13C nuclear magnetic resonance and circular dichroism studies of the tuftsin conformation in water.
13C-NMR and circular dichroic (CD) spectra of tuftsin and its analogues are discussed in connection with our hypothesis that the beta-turn is the biologically active conformation of tuftsin. The changes in CD spectra evoked by an increase in pH are interpreted as a demonstration of the increasing amount of beta-turn conformers in solution. Configurational changes in successive residues of tuftsin showed that residues 2 and 3 of the peptide chain are important for the tuftsin conformation.
D000596:Amino Acids / Q000032:analysis; D002942:Circular Dichroism; D007128:Immunoglobulin Fragments; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D014405:Tuftsin; D014867:Water
D000596:Amino Acids; D007128:Immunoglobulin Fragments; D014867:Water; D014405:Tuftsin