A practical guide to small angle X‐ray scattering (SAXS) of flexible and intrinsically disordered proteins

Small‐angle X‐ray scattering (SAXS) is a biophysical method to study the overall shape and structural transitions of biological macromolecules in solution. SAXS provides low resolution information on the shape, conformation and assembly state of proteins, nucleic acids and various macromolecular complexes. The technique also offers powerful means for the quantitative analysis of flexible systems, including intrinsically disordered proteins (IDPs). Here, the basic principles of SAXS are presented, and profits and pitfalls of the characterization of multidomain flexible proteins and IDPs using SAXS are discussed from the practical point of view. Examples of the synergistic use of SAXS with high resolution methods like X‐ray crystallography and nuclear magnetic resonance (NMR), as well as other experimental andin silico techniques to characterize completely, or partially unstructured proteins, are presented.

• Publication year

  2015

• Venue

  FEBS Letters

• Publication date

  2015-09-14

• Fields of study

  Biology, Medicine, Materials Science, Chemistry

• Identifiers
  DOI 10.1016/j.febslet.2015.08.027PMID 26320411
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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