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• W2034073886 abstract "The conformational properties of the configurational isomers of tuftsin, a linear tetrapeptide with the sequence Thr-Lys-Pro-Arg, were investigated with six 1 ns molecular dynamics simulations in explicit water and in a 1.0 m NaCl solution. The average conformation of the cis isomer is a type VI beta-turn. Our results indicate that water-peptide hydrogen bonding, in addition to intramolecular hydrogen bonds, stabilizes the cis conformer. The trans isomer is neither a beta- nor a gamma-turn. Results are compared with parallel studies on a cyclic analog of tuftsin, cyclo(Thr-Lys-Pro-Arg-Gly). The addition of salt does, not influence the backbone conformation of the peptide. Differences between the structures are confined to the side-chain orientations of the Lys and Arg residues." @default.
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• W2034073886 date "2009-01-12" @default.
• W2034073886 modified "2023-09-26" @default.
• W2034073886 title "Simulations of conformers of tuftsin and a cyclic tuftsin analog" @default.
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• W2034073886 doi "https://doi.org/10.1111/j.1399-3011.1995.tb01071.x" @default.
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