Author

J. Aqvist

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

G. V. Isaksen· 2 shared A. Gogoll· 1 shared A. P. IJzerman· 1 shared A. Söderholm· 1 shared B. A. Lund· 1 shared B. O. Brandsdal· 1 shared D. Andersson· 1 shared E. Sotelo· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

G. V. Isaksen

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Author profile →

3 papers

Recent·Most cited

Biophysical characterization and analysis of a mesophilic chorismate mutase from B. pumilus

R. S. Wilkins, B. A. Lund, G. V. Isaksen, J. Aqvist, B. O. Brandsdal

This study reports the first crystal structure and kinetic analysis of a mesophilic chorismate mutase from B. pumilus, using EVB/MD simulations to extract thermodynamic activation parameters.

bioRxiv · Apr 20, 2023 · PreprintBiochemistry

Deciphering conformational selectivity in the A2A adenosine G protein-coupled receptor by Free Energy simulations

H. Gutierrez de Teran, W. Jespers, L. H. Heitman, A. P. IJzerman, E. Sotelo, G. J. P. van Westen, J. Aqvist

This paper uses free energy simulations to study conformational selectivity in the A2A adenosine receptor, revealing how ligands and mutations affect receptor activation and pharmacological profiles.

bioRxiv · Jun 9, 2021Biophysics

Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family

X. Guo, A. Söderholm, S. Kanchugal P, G. V. Isaksen, O. Warsi, U. Eckhard, S. Trigüis, A. Gogoll, J. Jerlström-Hultqvist, J. Aqvist, D. Andersson, M. Selmer

The paper reveals the structure and mechanism of phage-encoded SAM lyases, showing they function as lyases rather than hydrolases, forming MTA and L-homoserine lactone through a unimolecular reaction.

bioRxiv · Aug 16, 2020Biochemistry