Magnetization-transfer n.m.r. investigation of the hydrogen exchange in H2O of the peptide fragment B23-B29 of insulin.
Detailed and precise information on the exchanges in water of the peptide hydrogens of the insulin fragment B23-B29 (Gly23-Phe24-Phe25-Tyr26-Thr27-Pro28 -Lys29) has been obtained from magnetization-transfer measurements, and nonlinear least-squares fits of the experimental spectra using the expression for the discrete Fourier transform of a sum of exponentially damped sinusoids. From a comparison of the differential exchange rates with those expected for completely solvent-exposed peptide hydrogens, specific conformational features of the heptapeptide are suggested.
Abildgaard
F
F
Department of Chemistry, University of Copenhagen, Denmark.
Led
J J
JJ
Balschmidt
P
P
Hansen
F B
FB
D000595:Amino Acid Sequence; D000818:Animals; D006859:Hydrogen / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000032:analysis*; D007474:Ion Exchange; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis*; D011522:Protons; D013552:Swine; D013696:Temperature; D014867:Water
D007328:Insulin; D010446:Peptide Fragments; D011522:Protons; D014867:Water; D006859:Hydrogen