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.