Author

H. Fraga

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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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 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 Assay:proteomics· 1

Frequent Co-Authors

P. Schanda· 3 shared A. Hessel· 2 shared D. F. Gauto· 2 shared P. Macek· 2 shared A. Barducci· 1 shared A. Velazquez-Campoy· 1 shared C. Breyton· 1 shared C. Chipot· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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3 shared papersBiochemistry

P. Schanda

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Author profile →

3 papers

Recent·Most cited

Deuteration of proteins boosted by cell lysates: high-resolution amide and Hα MAS NMR without re-protonation bottleneck

F. Napoli, J.-Y. Guan, C.-A. Arnaud, P. Macek, H. Fraga, C. Breyton, P. Schanda

This paper demonstrates a method to overcome the re-protonation bottleneck in NMR by using deuterated cell lysates, enabling high-resolution amide and Hα MAS NMR with improved sensitivity.

bioRxiv · Jan 8, 2024 · PreprintBiochemistry

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