Conformation of four peptides corresponding to the alpha-helical segments of human GM-CSF.
The conformation of segments corresponding to the four alpha-helical stretches found in human granulocyte-macrophage colony-stimulating factor was studied in water solution in the presence of different amounts of 2,2,2-trifluoroethanol (TFE). The CD spectra reveal the onset of secondary structure upon addition of TFE. The final amount of helical conformation varies among the four peptides. In all cases, the conformational transition is complete before 50% TFE (v/v). 1H-NMR studies were conducted at this solvent composition, leading to the assignment of all the resonances and to the definition of the secondary structure for all four fragments.
Fiori
S
S
University of Padova, Department of Organic Chemistry, CNR, Italy.
Mammi
S
S
Peggion
E
E
Rovero
P
P
Pegoraro
S
S
Revoltella
R P
RP
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D016178:Granulocyte-Macrophage Colony-Stimulating Factor / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D010455:Peptides; D016178:Granulocyte-Macrophage Colony-Stimulating Factor