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

2015; Bentham Science Publishers; Volume: 16; Issue: 8 Linguagem: Inglês

10.2174/1389203716666150505225744

1875-5550

Fernanda Aparecida Heleno Batista, Lisandra M. Gava, Gláucia M.S. Pinheiro, Carlos H.I. Ramos, Júlio C. Borges,

Computational Drug Discovery Methods

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.