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Enzyme enhancement through computational stability design targeting NMR-determined catalytic hotspots.

Year: 2024

Type: article

Abstract: Required files to run the classical molecular dynamics and empirical valence bond (EVB) simulations performed to generate the data for the article: Enzyme enhancement through computational stability design targeting NMR-determined catalytic hotspots

Source: Zenodo (CERN European Organization for Nuclear Research)

DOI: 10.5281/zenodo.12666978

Authors: Gutierrez Rus, Luis I., Vos, Eva, Pantoja-Uceda, David, Hoffka, Gyula, Gutierrez-Cardenas, Jose, Ortega Muñoz, Mariano, Risso, Valeria A., Jimenez, Maria Angeles, Kamerlin, Shina Caroline Lynn, Sanchez-Ruiz, Jose M.

Institutions: Universidad de Granada, Georgia Institute of Technology, Instituto de Química Física Blas Cabrera, Uppsala University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W6949255654

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