Author

Vitor B. P. Leite

Instituto de Biociências, Letras e Ciências Exatas, câmpus de São José do Rio PretoPrimary ORCID profile (0000-0003-0008-9079 · 1 paper)Unclaimed ORCID profile · follow to get notified of new preprints

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Same name, identified by ORCID

Vitor B. P. LeiteiD1 paper · Universidade Estadual Paulista (Unesp)

Biology Disciplines

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Bioinformatics· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:protein structure· 2 Approach:mechanistic / dynamical model· 1 Research Focus:protein design· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

Vinícius G. ContessotoiD· 2 shared Vinícius M. de OliveiraiD· 2 shared Bruno R. Fernandes· 1 shared Fernando Bruno da Silva· 1 shared Gabriel Gouvêa SladeiD· 1 shared Jane Clarke· 1 shared

Activity by Year

2017-2018 · peak 1/yr

Co-Author Collaboration Network

6 top collaborators · 11 mutual co-author links

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2 shared papersBioinformatics

Vinícius G. ContessotoORCID

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2 papers

Recent·Most cited

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, Gabriel Gouvêa Slade, Vitor B. P. Leite

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

Proteins Structure Function and Bioinformatics · Sep 16, 2018Peer-reviewedBioinformatics

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, Jane Clarke, 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.

bioRxiv · Dec 10, 2017 · PreprintBiophysics