On Protein Folding in Crowded Conditions.

David Gomez1,2, Klaus Huber3, Stefan Klumpp1,4

  • 1Max Planck Institute of Colloids and Interfaces , 14476 Potsdam , Germany.

Summary

Cells are densely packed with macromolecules, which influences protein folding and stability. This study uses simulations to explore how different types of crowders affect protein stability in crowded environments. The researchers found that polymeric crowders have a stronger effect than spherical ones. The effect of polymeric crowders increases with length, while spherical crowders show decreasing effects with increasing size. These findings are explained by entropy changes from excluded volume and demixing. The study highlights the importance of crowder geometry in determining protein stability. These results may help improve models of protein folding in realistic cellular conditions.

Frequently Asked Questions

Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
10.8K
Protein Folding01:22

Protein Folding

Overview
125.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.6K
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
11.5K
Protein Organization01:13

Protein Organization

Overview
155.4K