Structural differences between erabutoxins in aqueous solution and in crystalline states.
The snake venom toxins erabutoxin a and b, have been studied in detail in aqueous solution over a wide pH range by proton NMR spectroscopy. Great care has been taken particularly to assign and locate in the structure residue histidine-7 with reference to other amino-acid sidechains. It lies in a pocket away from the surface in agreement with its lack of chemical reactivity. The data are not consistent with two structure determinations in crystals by X-ray diffraction. The aqueous solution conformation explains in greater depth the observed essentially of amino acids to the activity of the toxin.
D003460:Crystallization; D004546:Elapid Venoms; D004870:Erabutoxins; D005035:Ethylmercury Compounds; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012996:Solutions; D014961:X-Ray Diffraction
D004546:Elapid Venoms; D005035:Ethylmercury Compounds; D012996:Solutions; C026835:ethylmercury phosphate; D004870:Erabutoxins