Peptide T exhibits a well-defined structure in fluorinated solvent at low temperature.
The structure of Peptide T was determined by solution NMR spectroscopy, under strong structure-inducing conditions: 40% hexafluoro-2-propanol aqueous solution at 5 degrees C. Under these conditions it was possible to detect medium-range NOEs for the first time for this peptide. This allowed a much better-defined structure to be determined for Peptide T in comparison with earlier NMR and computational studies. Peptide structures consistent with the experimental restraints were generated using a restrained MD simulation with a full empirical force field. Residues 4-8 of Peptide T take on a well-defined structure with a heavy atom RMSD of 0.78 A. The structure is stabilized by hydrogen bonding to side-chain oxygen atoms of Thr 4 and Thr 8, as well as backbone hydrogen bonding between residues 5 and 7 that forms this region into a classic gamma-turn.
Yang
Tran-Chin
TC
Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada.
Rendell
Jennifer
J
Gulliver
Wayne
W
Booth
Valerie
V
D000595:Amino Acid Sequence; D003080:Cold Temperature; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D015717:Peptide T / Q000737:chemistry* / Q000235:genetics; D020005:Propanols / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D012997:Solvents / Q000737:chemistry*; D006845:Hydrocarbons, Fluorinated
D015717:Peptide T; D020005:Propanols; D012997:Solvents; C001337:hexafluoroisopropanol; D006845:Hydrocarbons, Fluorinated