Evaluation of the secondary structure of vaccinia-virus thymidine kinase by circular-dichroism spectroscopy of overlapping synthetic peptides

European Journal of Biochemistry

Volumn 241, Issue 1, 1996, Pages 126-132

  Behrends, Henrik W ^a   Beck Sickinger, Annette G ^a   Folkers, Gerd ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Circular dichroism; Secondary structure prediction; Tartiary structure validation; Thymidine kinase

Indexed keywords

THYMIDINE KINASE;

AMINO ACID ANALYSIS; ARTICLE; CIRCULAR DICHROISM; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; VACCINIA VIRUS;

GOSSYPIUM HIRSUTUM; VACCINIA; VACCINIA VIRUS;

EID: 0029850684     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0126t.x     Document Type: Article

References (30)

1. Andrade, M. A., Chacun, P., Merelo, J. J. & Moran, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6, 383-390.
2. Beck, W. & Jung, G. (1994) Convenient reduction of S-oxides in synthetic peptides lipopeptides and peptide libraries. Lett. Pet. Sci. 1, 31-37.
3. Behrends, H. W., Folkers. G. & Beck-Sickinger, A. G. (1996) A new approach to secondary structure evaluation: secondary structure prediction of porcine adenylate kinase and yeast guanylate kinase by circular dichroism spectroscopy of overlapping synthetic peptide segments. Biopolymers, in the press.
4. Berger, A., Schiltz, E. & Schulz., G. E. (1989) Guanylate kinase from Saccharomyces cerevisiae. Eur. J. Biochem. 184, 433-445.
5. Black, M. E. & Hubry, D. E. (1990a) Quaternary structure of vacciniavirus thymidine kinase. Biochem. Biophys. Res. Commun. 169, 1080-1086.
6. Black, M. E. & Hubry, D. E. (1990b) Identification of the ATP-binding domain of vaccinia-virus thymidine kinase. J. Biol. Chem. 265, 17584-17592.
7. Black, M. E. & Hubry. D. E. (1991) Structure and function of vaccinia virus thymidine kinase: biomedical relevance and implications for antiviral drug design. Rev. Med Virol. 1, 235-245.
8. Blundell, T., Sibanda, B. L., Sternberg. M. J. K. & Thornton. J. M. (1987) Knowledge-based prediction of protein structures and the design of novel molecules. Nature 32, 347-352.
9. Blundeell, T., Carney, D., Gardner. S., Hayes, F., Howlin, B., Hubbard, T., Overington, J., Singh, D. A., Sibanda, B. L. & Sutcliffe. M. (1988) Knowledge-based protein modelling and design, Eur. J. Biochem. 172, 513-520.
10. Bodkin, M. J. & Goodfellow, J. M. (1995) Competing interactions contributing to α-helical stability in aqueous solution, Protein Sci. 4, 603-612.
11. Brahms, S. & Brahms, J. (1980) Determination of protein secondary structure in solution by vacuum UV circular dichroism, J. Mol. Biol. 138, 149-178.
12. Chothia, C. & Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins. EMBO J. 5, 823-826.
13. Dreusicke, D. & Schulz., G. E. (1986) The glycine-rich loop of adenylate kinase forms a giant anion hole. FEBS Lett. 208, 301-304.
14. Dreusicke, D., Karplus, P. A. &. Schulz, G. H. (1988) Refined structure of porcine cytosolic adenylate kinase at 2.1 Ä resolution. J. Mol. Biol. 199, 359-371.
15. Greenfield, N. & Fasman, G. D. (1969) Computer circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8. 4108-4116.
16. Haris, P. I. & Chapman, D. (1995) The conformational analysis of peptides usina Fourier transform IR spectroscopy. Biopolymers 37, 251-263.
17. Hennessey, J. P. & Johnson, W. C. (1981) Information content in the circular dichroism of proteins. Biochemistry 20, 1085-1094.
18. Jung, G. & Beck-Sickinger, A. G. (1992) Multiple peptide synthesis methods and their applications. Angew chem .Int. Ed. Engl.31, 367-383.
19. Manavalan, P. & Johnson, W. C. (1985) Protein secondary structure from circular dichroism spectra. J. Biosci. 8, 141-149.
20. Merrifield, R. B. (1963) Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 85, 2149-2154.
21. Perczel, A. & Fasman, G. D. (1991) Convex constraint analysis: A natural deeonvolution of circular dichroism curves of proteins. Protein Eng. 4, 669-679.
22. Provencher, S. & Glöckner,. J. (1981) Estimation of globular secondary structure from circular dichroism, Biochemistry 20, 33-37.
23. Qian, N. & Sejnowski, T. J. (1988) Predicting the secondary structure of globular proteins using neural network models, J. Mol Biol. 202, 865-884.
24. Rost, B. & Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol 232, 584-599.
25. Schulz. G. E. (1992) Binding of nucleotides by proteins, Curr. Opin. Struct. Biol. 2, 61-67.
26. Wagner, M. J., Sharp, J. A. & Summers, W. C. (1981) Nucleotide sequence of the thimidine kinase gene of herpes simplex virus type 1. Proc. Natl Acad. Sci. USA 78, 1441-1445.
27. Waterhouse. D. V. & Johnson, W. C. Jr (1994) Importance ot environment in determining secondary structure in proteins, Biochemistry 33, 2121-2128.
28. Wild, K., Bohner, T., Aubry, A., Folkers, G. & Schulz, G. H. (1995) The three-dimensional structure of thymidine kinase from herpes simplex virus type 1, FEBS Lett. 338, 289-292.
29. Woody, R. W. (1985) Cireular dichroism of peptides, Peptides (Orlando) 7, 16-114.
30. Yang, J. T., Wu, C.-S. C. & Martinez, H. M. (1986) Calculation of protein conformation from circular diehroism. Method Enzymol. 130, 208-269.