Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions.
alpha-Helix formation in the S-peptide (residues 1-19 of ribonuclease A) was studied in detail by use of two-dimensional 1H nuclear magnetic resonance to monitor the effects of 2,2,2-trifluoroethanol (TFE) at 0 degrees C and pH* 2.07. TFE stabilizes the S-peptide alpha-helix. Helix formation by a particular amino acid was monitored by the chemical shifts of the C alpha, C beta, and C gamma protons while increasing the concentration of TFE: large changes in chemical shift of a particular residue indicate that it is induced to go helical, whereas small chemical shift changes indicate little helix formation. Residues Thr-3 to Met-13 undergo chemical shift changes consistent with helix formation, whereas the other residues do not. Earlier work [Kim, P. S., & Baldwin, R. L. (1984) Nature 307, 329-334] reported that residues Thr-3 to His-12 become helical in aqueous solution. The existence of a "helix stop signal" was inferred from this behavior. We thus conclude that this helix stop signal persists in TFE solutions.
Nelson
J W
JW
Department of Biochemistry, Louisiana State University, Baton Rouge 70803.
Kallenbach
N R
NR
D000596:Amino Acids / Q000032:analysis; D004735:Energy Transfer; D000431:Ethanol / Q000031:analogs & derivatives; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000032:analysis*; D021382:Protein Sorting Signals; D011522:Protons; D012259:Ribonuclease, Pancreatic / Q000032:analysis*; D012996:Solutions; D013696:Temperature; D014270:Trifluoroethanol
D000596:Amino Acids; D010446:Peptide Fragments; D021382:Protein Sorting Signals; D011522:Protons; D012996:Solutions; C060871:ribonuclease A S-peptide; D000431:Ethanol; D014270:Trifluoroethanol; D012259:Ribonuclease, Pancreatic