1H nuclear magnetic resonance assignments and secondary structure of porcine C5ades Arg.
Sequence-specific assignments of the 1H nuclear magnetic resonance spectrum of porcine C5ades Arg are described. Assignments were facilitated by comparison of spectra obtained in H2O with partially exchanged spectra obtained in 2H2O. The sequence-specific assignments thus obtained were used to characterized the regular secondary structure in the protein, which is helical in the regions 2 to 11, 16 to 27, 35 to 41 and 45 to 64. The structure is very similar to that of human and bovine C5a.
Williamson
M P
MP
Roche Products Ltd, Welwyn Garden City, Herts, U.K.
D000595:Amino Acid Sequence; D000818:Animals; D003182:Complement C5 / Q000031:analogs & derivatives*; D015937:Complement C5a, des-Arginine; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D013552:Swine
D003182:Complement C5; D015937:Complement C5a, des-Arginine