Conformation of physalaemin.
The conformational and spatial configuration of the biologically active undecapeptide physalaemin was studied using 350-MHz1H NMR. The NMR analyses suggested the existence of a strong hydrogen bond between the amide proton of the Phe7 and a carbonyl group in the N-terminal moiety, most likely the Pro4 one. Other bondings were postulated, involving the side-chain amine of Lys6 and the side-chain amide of Asn5 and respectively the side-chain carboxyl of Asp3 and the terminal amide carbonyl of Met-NH2. Thus unlike its shorter peptidic fragments, physalaemin exhibited a stable molecular structure in solution, giving some insight into the conformation required for interaction at the biological receptor of tachykinins.
D006860:Hydrogen Bonding; D007705:Kinins; D009682:Magnetic Resonance Spectroscopy; D010803:Physalaemin; D011487:Protein Conformation; D012996:Solutions; D013055:Spectrophotometry, Infrared; D013696:Temperature
D007705:Kinins; D012996:Solutions; D010803:Physalaemin