Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 2 and 5 in peptide chain.
Conformational preferences of a group of hexapeptides containing two dehydroamino acid residues in Positions 2 and 5 in peptide chain were investigated by means of spectroscopic methods (NMR and CD) and theoretical calculations. In the case of dimethylsulfoxide (DMSO) solution, only peptide with free N-termini adopted rigid 3(10)-helical conformation, for the rest of examined peptides extended and "zig-zag" conformers were predominant. CD measurements showed that only in chloroform solution the conformational freedom of investigated peptides was restricted.
Latajka
Rafal
R
Faculty of Chemistry, Department of Bioorganic Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland. rafal.latajka@pwr.wroc.pl
Jewginski
Michal
M
Makowski
Maciej
M
Krezel
Artur
A
Paluch
Slawomir
S
D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011522:Protons; D013696:Temperature
D000577:Amides; D000596:Amino Acids; D010455:Peptides; D011522:Protons