Molecular Crowding Stabilizes Both the Intrinsically Disordered Calcium-Free State and the Folded Calcium-Bound State of a Repeat in Toxin (RTX) Protein-Reference-Cited by-同舟云学术

Molecular Crowding Stabilizes Both the Intrinsically Disordered Calcium-Free State and the Folded Calcium-Bound State of a Repeat in Toxin (RTX) Protein

Published:2013-07-31 Issue:32 Volume:135 Page:11929-11934
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Sotomayor-Pérez Ana-Cristina¹,Subrini Orso¹,Hessel Audrey¹,Ladant Daniel¹,Chenal Alexandre¹

Affiliation:

1. Unité de Biochimie des Interactions Macromoléculaires, CNRS UMR 3528, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris cedex 15, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja404790f

Reference42 articles.

1. The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences

2. Macromolecular crowding: obvious but underappreciated

3. Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences

4. Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding

5. Protein Stability and Folding Kinetics in the Nucleus and Endoplasmic Reticulum of Eucaryotic Cells

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