Author

D. F. Gauto

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Assay:structural biology· 2 Research Focus:host-pathogen & immune response· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

P. Schanda· 3 shared A. Hessel· 2 shared H. Fraga· 2 shared A. Barducci· 1 shared A. Velazquez-Campoy· 1 shared C. Chipot· 1 shared C. Morlot· 1 shared D. Malinverni· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiophysics

P. Schanda

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3 papers

Recent·Most cited

Aromatic ring flips in differently packedubiquitin protein crystals from MAS NMR andMD

D. F. Gauto, O. O. Lebedenko, L. M. Becker, I. Ayala, R. Lichtenecker, N. R. Skrynnikov, P. Schanda

The paper investigates how crystal packing affects aromatic ring flips in ubiquitin using NMR and MD simulations, finding that intramolecular factors dominate over packing effects.

bioRxiv · Jul 7, 2022Biophysics

Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR

D. F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sucec, A. Hessel, J. P. Bustamante, A. Barducci, P. Schanda

The paper uses MAS NMR and computational methods to show a flexible loop in TET2 aminopeptidase is critical for catalytic function and substrate processing.

bioRxiv · Jun 29, 2021Biophysics

Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors

J. Felix, K. Weinhaupl, C. Chipot, F. Dehez, A. Hessel, D. F. Gauto, C. Morlot, O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga

The paper investigates how bortezomib activates ClpP protease by mimicking a substrate and inducing allosteric conformational changes that enhance its interaction with ClpX.

bioRxiv · Mar 15, 2019Biochemistry