Specific Interactions and Environment Flexibility Tune Protein Stability under Extreme Crowding-Reference-Cited by-同舟云学术

Specific Interactions and Environment Flexibility Tune Protein Stability under Extreme Crowding

Published:2021-06-08 Issue:23 Volume:125 Page:6103-6111
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Katava Marina¹,Stirnemann Guillaume¹^ORCID,Pachetti Maria²³^ORCID,Capaccioli Simone⁴⁵,Paciaroni Alessandro⁶,Sterpone Fabio¹^ORCID

Affiliation:

1. Laboratoire de Biochimie Théorique, IBPC, CNRS UPR9080, Université Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005 Paris, France

2. Elettra-Sincrotrone Trieste, S.S. 14 km 163.5, Area Science Park, 34149 Trieste, Italy

3. Department of Physics, University of Trieste, Via Valerio 2, 34127 Trieste, Italy

4. Dipartimento di Fisica, Universitá di Pisa, largo Pontecorvo 3, 56127 Pisa, Italy

5. CISUP, Centro per l’Integrazione della Strumentazione dell’Università di Pisa, Lungarno Pacinotti 43, I-56127 Pisa, Italy

6. Dipartimento di Fisica e Geologia, Universitá di Perugia, via A. Pascoli, 06123 Perugia, Italy

Funder

Agence Nationale de la Recherche

FP7 Ideas: European Research Council

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c01511

Reference59 articles.

1. Join the crowd

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

3. Protein folding in confined and crowded environments

4. Protein Crowding Tunes Protein Stability

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