Protein thermal denaturation is modulated by central residues in the protein structure network

The FEBS Journal
Valquiria P SouzaSandro R Marana

Abstract

Network structural analysis, known as residue interaction networks or graphs (RIN or RIG, respectively) or protein structural networks or graphs (PSN or PSG, respectively), has recently been proven to be a useful tool for detecting important residues for protein function, stability, folding and allostery. In RIN, the tertiar y structure is represented by a network in which residues (nodes) are connected by interactions (edges). Such structural networks have consistently presented a few central residues that are important for shortening the pathways linking any two residues in a protein structure. To experimentally demonstrate that central residues effectively participate in protein properties, mutations were directed to seven central residues of the β-glucosidase Sfβgly. These mutations reduced the thermal stability of the enzyme, as evaluated by changes in Tm and the denaturation rate at 45 °C. Moreover, mutations directed to the vicinity of a central residue also caused significant decreases in the Tm of Sfβgly and clearly increased the unfolding rate constant at 45°C. However, mutations at non-central residues or at surrounding residues did not affect the thermal stability of Sfβgly. Therefore, the data presented here sugges...Continue Reading

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Citations

Jun 7, 2018·PloS One·Ammu Prasanna Kumar, Suryani Lukman
Jan 18, 2020·Briefings in Bioinformatics·Ammu Prasanna KumarSuryani Lukman
Jan 18, 2018·PloS One·Vitor M AlmeidaSandro R Marana
Jul 1, 2020·Protein Science : a Publication of the Protein Society·Felipe A M OtsukaSandro R Marana
Jul 29, 2021·Journal of Structural Biology·Vitor Medeiros AlmeidaSandro Roberto Marana
Nov 19, 2019·Journal of Chemical Information and Modeling·André A O ReisGuilherme M Arantes

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