Effects of Molecular Chaperone, Protein Aggregation and Macromolecular Crowding on Protein Folding

doi:10.7523/j.issn.2095-6134.2002.2.021

Abstract

Abstract:

The effects of molecular chaperones, protein aggregation and macromolecular crowding on protein folding have been studied. It has been demonstrated that there are two binding ways between molecular chaperone GroEL and its substrates, "all of sites" and "half of sites", depending on the shape, the size of substrates and the interaction between GroEL and substrates. It has also provided insights into a mechanism of cells to prevent protein folding against interference from aggregation of other proteins. In addition, it has been suggested that pre-molten globule state of α-lactalbumin is the target not only for chaperones but also for protein aggregates. Finally, it has displayed the complexity and the diversity of effects of macromolecular crowding on both the thermodynamics and kinetics of protein folding and assembly.

Key words: protein folding, molecular chaperone, protein aggregation, macromolecular crowding

CLC Number:

LI Jian, WANG Zhi-Zhen. Effects of Molecular Chaperone, Protein Aggregation and Macromolecular Crowding on Protein Folding[J]. , 2002, 19(2): 215-218.

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