Topology in Molecular Biology

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144 A.E. Kister et al.


proposed search algorithm compares favorably with the powerful and widely
used techniques based on hidden Markov Models.
Another advantage of carrying out a structure-based analysis is that it
often allows one not only to predict the affiliation of a particular protein and
outline its secondary and 3D structure, but also to make “educated guesses”
about functional role of various portions of the sequence. It is evident that
an ability to pinpoint parts of protein sequence that is likely to take part in
protein binding, for example, can prove invaluable for planning mutagenesis
experiments or rational drug design.


References



  1. National center for biotechnology information. http://www.ncbi.nlm.nih.gov/

  2. H.M. Berman, J.Z. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig,
    I.N. Shindyalov, P.E. Bourne, Nucleic Acids Res. 28 , 235–242 (2000).
    http://www.rcsb.org/pdb/

  3. A.G. Murzin, S.E. Brenner, T. Hubbard, C. Chothia, J. Mol. Biol. 247 , 536–540
    (1995). http://scop.mrc-lmb.cam.ac.uk/scop/

  4. C.B. Anfinsen, Science 181 , 223–230 (1973)

  5. E.E. Lattman, G.D. Rose, Proc. Natl Acad. Sci. USA 90 , 439–441 (1993)

  6. T.C. Wood, W.R. Pearson, J. Mol. Biol. 291 , 977–995 (1999)

  7. A.A. Schaffer, L. Aravind, T.L. Madden, S. Shavirin, J.L. Spouge, Y.I. Wolf,
    E.V. Koonin, S.F. Altschul, Nucleic Acids Res. 29 (14)2994–3005 (2001).
    http://www.ncbi.nlm.nih.gov/BLAST/

  8. W.R. Pearson, D.J. Lipman, Proc. Natl Acad. Sci. USA 85 , 2444–2448 (1988)

  9. J. Park, K. Karplus, C. Barret, R. Hughey, D. Haussler, T. Hubbard, C. Chothia,
    J. Mol. Biol. 284 , 1201–1210 (1998)

  10. C. Chothia, A.M. Lesk, EMBO J. 5 , 823–826 (1986)

  11. C. Chothia, A.M. Lesk, I.M. Gelfand, A.E. Kister, in,Why Structure Changes
    More Slowly Than Sequence in Protein Evolution, Simplicity and Complexity in
    Proteins and Nucleic acidsed. by H. Frauenfelder, J. Deisenhofer, P.G. Wolynes.
    (Dantem University Press 1999), pp. 281–295

  12. C. Chothia, I.M. Gelfand, A.E. Kister, J. Mol. Biol. 278 , 457–479 (1995)

  13. C. Chothia, T. Hubbard, S. Brenner, H. Barns, A. Murzin, Biomol. Struct. 26 ,
    597–627 (1997)

  14. C.A. Orengo, A.D. Michie, S. Jones, D.T. Jones, M.B. Swindells, J.M. Thornton,
    Structure 5 (8), 1093–1108 (1997)

  15. J.S. Richardson, Adv. Protein Chem. 34 , 167–339 (1981)

  16. J.S. Richardson, D. Richardson, Natl Acad. Sci. USA 99 , 2754–2759 (2002)

  17. A.D. McLachlan, J. Mol. Biol. 128 , 49–79 (1979)

  18. I. Ruczinski, C. Kooperberg, R. Bonneau, D. Baker, Proteins 48 , 85–97 (2002)

  19. A.G. Murzin, A.M. Lesk, C. Chothia, J. Mol. Biol., 236 , 1369–1381 (1994a)

  20. A.G. Murzin, A.M. Lesk, C. Chothia, J. Mol. Biol., 236 , 1382–1400 (1994b)

  21. N. Nagano, C.A. Orengo, J.M. Thornton, J. Mol. Biol. 321 , 741–765 (2002)

  22. R.E. Steward, J.M. Thornton, Proteins 48 , 178–191 (2002)

  23. F.A. Syud, H.E. Stanger, H.S. Mortell, J.F. Espinosa, J.D. Fisk, C.G. Fry,
    S.H. Gellman, J. Mol. Biol., 326 , 553–568 (2003)

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