Characterization Of Nucleotide-induced Changes On The Quaternary Structure Of Human 70 Kda Heat Shock Protein Hsp70.1 By Analytical Ultracentrifugation.

dc.creatorBorges, Julio C
dc.creatorRamos, Carlos H I
dc.date2009-Mar
dc.date2015-11-27T13:15:03Z
dc.date2015-11-27T13:15:03Z
dc.date.accessioned2018-03-29T01:08:33Z
dc.date.available2018-03-29T01:08:33Z
dc.identifierBmb Reports. v. 42, n. 3, p. 166-71, 2009-Mar.
dc.identifier1976-6696
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/19336004
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/198245
dc.identifier19336004
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1298478
dc.descriptionHsp70s assist in the process of protein folding through nucleotide-controlled cycles of substrate binding and release by alternating from an ATP-bound state in which the affinity for substrate is low to an ADP-bound state in which the affinity for substrate is high. It has been long recognized that the two-domain structure of Hsp70 is critical for these regulated interactions. Therefore, it is important to obtain information about conformational changes in the relative positions of Hsp70 domains caused by nucleotide binding. In this study, analytical ultracentrifugation and dynamic light scattering were used to evaluate the effect of ADP and ATP binding on the conformation of the human stress-induced Hsp70.1 protein. The results of these experiments showed that ATP had a larger effect on the conformation of Hsp70 than ADP. In agreement with previous biochemical experiments, our results suggest that conformational changes caused by nucleotide binding are a consequence of the movement in position of both nucleotide- and substrate-binding domains.
dc.description42
dc.description166-71
dc.languageeng
dc.relationBmb Reports
dc.relationBMB Rep
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdenosine Diphosphate
dc.subjectAdenosine Triphosphate
dc.subjectHsp70 Heat-shock Proteins
dc.subjectHumans
dc.subjectProtein Structure, Quaternary
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.subjectUltracentrifugation
dc.titleCharacterization Of Nucleotide-induced Changes On The Quaternary Structure Of Human 70 Kda Heat Shock Protein Hsp70.1 By Analytical Ultracentrifugation.
dc.typeArtículos de revistas


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