From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network

Author(s): Fernanda A.H. Batista, Lisandra M. Gava, Glaucia M. S. Pinheiro, Carlos H.I. Ramos, Julio C. Borges

Journal Name: Current Protein & Peptide Science

Volume 16 , Issue 8 , 2015

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Graphical Abstract:


Proteins participate in almost every cell physiological function, and to do so, they need to reach a state that allows its function by folding and/or exposing surfaces of interactions. Spontaneous folding in the cell is in general hindered by its crowded and viscous environment, which favors misfolding and nonspecific and deleterious self-interactions. To overcome this, cells have a system, in which Hsp70 and Hsp90 play a central role to aid protein folding and avoid misfolding. The topics of this review include the biophysical tools used for monitoring protein-ligand and protein-protein interactions and also some important results related to the study of molecular chaperones and heat shock proteins (Hsp), with a focus on the Hsp70/Hsp90 network. The biophysical tools and their use to probe the conformation and interaction of Hsp70 and Hsp90 are briefly reviewed.

Keywords: Analytical ultracentrifugation, Calorimetry, Fluorescence, Molecular chaperones and Hsps, Protein folding, Protein interaction, Thermodynamics.

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Article Details

Year: 2015
Published on: 27 August, 2015
Page: [735 - 753]
Pages: 19
DOI: 10.2174/1389203716666150505225744
Price: $65

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