Characterization of intrinsically disordered proteins by analytical ultracentrifugation

Scott, David J. and Winzor, Donald J. (2015) Characterization of intrinsically disordered proteins by analytical ultracentrifugation. Methods in Enzymology, 562 225-239. doi:10.1016/bs.mie.2015.06.034


Author Scott, David J.
Winzor, Donald J.
Title Characterization of intrinsically disordered proteins by analytical ultracentrifugation
Journal name Methods in Enzymology   Check publisher's open access policy
ISSN 1557-7988
0076-6879
ISBN 978-0-12-802908-4
Publication date 2015
Sub-type Research book chapter (original research)
DOI 10.1016/bs.mie.2015.06.034
Open Access Status Not yet assessed
Volume 562
Start page 225
End page 239
Total pages 15
Place of publication Maryland Heights, MO, United States
Publisher Academic Press
Collection year 2016
Language eng
Abstract Intrinsically disordered proteins have traditionally been largely neglected by structural biologists because a lack of rigid structure precludes their study by X-ray crystallography. Structural information must therefore be inferred from physicochemical studies of their solution behavior. Analytical ultracentrifugation yields important information about the gross conformation of an intrinsically disordered protein. Sedimentation velocity studies provide estimates of the weight-average sedimentation and diffusion coefficients of a given macromolecular state of the protein.
Keyword Diffusion coefficient
Intrinsically disordered proteins
Lamm equation
Sedimentation coefficient
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Research book chapter (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
 
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