Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance.
The 1H nuclear magnetic resonance (n.m.r.) assignments for the aromatic spin systems of the four tyrosines and four phenylalanines in the basic pancreatic trypsin inhibitor (BPTI) were reinvestigated using novel 13C-1H heteronuclear two-dimensional experiments. Resonance lines which are degenerate in homonuclear 1H n.m.r. spectra could thus be resolved. Based on this new evidence the previous assignments for Phe22 and Phe33 had to be corrected. This affects the earlier conclusions on aromatic ring flips in BPTI in that Phe22 is rotating rapidly on the n.m.r. time scale at 36 degrees C, rather than being immobilized up to 80 degrees C.
D000595:Amino Acid Sequence; D007611:Aprotinin; D009682:Magnetic Resonance Spectroscopy / Q000379:methods
D007611:Aprotinin