SMS 201-995, an octapeptide somatostatin analogue. Assignment of the 1H 500 MHZ n.m.r. spectra and conformational analysis of SMS 201-995 in dimethylsulfoxide.
The possible conformations of SMS 201-995, an active analogue of somastostatin, have been studied in dimethylsulfoxide solution by 500 MHz proton n.m.r. spectroscopy. The assignments have been made by use of 2D-correlated methods to detect long-range coupling connectivities in aromatic residues and between the alpha protons of consecutive residues. NOESY experiments enabled us to correlate amide and alpha protons of neighbouring amino acid residues, which indicate a less flexible situation than in water. Measurements of temperature coefficients of the amide protons, of NH-C alpha H coupling constants and NOE effects are in favour of one predominant conformation with a beta turn, of type II', involving amino acids Phe3 to Thr6.
Wynants
C
C
Van Binst
G
G
Loosli
H R
HR
D000595:Amino Acid Sequence; D004121:Dimethyl Sulfoxide; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D015282:Octreotide; D011487:Protein Conformation; D013004:Somatostatin / Q000031:analogs & derivatives*
D013004:Somatostatin; D015282:Octreotide; D004121:Dimethyl Sulfoxide