Quaternary Structure of Chaperones from the Hsp70 System Determined by Small Angle X-Ray Scattering (SAXS) and Analytical Ultracentrifugation
Pp. 47-72 (26)
Julio C. Borges and Carlos H.I. Ramos
High-resolution techniques, such as X-ray crystallography and nuclear
magnetic resonance, are not always capable of providing insight into the quaternary
structure of full-length forms of eukaryotic chaperones. This has somewhat limited the
field’s ability to understand the mechanisms by which chaperones regulate and specify
their functions. To fill this information gap, small angle X-ray scattering (SAXS) has
been used to gain insight into the quaternary structure of chaperones and co-chaperones
in the absence and in the presence of their ligands. This chapter will review selected
structural biology publications of the Hsp70 system, in which SAXS was used to
investigate the quaternary structure of these molecular chaperones, and will examine
how analytical ultracentrifugation can be used as an important tool to validate SAXS
Protein folding, Molecular chaperone, Heat shock protein, SAXS,
Analytical ultracentrifugation, Hsp70, Hsp40, Nucleotide exchange factor.
Institute of Chemistry, University of Campinas UNICAMP, Campinas SP, 13083-970, Brazil.