title: From Conformation to Interaction: Techniques to Explore the Hsp70/Hsp90 Network.
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.
authors.forename: Fernanda A H
authors.initials: FA
authors.lastname: Batista
authors.forename: Lisandra M
authors.initials: LM
authors.lastname: Gava
authors.forename: Glaucia M S
authors.initials: GM
authors.lastname: Pinheiro
authors.forename: Carlos H I
authors.initials: CH
authors.lastname: Ramos
authors.affiliation: Institute of Chemistry of Sao Carlos, USP, Av. Trabalhador Sancarlense, 400, Sao Carlos - SP, 13560-970, Brazil. borgesjc@iqsc.usp.br.
authors.forename: Julio C
authors.initials: JC
authors.lastname: Borges
mesh_terms: D000818:Animals; D055592:Biophysical Phenomena; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D025941:Protein Interaction Mapping
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D008024:Ligands