Coevolution-Driven Method for Efficiently Simulating Conformational Changes in Proteins Reveals Molecular Details of Ligand Effects in the β2AR Receptor-Reference-Cited by-同舟云学术

Coevolution-Driven Method for Efficiently Simulating Conformational Changes in Proteins Reveals Molecular Details of Ligand Effects in the β2AR Receptor

Published:2023-11-10 Issue:46 Volume:127 Page:9891-9904
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Mitrovic Darko¹^ORCID,Chen Yue¹,Marciniak Antoni¹^ORCID,Delemotte Lucie¹^ORCID

Affiliation:

1. Department of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, Sweden Tomtebodavägen 23, 171 65 Solna, Sweden

Funder

Science for Life Laboratory

Vetenskapsr?det

G?ran Gustafssons Stiftelser

Knut och Alice Wallenbergs Stiftelse

Swedish e-Science Research Centre

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.3c04897

Reference58 articles.

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3. Large-Scale Conformational Changes and Protein Function: Breaking the in silico Barrier

4. Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS)

5. New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels

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