Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1 beta.
1H alpha, 13C alpha, and 15N alpha secondary shifts, defined as the difference between the observed value and the random coil value, have been calculated for interleukin-1 receptor antagonist protein and interleukin-1 beta. Averaging of the secondary chemical shifts with those of adjacent residues was used to smooth out local effects and to obtain a correlation dependent on secondary structure. Differences and similarities in the placement of secondary structure elements in the primary sequences of these structurally homologous proteins are manifested in the smoothed secondary chemical shifts of all three types of nuclei. The close correlation observed between the secondary chemical shifts and the previously defined locations of secondary structure, as defined by traditional methods, exemplifies the advantage of chemical shifts to delineate regions of secondary structure.
Stockman
B J
BJ
Upjohn Laboratories, Upjohn Company, Kalamazoo, MI 49007.
Scahill
T A
TA
Strakalaitis
N A
NA
Brunner
D P
DP
Yem
A W
AW
Deibel
M R
MR
D000595:Amino Acid Sequence; D002244:Carbon; D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1 / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009584:Nitrogen; D017433:Protein Structure, Secondary; D011522:Protons; D017386:Sequence Homology, Amino Acid; D012795:Sialoglycoproteins / Q000737:chemistry*
D053590:Interleukin 1 Receptor Antagonist Protein; D007375:Interleukin-1; D011522:Protons; D012795:Sialoglycoproteins; D002244:Carbon; D009584:Nitrogen