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. 1978 Aug 1;173(2):373–385. doi: 10.1042/bj1730373

Amino acid sequences of alpha-helical segments from S-carbosymethylkerateine-A. Complete sequence of a type-I segment.

K H Gough, A S Inglis, W G Crewther
PMCID: PMC1185789  PMID: 697725

Abstract

The amino acid sequence of a type-I helical segment from the low-sulphur protein (S-carboxymethylkerateine-A) of wool was determined by combining automatic and manual-sequencing data. Whereas in the type-II helical segment most of the cationic groups occur in pairs, 11 of the 22 anionic residues in the sequence of the type-I segment were situated next to a second anionic residue. This suggests possible interactions between type-I and type-II helical segments in alpha-keratin. As observed with the sequence of a type-II helical segment a model constructed on 3.6 residues per turn of helix shows a line of hydrophobic residues along the helix, thereby supporting the physicochemical evidence that the molecule is predominantly helical and forms part of a coiled-coil structure. Examination of the sequence data by predictive methods indicates the possibilty of extensive sections of alpha-helix interspersed with discontinuities. The molecule contains a number of regions with peptide sequences identical with those found by other workers after enzymic digestion of fractions from oxidized wool.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AMBLER R. P. THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:349–378. doi: 10.1042/bj0890349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CRICK F. H. C. Is alpha-keratin a coiled coil? Nature. 1952 Nov 22;170(4334):882–883. doi: 10.1038/170882b0. [DOI] [PubMed] [Google Scholar]
  3. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  4. Corfield M. C., Fletcher J. C. Amino acid sequences of peptides from a chymotryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool. Biochem J. 1969 Nov;115(2):323–334. doi: 10.1042/bj1150323. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Corfield M. C., Fletcher J. C., Robson A. Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool. Biochem J. 1967 Mar;102(3):801–814. doi: 10.1042/bj1020801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Crewther W. G., Harrap B. S. The preparation and properties of a helix-rich fraction obtained by partial proteolysis of low sulfur S-carboxymethylkerateine from wool. J Biol Chem. 1967 Oct 10;242(19):4310–4319. [PubMed] [Google Scholar]
  7. Crewther W. G., Inglis A. S. Automatic procedures for determining amino acid sequences of peptides. Anal Biochem. 1975 Oct;68(2):572–585. doi: 10.1016/0003-2697(75)90653-3. [DOI] [PubMed] [Google Scholar]
  8. Crewther W. G., Inglis A. S., McKern N. M. Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment. Biochem J. 1978 Aug 1;173(2):365–371. doi: 10.1042/bj1730365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Easley C. W. Combinations of specific color reactions useful in the peptide mapping technique. Biochim Biophys Acta. 1965 Sep 13;107(2):386–388. doi: 10.1016/0304-4165(65)90147-9. [DOI] [PubMed] [Google Scholar]
  10. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  11. Elleman T. C., Crewther W. G., Van Der Touw J. Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Statistical analysis. Biochem J. 1978 Aug 1;173(2):387–391. doi: 10.1042/bj1730387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. FRAENKEL-CONRAT H., HARRIS J. I., LEVY A. L. Recent developments in techniques for terminal and sequence studies in peptides and proteins. Methods Biochem Anal. 1955;2:359–425. doi: 10.1002/9780470110188.ch12. [DOI] [PubMed] [Google Scholar]
  13. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hogg D. M., Dowling L. M., Crewther W. G. Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Tryptic and chymotryptic peptides from a type-II segment. Biochem J. 1978 Aug 1;173(2):353–363. doi: 10.1042/bj1730353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Inglis A. S., Nicholls P. W. Identification of phenylthiohydantoins of amino acids by thin-layer chromatography. J Chromatogr. 1973 May 16;79:344–346. doi: 10.1016/s0021-9673(01)85310-3. [DOI] [PubMed] [Google Scholar]
  16. Inglis A. S., Nicholls P. W., Roxburgh C. M. Hydrolysis of the peptide bond and amino acid modification with hydriodic acid. Aust J Biol Sci. 1971 Dec;24(6):1235–1240. doi: 10.1071/bi9711235. [DOI] [PubMed] [Google Scholar]
  17. Moffitt W., Yang J. T. THE OPTICAL ROTATORY DISPERSION OF SIMPLE POLYPEPTIDES. I. Proc Natl Acad Sci U S A. 1956 Sep;42(9):596–603. doi: 10.1073/pnas.42.9.596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  19. PAULING L., COREY R. B. Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type. Nature. 1953 Jan 10;171(4341):59–61. doi: 10.1038/171059a0. [DOI] [PubMed] [Google Scholar]
  20. Parry D. A., Crewther W. G., Fraser R. D., MacRae T. P. Structure of alpha-keratin: structural implication of the amino acid sequences of the type I and type II chain segments. J Mol Biol. 1977 Jun 25;113(2):449–454. doi: 10.1016/0022-2836(77)90153-x. [DOI] [PubMed] [Google Scholar]
  21. Robson B., Suzuki E. Conformational properties of amino acid residues in globular proteins. J Mol Biol. 1976 Nov 5;107(3):327–356. doi: 10.1016/s0022-2836(76)80008-3. [DOI] [PubMed] [Google Scholar]
  22. Woods K. R., Wang K. T. Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967 Feb 21;133(2):369–370. doi: 10.1016/0005-2795(67)90078-5. [DOI] [PubMed] [Google Scholar]

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