Literature DB >> 26412654

Characterization of Intrinsically Disordered Proteins by Analytical Ultracentrifugation.

David J Scott1, Donald J Winzor2.   

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.
© 2015 Elsevier Inc. All rights reserved.

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Keywords:  Diffusion coefficient; Intrinsically disordered proteins; Lamm equation; Sedimentation coefficient

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Year:  2015        PMID: 26412654     DOI: 10.1016/bs.mie.2015.06.034

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  1 in total

1.  Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity.

Authors:  Sumit K Chaturvedi; Jia Ma; Patrick H Brown; Huaying Zhao; P Schuck
Journal:  Nat Commun       Date:  2018-10-24       Impact factor: 14.919

  1 in total

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