Sandro Roberto Marana

• Abstract

  This research project is divided in two fronts: 1 - Quaternary Structure and Enzyme Kinetics in beta-Glucosidases and 2 - Structure Network and Thermostability in Proteins.Front 1 - The presence of beta-glucosidases oligomers (dimers to octamers) is already well reported in the literature. However, there is no clear view of the oligomerization effect on the enzyme kinetics. Indeed, the fe…

  Catalysis and Thermostability in Enzymes: Oligomerization, Structure Network and Dynamics Effects, AP.R

• Abstract

  Protein structures can be represented as an interaction network of amino acid residues, which exhibits high clustering and small world properties. Hence protein structural networks are formed by residue clusters connected through short contact pathways. Indeed, the small world property is determined by a small set of residues called central residues or hubs. Protein structures are also dy…

  Enzyme structural network and dynamics, AP.R

• Abstract

  The active site residues in GH1 b-glycosidases are compartmentalized into 3 functional regions, involved in catalysis or binding of glycone and aglycone motifs from substrate. However, it still remains unclear how residues outside the active site modulate the enzymatic activity. To tackle this question, we solved the crystal structure of the GH1 b-glycosidase from Spodoptera frugiperda (S…

  Using the amino acid network to modulate the hydrolytic activity of b-glycosidases, PUB.ART

(Only some records are available in English at this moment)

• Abstract

  Tridimensional protein structures can be analyzed as graphs (Protein Structure Networks). On this analysis, the protein amino acid residues are the vertex of the network and both covalent and non-covalent interactions between residues are the edges. Therefore, this approach allows a global analysis of thousands of interactions responsible for keeping the structure of a protein, determinin…

  Centrality in protein structure networks and molecular dynamics, BP.IC

• Abstract

  Protein domains are segments with stable and independent folding (Richardson, 1981; Dootlitle, 1995; Porter e Rose, 2012). Based on this definition, the structure of the (beta/alpha)8 barrels proteins was shown to be composed by two domains corresponding to its N- and C-terminal halves. In agreement, the analysis of the contact map of the beta-glucosidases GH1, also (beta/alpha)8 barrels,…

  Role of the half-barrels subdomains on the stability of beta-glucosidases, BP.DR

• Abstract

  Enzymatic hydrolysis of cellulose depends on the combined action of endoglucanases, cellobiohydrolases and b-glucosidases. In the "initial steps" endoglucanases and cellobiohydrolases attack the cellulose fibers generating the disaccharide cellobiose, which in the "final stage" is hydrolyzed by b-gtycosidases. However, the rate of cellulose hydrolysis decreases during the reaction, result…

  Production and characterization of Sfbgli-CBM, a chimeric protein with beta-glycosidic and cellulose binding domains, BP.PD

(Only some records are available in English at this moment)