[Conformation of trypsin molecules in aqueous solutions containing 2-chloroethanol].
Changes in the macromolecular parameters of trypsin in the presence of 2-chloroethanol in aqueous solutions have been studied by means of optical and hydrodynamic methods. At temperature--dependent volume fraction of 2-chloroethanol in solution upsilon t < 0.30 the globular structure of trypsin is destroyed but the regularity of polypeptide chains within the limits of secondary structure is maintained. At 0.30 < upsilon < 0.80 the solvation envelope of macromolecules is kept constant mainly owing to hydration, but the solubilization takes place only at upsilon < 0.30. At upsilon < 0.80 spiralization sharply increases and reaches in pure 2-chloroethanol its maximum value (50%). The intrinsic viscosity moreover reaches only half the whole value [eta]coil--[eta]glob.
D005023:Ethylene Chlorohydrin; D008956:Models, Chemical; D009905:Optical Rotatory Dispersion; D011487:Protein Conformation; D012996:Solutions; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D014357:Trypsin; D014783:Viscosity; D014867:Water
D012996:Solutions; D014867:Water; D005023:Ethylene Chlorohydrin; D014357:Trypsin
Konformatsiia molekul tripsina v vodnykh rastvorakh, soderzhashchikh 2-khlorétanol.