Author

Vinícius M. de Oliveira

Instituto de Biociências, Letras e Ciências Exatas, câmpus de São José do Rio PretoORCID 0000-0003-0927-3825Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Bioinformatics· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:protein structure· 3 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein design· 1 Approach:statistical model· 1 Organism:virus· 1

Frequent Co-Authors

Vinícius G. ContessotoiD· 2 shared Vitor B. P. Leite· 2 shared Bruno R. Fernandes· 1 shared Fernando Bruno da Silva· 1 shared Gabriel Gouvêa SladeiD· 1 shared Haifa El KilaniiD· 1 shared Jana SheniD· 1 shared Jane Clarke· 1 shared

Activity by Year

2017-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBioinformatics

Vinícius G. ContessotoORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistryhLifePeer-reviewedJun 15, 2024

Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study of the free enzyme and its complex with inhibitor 13b-K

Mohamed Ibrahim, Xinyuanyuan Sun, Vinícius M. de Oliveira…·Rolf Hilgenfeld

This study investigates why the Omicron variant's main protease is less stable than the wild-type by analyzing its structure, enzymatic activity, and biophysical properties.

15 citationstop 4%

virusprotein structure

𝕏 PostBluesky

BioinformaticsProteins Structure Function and BioinformaticsPeer-reviewedSep 16, 2018

TKSA-MC: A Web Server for rational mutation through the optimization of protein charge interactions

Vinícius G. Contessoto, Vinícius M. de Oliveira, Bruno R. Fernandes…·Vitor B. P. Leite

TKSA-MC calculates protein charge-charge interactions to identify residues for mutation to enhance thermal stability.

40 citations

protein structurestatistical model

𝕏 PostBluesky

BiophysicsbioRxivPreprintDec 10, 2017

Non-native Interactions Explain the Folding Rate Differences in α-Spectrin Domains and the Origin of Internal Friction Effects

Fernando Bruno da Silva, Vinícius G. Contessoto, Vinícius M. de Oliveira…·Vitor B. P. Leite

The paper investigates internal friction in protein folding by simulating α-spectrin domains with non-native interactions, showing that cooperativity among these interactions explains folding rate differences and internal friction effects.

DOI 10.1101/232116

protein structuremechanistic / dynamical model

𝕏 PostBluesky