4.4 Review

Connecting the Dots: Macromolecular Crowding and Protein Aggregation

Journal

JOURNAL OF FLUORESCENCE
Volume 33, Issue 1, Pages 1-11

Publisher

SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10895-022-03082-2

Keywords

Macromolecular crowding; Protein aggregation; Protein conformational disorders; Neurodegeneration

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Alterations in protein folding and the formation of protein aggregates are linked to various diseases. The heterogeneous crowding environment in cells can affect protein conformation.
Proteins are one of the dynamic macromolecules that play a significant role in many physiologically important processes to sustain life on the earth. Proteins need to be properly folded into their active conformation to perform their function. Alteration in the protein folding process may lead to the formation of misfolded conformers. Accumulation of these misfolded conformers can result in the formation of protein aggregates which are attributed to many human pathological conditions including neurodegeneration, cataract, neuromuscular disorders, and diabetes. Living cells naturally have heterogeneous crowding environments with different concentrations of various biomolecules. Macromolecular crowding condition has been found to alter the protein conformation. Here in this review, we tried to show the relation between macromolecular crowding, protein aggregation, and its consequences.

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