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Molecular modeling of hair keratin/peptide complex : using MM-PBSA calculations...
Azoia, Nuno G.; Fernandes, Margarida M.; Micaelo, N. M.; Soares, Cláudio M.; Paulo, Artur CavacoMolecular dynamics simulations of a keratin/peptide complex have been conducted to predict the binding affinity of four different peptides toward human hair. Free energy calculations on the peptides' interaction with the keratin model demonstrated that electrostatic interactions are believed to be the main driving force stabilizing the complex. The molecular mechanics–Poisson-Boltzmann surface area methodology ...
Specific amino acids of Olive mild mosaic virus coat protein are involved in tr...
Varanda, Carla; Félix, Maria R.; Soares, Cláudio M.; Oliveira, Solange; Clara, M. IvoneAbstract: Transmission of Olive mild mosaic virus (OMMV) is facilitated by Olpidium brassicae (Wor.) Dang. An OMMV mutant (OMMVL11) containing two changes in the coat protein (CP), asparagine to tyrosine at position 189 and alanine to threonine at position 216, has been shown not to be Olpidium brassicae-transmissible owing to inefficient attachment of virions to zoospores. In this study, these amino acid chang...
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin
Broco, Manuela; Soares, Claudio M.; Oliveira, Solange; Mayhew, Stephen G; Rodrigues-Pousada, ClaudinaAbstract: Flavoredoxin participates in Desulfovibrio gigas thiosulfate reduction pathway. Its 3-dimensional model was generated allowing the oxidized riboflavin-5'-phosphate (FMN) site to be predicted. Residues likely to be involved in FMN-binding were identified (N29, W35, T56, K92, H131 and F164) and mutated to alanine. Fluorescence titration with apoprotein showed that FMN is strongly bound in the wild-type ...
Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,...
Araújo, Rita; Silva, Carla Manuela; O'Neill, Jaime Alexandre Antunes; Micaelo, N. M.; Gübitz, Georg M.; Soares, Cláudio M.; Casal, MargaridaCutinase from Fusarium solani pisi was genetically modified near the active site, by site-directed mutagenesis, to enhance its activity towards polyethylene terephthalate (PET) and polyamide 6,6 (PA 6,6) fibers. The mutations L81A, N84A, L182A, V184A and L189A were done to enlarge the active site in order to better fit a larger polymer chain. Modeling studies have shown enhanced free energy stabilization of mod...
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