The influence of configuration changes in tuftsin peptide chain on its folding properties.
IR spectra of ten tuftsin structural analogues containing D-amino acid residues were investigated in solid state, and in chloroform and carbon tetrachloride solutions. The effect of configurational changes on folding ability of the peptide and on formation of beta-bend structure seems to depend on the position of the altered residue.
D007128:Immunoglobulin Fragments; D011487:Protein Conformation; D012996:Solutions; D013329:Structure-Activity Relationship; D014405:Tuftsin
D007128:Immunoglobulin Fragments; D012996:Solutions; D014405:Tuftsin