Studies on barley trypsin inhibitor. II. Structural changes induced by denaturants and their reversibility.
No change in the activity of a trypsin inhibitor from barley was observed on treatment with heat and denaturants such as urea and guanidine hydrochloride. Thus, the conformational properties of the inhibitor were investigated. CD spectra of the native inhibitor were analysed on a curve-fitting technique using the data for poly-L-lysine...
D002942:Circular Dichroism; D004220:Disulfides; D006146:Guanidines; D001467:Hordeum; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D011487:Protein Conformation; D011489:Protein Denaturation; D013438:Sulfhydryl Compounds; D013696:Temperature; D014361:Trypsin Inhibitors; D014508:Urea
D004220:Disulfides; D006146:Guanidines; D046911:Macromolecular Substances; D013438:Sulfhydryl Compounds; D014361:Trypsin Inhibitors; D014508:Urea