Biophysical Reviews

, Volume 10, Issue 2, pp 229–233 | Cite as

Analytical ultracentrifugation in structural biology

Review

Abstract

Researchers in the field of structural biology, especially X-ray crystallography and protein nuclear magnetic resonance, are interested in knowing as much as possible about the state of their target protein in solution. Not only is this knowledge relevant to studies of biological function, it also facilitates determination of a protein structure using homogeneous monodisperse protein samples. A researcher faced with a new protein to study will have many questions even after that protein has been purified. Analytical ultracentrifugation (AUC) can provide all of this information readily from a small sample in a non-destructive way, without the need for labeling, enabling structure determination experiments without any wasting time and material on uncharacterized samples. In this article, I use examples to illustrate how AUC can contribute to protein structural analysis. Integrating information from a variety of biophysical experimental methods, such as X-ray crystallography, small angle X-ray scattering, electrospray ionization-mass spectrometry, AUC allows a more complete understanding of the structure and function of biomacromolecules.

Keywords

Protein AUC Crystallography Interaction 

Notes

Acknowledgments

I would like to thank my colleagues at Yokohama City University for their support during my stay, when the main results of this article were obtained.

Compliance with ethical standards

Conflicts of interest

Satoru Unzai declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by the author.

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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Department of Frontier Bioscience, Faculty of Bioscience and Applied ChemistryHosei UniversityTokyoJapan

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