Simulations of conformers of tuftsin and a cyclic tuftsin analog

C. V H D Valdeavella Blatt, Bernard Pettitt

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 β-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 β- nor a γ-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.

Original languageEnglish (US)
Pages (from-to)372-380
Number of pages9
JournalInternational Journal of Peptide and Protein Research
Volume46
Issue number5
StatePublished - 1995
Externally publishedYes

Fingerprint

Tuftsin
Isomers
Peptides
Conformations
Water
Hydrogen bonds
Molecular Dynamics Simulation
Hydrogen Bonding
Hydrogen
Salts
Molecular dynamics
Computer simulation

Keywords

  • β-Turn
  • Salt effects
  • Solution conformation
  • Tuftsin analog

ASJC Scopus subject areas

  • Biochemistry

Cite this

Simulations of conformers of tuftsin and a cyclic tuftsin analog. / Valdeavella Blatt, C. V H D; Pettitt, Bernard.

In: International Journal of Peptide and Protein Research, Vol. 46, No. 5, 1995, p. 372-380.

Research output: Contribution to journalArticle

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