Abstract
1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.
Dates
Type | When |
---|---|
Created | 10 years ago (Aug. 10, 2015, 4:12 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 26, 2021, 12:57 p.m.) |
Indexed | 1 year, 1 month ago (July 11, 2024, 7:17 a.m.) |
Issued | 47 years, 1 month ago (Aug. 1, 1978) |
Published | 47 years, 1 month ago (Aug. 1, 1978) |
Published Print | 47 years, 1 month ago (Aug. 1, 1978) |
@article{Crewther_1978, title={Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment}, volume={173}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1730365}, DOI={10.1042/bj1730365}, number={2}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Crewther, W G and Inglis, A S and McKern, N M}, year={1978}, month=aug, pages={365–371} }