Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix-forming or -breaking propensity of peptide segments
✍ Scribed by Shin-ichi Segawa; Takuji Fukuno; Keiro Fujiwara; Yasuo Noda
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 818 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
SYNOPSIS
CD spectra of reduced and S-3-(trimethylated amino) propylated lysozyme (TMAP lysozyme ) have been measured in various solutions containing guanidine hydrochloride or trifluoroethanol ( T F E ) . 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 a t 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),