Skip to main content

Part of the book series: Lecture Notes in Computer Science ((LNBI,volume 2666))

  • 522 Accesses

Abstract

During the last decade, it has been shown that several properties of natural proteins can be captured by simple models, such as 2-D or 3-D lattice models [1, 2, 5, 6, 9, 11, 13]. In these models, the protein is figured as a chain of beads occupying the sites of a lattice in a self avoiding way.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bornberg-Bauer, E.: How are model protein structures distributed in sequence space? Biophys. J. 73(5), 2393–2403 (1997)

    Article  Google Scholar 

  2. Chan, H., Dill, K.: Compact polymers. Macromolecules 22(12), 4559–4573 (1989)

    Article  Google Scholar 

  3. Chorev, M., Goodman, M.: Recent developments in retro peptides and proteins -an ongoing topochemical exploration. Trends Biotechnol. 13, 438–445 (1995)

    Article  Google Scholar 

  4. Ejtehadi, M., Hamedani, N., Seyed-Allaei, H., Shahrezaei, V., Yahyanejad, M.: Stability of preferable structures for a hydrophobic-polar model of protein folding. Phys. Rev. E 57(3), 3298–3301 (1998)

    Article  Google Scholar 

  5. Go, N.: The consistency principle in protein-structure and pathways of folding. Adv. Biophys. 18, 149–164 (1984)

    Article  Google Scholar 

  6. Li, H., Helling, R., Tang, C., Wingreen, N.: Emergence of preferred structures in a simple model of protein folding. Science 273, 666–669 (1996)

    Article  Google Scholar 

  7. Li, C., Tang, C., Wingreen, N.: Nature of driving force for protein folding: A result from analyzing the statistical potential. Phys. Rev. letters 79(4), 765–768 (1997)

    Article  Google Scholar 

  8. Li, H., Tang, C., Wingreen, N.: Are protein folds atypical? Proc. Natl. Acad. Sci. USA 95(9), 4987–4990 (1998)

    Article  Google Scholar 

  9. Pande, V., Rokhsar, D.: Folding pathway of a lattice model for proteins. Proc. Natl. Acad. Sci. USA 96(4), 1273–1278 (1999)

    Article  Google Scholar 

  10. Raghunathan, G., Jernigan, R.: Ideal architecture of residue packing and its observation in protein structures. Protein Sci. 6(10), 2072–2083 (1997)

    Article  Google Scholar 

  11. Sali, A., Shakhnovich, E., Karplus, M.: How does a protein fold? Nature 369, 248–251 (1994)

    Article  Google Scholar 

  12. Shemyakin, M., Ovchinnikov, Y., Ivanov, V.: Topochemical investigations of peptide systems. Angew. Chem. Int. Ed. Engl. 8, 492–499 (1968)

    Article  Google Scholar 

  13. Trinquier, G., Sanejouand, Y.-H.: New protein-like properties of cubic lattice models. Phys. Rev. E 59(1), 942–946 (1999)

    Article  Google Scholar 

  14. Wales, D., Doye, J.: Global optimization by basin-hopping and the lowest energy structures of lennard-jones clusters containing up to 110 atoms. J. Phys. Chem. A 101, 5111–5116 (1997)

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2003 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

Sanejouand, YH., Trinquier, G. (2003). Proteinlike Properties of Simple Models. In: Guerra, C., Istrail, S. (eds) Mathematical Methods for Protein Structure Analysis and Design. Lecture Notes in Computer Science(), vol 2666. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-44827-3_11

Download citation

  • DOI: https://doi.org/10.1007/978-3-540-44827-3_11

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-40104-9

  • Online ISBN: 978-3-540-44827-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics