1H n.m.r. parameters of the N-terminal 19-residue S-peptide of ribonuclease in aqueous solution.
The 1H n.m.r. chemical shifts and the spin-spin coupling constants of the N-terminal 19-residue S-peptide of ribonuclease A have been measured in a 10 mM solution in D2O, pD 3.0, 27 degrees, at 300 MHz. The titration parameters for end groups Lys-1 and Ala-19 and side chains Lys-1, Glu-2, Lys-7, Glu-9, Arg-10, His-12 and Asp-14 have been determined at 90 MHz. An assignment of observed signals to individual residue protons based upon characteristic shifts, spectral analysis, double resonance, titration shifts and comparison with the spectrum of C-peptide (N-terminal 13-residue) is proposed. Differences in the observed chemical shifts, pKa's and titration shifts with reference to those proposed as "random coil" parameters are not large enough to assume the existence of a significant population of secondary structure in the conditions studied. The H alpha chemical shifts differences can be accounted for by the Phe-8 phenyl ring current for an extended peptide backbone conformation and appropriate values for the torsion angles chi 1 Phe-8 and chi 2 Phe-8.
D000595:Amino Acid Sequence; D004722:Endoribonucleases; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments; D011487:Protein Conformation; D012259:Ribonuclease, Pancreatic; D012260:Ribonucleases
D010446:Peptide Fragments; C023560:ribonuclease S-peptide; D004722:Endoribonucleases; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic