A comparative study of carboxy myoglobin in saccharide-water systems by molecular dynamics simulation.
Results from room-temperature molecular dynamics simulation on a system containing carboxy-myoglobin, water, and maltose molecules are reported. Protein atomic fluctuations, protein-solvent and solvent-solvent hydrogen bonding have been analyzed and compared to the ones in trehalose-water and sucrose-water systems (Proteins 2005, 59, 291-302). Results help in rationalizing, at a molecular level, the effects of homologues disaccharides on protein structure/dynamics experimentally observed. Furthermore, the effectiveness of disaccharides in bioprotection in terms of peculiar protein-matrix coupling is also discussed.
Cottone
Grazia
G
Dipartimento di Scienze Fisiche ed Astronomiche, Università Degli Studi di Palermo and CNISM, Via Archirafi 36, I-90123 Palermo, Italy. cottone@fisica.unipa.it
D003198:Computer Simulation; D006860:Hydrogen Bonding; D008320:Maltose / Q000737:chemistry*; D008956:Models, Chemical; D009211:Myoglobin / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013395:Sucrose / Q000737:chemistry*; D014199:Trehalose / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D009211:Myoglobin; C018013:carboxymyoglobin; D014867:Water; D013395:Sucrose; D008320:Maltose; D014199:Trehalose