Studies on somatostatin with time-resolved spectroscopy and molecular dynamics simulations.
Somatostatin was studied by time-resolved fluorescence spectroscopy and by molecular dynamics simulations. The results obtained indicate the existence of mainly one conformation in DMSO, and the existence of several conformations in other solvents. Molecular dynamics simulations showed that the most important region for activity (residue 7-9) is also the most flexible region in the peptide.
Elofsson
A
A
Department of Medical Biophysics, Karolinska Institutet, Stockholm, Sweden.
Nilsson
L
L
Rigler
R
R
D003198:Computer Simulation; D004121:Dimethyl Sulfoxide; D011487:Protein Conformation; D012997:Solvents; D013004:Somatostatin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D012997:Solvents; D013004:Somatostatin; D014364:Tryptophan; D004121:Dimethyl Sulfoxide