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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-23 18:35 |
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Conference: Bucharest University Faculty of Physics 2009 Meeting
Section: Biophysics; Medical Physics
Title:
Mechanism and importance of protein folding
Authors:
Aurel I. Popescu, Doina M. Gazdaru, Claudia G. Chilom, Catalin L. Geanta
Affiliation:
Research Centre in Molecular Biophysics, Department of Electricity and Biophysics, Faculty of Physics, University of Bucharest
E-mail
aurel.popescu.46@gmail.com
Keywords:
folding mechanism, protein folding diseases, chaperones
Abstract:
A cell expresses over10,000 proteins, at any moment, for three types of activities: metabolic, maintaining its structures, and producing signals for other cells.
The proteins are a special class of polymers that is properly and optimally operating only if they possess a native spatial structure. This means that every member of a population of a protein specific class is adopting the same space configuration of its atoms. Otherwise, any critical deviation from the specific space shape of protein is implying a significant, sometimes dramatic, modification of its biochemical function.
Protein folding is the dynamical process by which a protein assumes its functional 3D shape (conformation).Two factors contribute to folding of a protein: the intrinsic properties of the amino acid sequence and the multiple influences from the crowded cellular microenvironment of the nascent protein.
While small proteins are spontaneously folding, the larger ones need to be assisted by other proteins, named chaperones, otherwise it risking to be incorrectly folded. While the number of the intermediary states from unfolded states to native folded one is a huge one, the process is very rapid, ranging from µs to s, implying energetically (DG < 0) favoured paths of folding.
Protein folding not only generates biologically active structures, but also protects the protein from degradation by proteases and reduces the probability that aggregation will occur, as in the case of many diseases (e.g., Alzheimer, Parkinson).
The ability of proteins to fold rapidly is an important evolutionary gain that minimise competition with aggregations (amyloidal structures) by which these diseases are provoked.
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