Eva ; Vestergaard, Bente. / Methods for structural characterization of prefibrillar intermediates and amyloid fibrils. In: FEBS Letters. 2009 ; Vol. 583, No. 16. pp. 2600-2609.

Bibtex

@article{9e29e33030ea11df8ed1000ea68e967b,
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 = "The 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",
language = "English",
volume = "583",
pages = "2600--2609",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "16",

}

RIS

TY - JOUR

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 - The Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.febslet.2009.05.040

DO - 10.1016/j.febslet.2009.05.040

M3 - Journal article

VL - 583

SP - 2600

EP - 2609

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 16

ER -

ID: 18658291