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29 result(s)

The Hsp90 chaperone (heat shock protein 90 kDa) is found in all organisms and in all cellular compartments, and the two types found in the eukaryotic cytosol interact with at least 10% of all proteins produced by the cell. The Hsp90 plays a key role in the maturation of these proteins, which makes it important for many cellular processes such signaling, proteostasis, epigenetics, telomere maintenance, innate immunity, etc. Obviously, changes in this 'highly connected node', as one can label Hsp90, leads to disturbances in cell function resulting in drastic consequences for the organism. For example, Hsp90 appears to play a central role in the pathology of several types of cancer as many kinases are clients and are involved in the development of cancer. As a matter of fact, specific inhibitors of Hsp90 and co-chaperones are under investigation in clinical trials. No human cytosolic Hsp90 had its full three-dimensional structure determined and the mechanisms by which this chaperone functions and is modulated are not yet fully known. Even the set of co-chaperones and post-translational modifications, that play key role in the processes aforementioned, are not yet complete understood. The obvious therapeutic potential that Hsp90 from human, and Hsp90 from other organisms, have, make essential to unravel the forces that stabilize their structure and the mechanisms by which their functions are modulated resulting in the maturation of proteins clients. The importance in studying Hsp90 brought together researchers involved in studying the relationship between structure and function of proteins, particularly chaperones from human, plants and protozoa, that will focus on the following goals: 1) Determination of the conformational aspects of Hsp90, its isolated domains and some of its co-chaperones. 2) Characterization of the ATPase activity of the various types of Hsp90 available. 3) Investigation of the interaction of Hsp90 with several co-chaperones, inhibitors and client proteins. 4) Investigation of the effect that post-translational modifications have in the structure and function of Hsp90. To show our commitment to this proposal we would like to stress that some studies are already underway and already have potential to generate knowledge that is both new and relevant. (AU)


The coordinator of this proposal, Carlos Ramos, has a research project financed by FAPESP, which has as its objective the use of the technique of isothermal titration calorimetry (ITC) to study the interaction between proteins and small molecules. The proteins studied in the research group are those involved in protein homeostasis, especially molecular chaperones and sirtuins. With the great experience prof Minetti has in the area of study of thermodynamics of interaction between proteins and ligands, she can make important contributions in our research project and training of specialized personnel. In addition to that, an automated ITC will be installed in an Institutional Laboratory at UNICAMP and will be available to researchers of universities in Sao Paulo state. Thus the training of specialized personnel will be very important to the widespread use of this equipment. (AU)

Protein folding, stability and structure

Grant number:05/00462-8
Support type:Research Projects - Thematic Grants
Duration: April 01, 2006 - September 30, 2011
Field of knowledge:Biological Sciences - Biochemistry
Principal Investigator:Carlos Henrique Inacio Ramos
Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas, SP, Brazil
FAPESP publication about the research grant:

Our yet little understanding of the protein folding process holds back the understanding of several cellular processes because the conversion of a backbone into a native protein is a key element in the translation of organism's genetic information. As the organism ages, the folding seems to deviates becoming a signal to several diseases (mainly neurodegenerative). Protein misfolding causes deposition in the cell in the form of aggregates or amyloidal fibrils, both of which has toxic effects. One way to cell protection is throughout molecular chaperones, which help protein folding and may help protein disaggregation. Therefore, chaperones seem to have a fundamental role in the organism by increasing the success of physiological functions and protecting cells of become ill. My proposal has the main objective of understand protein folding by: 1) studying the folding pathway and the stability of proteins, mainly globins; 2) characterizing the forces and the mechanisms of amyloidal fibril formation; 3) structural and functional characterization of chaperones and 4) studying the mechanisms by which chaperones help folding, stop aggregation, ressolubilize aggregates, and interact with proteins involved in cell malignization. These phenomena mutually take place in the cell and their study in conjunction as proposed here may increase our understanding of protein folding inside the cell, which will generate important new thinking that lead to new therapies. (AU)


Some newly synthesized proteins require the assistance of molecular chaperones for their folding. Chaperones are also involved in the dissolution of protein aggregates. Hence, the study of molecular chaperones has biotechnology and medical importance. We intend to search the SUCEST data bank in order to identify and annotate the genes of stress related proteins, mainly chaperones and Hsps. (AU)

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