. "JOURNAL OF PHYSICAL CHEMISTRY B" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "Free energy; metadynamics; sialic acid"@en . "[C0CBA35500A2]" . "Z(MSM6046137305)" . "Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation."@en . . . . . "The conformational free energy surface of alpha-N-acetylneuraminic acid (Neu5Ac, sialic acid) in the space of ring-puckering coordinates was calculated using the metadynamics method. Free energy surfaces in vacuum and with an explicit solvent were calculated in GLYCAM 06 force field. In vacuum three structures are almost equivalently populated, namely, the 2C5 chair and the B3,6/2S6 and OS3 boat/skew-boat conformations. The B3,6/2S6 structure is stabilized by an ionic hydrogen bond between the amide N-H bond and the carboxylic group. However, this structure is unfavorable in a water environment in which the experimentally observed 2C5 chair conformation is predicted to be more stable than the other structures. These results indicate that environment significantly influences conformation of Neu5Ac and that Neu5Ac-processing enzymes might modify a conformation of their substrates solely by a changing polarity of the environment. The structure of Neu5Ac bound in influenza neuraminidase (4S2/B2,5) belongs" . "Spiwok, Vojt\u011Bch" . . "The conformational free energy surface of alpha-N-acetylneuraminic acid (Neu5Ac, sialic acid) in the space of ring-puckering coordinates was calculated using the metadynamics method. Free energy surfaces in vacuum and with an explicit solvent were calculated in GLYCAM 06 force field. In vacuum three structures are almost equivalently populated, namely, the 2C5 chair and the B3,6/2S6 and OS3 boat/skew-boat conformations. The B3,6/2S6 structure is stabilized by an ionic hydrogen bond between the amide N-H bond and the carboxylic group. However, this structure is unfavorable in a water environment in which the experimentally observed 2C5 chair conformation is predicted to be more stable than the other structures. These results indicate that environment significantly influences conformation of Neu5Ac and that Neu5Ac-processing enzymes might modify a conformation of their substrates solely by a changing polarity of the environment. The structure of Neu5Ac bound in influenza neuraminidase (4S2/B2,5) belongs"@en . . "RIV/60461373:22330/09:00022337!RIV10-MSM-22330___" . "Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation." . . . . "113" . "Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation." . . . "22330" . . . "1520-6106" . "2"^^ . "6"^^ . "Conformational free energy surface of a-N-acetylneuraminic acid: An interplay between hydrogen bonding and solvation."@en . "000268139000033" . . "308070" . "Tvaro\u0161ka, Igor" . "1"^^ . "RIV/60461373:22330/09:00022337" .