Lty'sozynie vaTiants lacking sorne of the disulfide bends i-'ere studied in selutions containing TFE Ctritluuroethanol) which is known to jnducc hclical stnicture.The helieal centent induced by the addition ef 5eV, TFE vuried with the Tiumber of remaining S-S bonds, that is to say. it was largest for OSS-yaTiunt.while it was intermediate for 2SS-variants und mlnimized for wild-type.This indicates that rernaining S-S bunds suppress the forniation of excess helical structures, but
TheBiophysicalSociety of Japan General IncorporatedAssociation the basic folded conformaUon whercas the non 1ineaT shifts are attnbutable ]argely to the mcrease in the popu]atien of low lymg exLited state confor mations Thesc results mdiLate that the insertion of the Lys side chain into the hydrophobic Lore gTgnincantly increased the eonfermdtienal fiuctuanong ( and suggested a censerved higheT energy conformer for thetr comrnon tunLtional strategy the El E2 E3 cascade Tb find a 1ink ot such low populated highei energy cenformers to ubiquitin tuncUon we extended the approaeh mLo
Lty'sozynie vaTiants lacking sorne of the disulfide bends i-'ere studied in selutions containing TFE Ctritluuroethanol) which is known to jnducc hclical stnicture.The helieal centent induced by the addition ef 5eV, TFE vuried with the Tiumber of remaining S-S bonds, that is to say. it was largest for OSS-yaTiunt.while it was intermediate for 2SS-variants und mlnimized for wild-type.This indicates that rernaining S-S bunds suppress the forniation of excess helical structures, but
Abstract CD spectra of reduced and S‐3‐(trimethylated amino) propylated lysozyme (TMAP lysozyme) have been measured in various solutions containing guanidine hydrochloride or trifluoroethanol (TFE). The CD spectra indicate that there remain residual secondary structures in protein in aqueous solution. The addition of TFE further promotes the formation of secondary structures. In order to examine whether secondary structures are evenly induced over all the polypeptide chain, or locally at particular segments, the limited proteolysis of TMAP lysozyme by trypsin has been performed, and the CD spectra of all the final and intermediate products have been observed in solutions containing TFE. As a result, the fragments vary in a helix‐forming propensity. The CD spectra of peptide fragments T5, T7, T9T10, T12T13, T14T15T16, and T17T18 are not significantly affected by the addition of TFE, where T refers to the nomenclature of R. E. Canfield [(1963), Journal of Biological Chemistry , Vol. 238, pp. 2691–2697]. They are fragments of a helix‐breaking propensity. On the other hand, fragment 12 composed of T1‐T4, and fragments T6T7, T8, and T11, attain secondary structures with the addition of TFE. They are fragments of a helix‐forming propensity. Further, it is found that the fragments of a helix‐forming propensity just correspond to the helical segments in native lysozyme. We examine the interactions between neighboring fragments, which contribute to the stabilization of local structures along the polypeptide chain.
