Skip to main content
Log in

Prot-Prop: J-tool to predict the subcellular location of proteins based on physiochemical characterization

  • Published:
Interdisciplinary Sciences: Computational Life Sciences Aims and scope Submit manuscript

Abstract

PROT-PROP is a computational tool to characterize 27 physicochemical properties of a protein along with its subcellular location (intra or extra) in a single-window application. Other significant features of this software include calculation of numerical values for hydrophobicity, hydrophilicity; composition of small and large amino acids; net hydrophobic content in terms of low/high; and Navie’s algorithm to calculate theoretical pI. PROT-PROP is an easy-to-install platform independent implementation of JAVA under a user-friendly interface. It is a standalone version as a virtual appliance and source code for platforms supporting Java 1.5.0 and higher versions, and downloadable from the web http://www.mzu.edu.in/schools/biotechnology.html. PROT-PROP can run under Windows and Macintosh Operating Systems. PROT-PROP is distributed with its source code so that it may be adapted or customized, if desired.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Aftabuddin, M., Kundu, S. 2007. Hydrophobic, hydrophilic and charged amino acid networks within protein. Biophysic J 93, 225–231.

    Article  CAS  Google Scholar 

  2. Ahmad, S., Sarai, A. 2004. Qgrid: Clustering tool for detecting charged and hydrophobic regions in proteins. Nucl Acid Res 32, 104–107.

    Article  Google Scholar 

  3. Ali, V., Nozaki, T. 2007. Current therapeutics, their problems and sulfur-containing-amino acid metabolism as a novel target against infections by amitochondriate protozoan parasites. Clin Microbiol Rev 20, 164–187.

    Article  PubMed  CAS  Google Scholar 

  4. Almlof, T., Gustafsson, J.A., Wright, A.P. 1997. Role of hydrophobic amino acids clusters in the transactivation activity of the human glucocorticoid receptor. Mol Cellular Biol 17, 934–945.

    CAS  Google Scholar 

  5. Betney, R., McEwan, I.J. 2003. Role of conserved hydrophobic amino acids in androgen receptors AF-1 function. J Mol Endocrinol 31, 427–439.

    Article  PubMed  CAS  Google Scholar 

  6. Bhasin, M., Garg, A., Raghava, G.P. 2005. PSLpred: Prediction of subcellular localization of bacterial proteins. Bioinformatics 21, 2522–2524.

    Article  PubMed  CAS  Google Scholar 

  7. Bradshaw, R.A. 1989. Protein translocation and turnover in eukaryotic cells. Trends Biochem Sci 14, 276–279.

    Article  PubMed  CAS  Google Scholar 

  8. Burley, S.K., Petsko, G.A. 1985. Aromatic-aromatic interaction: A mechanism of protein structure stabilization. Science 229, 23–28.

    Article  PubMed  CAS  Google Scholar 

  9. Cedano, J., Aloy, P., Perez-Pons, J.A., Querol, E. 1997. Relation between amino acid composition and cellular location of proteins. J Mol Biol 266, 594–600.

    Article  PubMed  CAS  Google Scholar 

  10. Creighton, T.E. 1993. Proteins: Structures and Molecular Properties, 2nd Edition, W.H. Freeman & Company, New York.

    Google Scholar 

  11. DeAngelis, P.L, Glabe, C.G. 1988. Role of basic amino acids in the interaction of binding with sulfated fucans. Biochemistry 27, 8189–8194.

    Article  PubMed  CAS  Google Scholar 

  12. DeLano, W.L. 2002. Unraveling hot spots in binding interfaces: Progress and challenges. Curr Opinion Structural Biol 12, 14–20.

    Article  CAS  Google Scholar 

  13. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D., Bairoch, A. 2005. Protein identification and analysis tools on the ExPASy server. In: Walker, J.M. (Ed.) The Proteomics Protocols Handbook, Humana Press, New Jersy, 571–607.

    Chapter  Google Scholar 

  14. Gill, S.C., von Hippel, P.H. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182, 319–326.

    Article  PubMed  CAS  Google Scholar 

  15. Gonda, D.K., Bachmair, A., Wunning, I., Tobias, J.W., Lane, W.S., Varshavsky, A.J. 1989. Universality and structure of the N-end rule. The J Biol Chem 264, 16700–16712.

    CAS  Google Scholar 

  16. Gregory, A.P., Dagmar, R. 2003. Protein motifs. In: Gregory, A.P., Dagmar, R., Waltham, M.A. (Eds.) Protein Structure and Function, 4th Edition, New Science Press, London, 89–101.

    Google Scholar 

  17. Ikai, A.J. 1980. Thermostability and aliphatic index of globular proteins. The J Biochem 88, 1895–1898.

    CAS  Google Scholar 

  18. Kyte, J., Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157, 105–132.

    Article  PubMed  CAS  Google Scholar 

  19. Lobry, J.R., Gautier, C. 1994. Hydrophobicity, expressivity and aromaticity are the major trends of amino acid usage in 999 Escherichia coli chromosome encoded genes. Nucleic Acids Res 22, 3174–3180.

    Article  PubMed  CAS  Google Scholar 

  20. Manavalan, P., Ponnusamy, P.K. 1978. Hydrophobic character of amino acid residues in globular proteins. Nature 275, 673–674.

    Article  PubMed  CAS  Google Scholar 

  21. Meierhenrich, U.J. 2008. Amino acids and the asymmetry of life. In: Advances in Astrobiology and Biogeophysics, Springer-Verlag, Berlin, Heidelberg, New York.

    Google Scholar 

  22. Nakashima, H., Nishikawa, K. 1994. Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies. J Mol Biol 238, 54–56.

    Article  PubMed  CAS  Google Scholar 

  23. Nozaki, T., Ali, V., Tokoro, M. 2005. Sulfur-containing amino acid metabolism in parasitic protozoa. Adv Parasitol 60, 1–99.

    Article  PubMed  Google Scholar 

  24. Ora, S.F., Baker, D. 2003. Conserved residue clustering and protein structure prediction. Proteins: Str Func Genet 52, 225–235.

    Article  Google Scholar 

  25. Ota, M., Shimizu, Y., Tonosaki, K., Ariyoshi, Y. 1998. Role of hydrophobic amino acids in gurmarin, a sweetness-suppressing polypeptide. Biopolymers 45, 231–238.

    Article  PubMed  CAS  Google Scholar 

  26. Qiu, X., Janson, C.A., Blackburn, M., Chhohan, I., Hibbs, M., Abdel-Meguid, S. 1999. Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases. Biochemistry 38, 12296–12304.

    Article  PubMed  CAS  Google Scholar 

  27. Rashid, M., Saha, S., Raghava, G.P. 2007. Support Vector Machine-based method for predicting subcellular localization of mycobacterial proteins using evolutionary information and motifs. BMC Bioinformatics 8, 337–345.

    Article  PubMed  Google Scholar 

  28. Rost, B., Casadio, R., Fariselli, P., Sander, C. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci 4, 521–533.

    Article  PubMed  CAS  Google Scholar 

  29. Sevier, C.S., Kaiser, C.A. 2002. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 3, 836–847.

    Article  PubMed  CAS  Google Scholar 

  30. Shortle, D. 1992. Mutational studies of protein structures and their stabilities. Quarterly Rev Biophysics 25, 205–250.

    Article  CAS  Google Scholar 

  31. Varshavsky, A. 1997. The N-end rule pathway of protein degradation. Genes Cells 2, 13–28.

    Article  PubMed  CAS  Google Scholar 

  32. Wang, J., Sung, W.K., Krishnan, A., Li, K.B. 2005. Protein subcellular localization prediction for Gramnegative bacteria using amino acid subalphabets and a combination of multiple support vector machines. BMC Bioinformatics 6, 174–183.

    Article  PubMed  Google Scholar 

  33. Zhang, H.Y. 2007. Exploring the evolution of standard amino-acid alphabet: When genomics meets thermodynamics. Biochem Biophy Res Comm 359, 403–405.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Senthilkumar Nachimuthu.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Senthilkumar, B., Sailo, S., Guruswami, G. et al. Prot-Prop: J-tool to predict the subcellular location of proteins based on physiochemical characterization. Interdiscip Sci Comput Life Sci 4, 296–301 (2012). https://doi.org/10.1007/s12539-012-0143-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12539-012-0143-8

Key words

Navigation