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.
I: FEBS Letters, Bind 583, Nr. 16, 2009, s. 2600-2609.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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 - 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
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