Post Translational Modifications

Led by: Elena GANEA
Fields: Medicine and pharmaceutics
Molec. Cell. & Sys. Biol.
Institution: Institute of Biochemistry
Scientists/Total: 2/2
Keywords:  Protein refolding by chemical and molecular chaperones.

Studies of protein folding, quite popular nowadays are very important both for understanding the molecular details of this process and for practical reasons, especially to prevent aggregation and to obtain correctly folded proteins by genetic engineering techniques. We have shown in our previous work that nonenzymatic posttranslational modifications of proteins such as carbamylation, aldehyde binding and glycation, which have a special importance for the control of the metabolism, under certain circumstances may induce protein unfolding; as a consequence, the inappropriately exposed hydrophobic surfaces on proteins can lead to the adoption of nonnative conformations that interact and form aggregates, compromising the protein function. Our in vitro experiments demonstrated that such modifications inactivated the enzymes and altered the interaction between myelin proteins (myelin basic protein- myelin associated glycoprotein). In the living cell, molecular chaperones are essential for the correct folding of proteins under physiological and stress conditions; they prevent aggregation of unfolded polypeptide and assist the refolding of the unfolded polypeptide to the appropriate, functional structure. Our aim is to provide a molecular description of the basic events during the in vitro refolding of proteins and hence to elucidate and understand the factors that control this process.





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