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Long range correlation of hydrophilicity and flexibility along the calcium binding protein chains

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  • Craciun, Dana
  • Isvoran, Adriana
  • Avram, N.M.

Abstract

Long range correlation concerning hydrophilicity and flexibility along a number of 80 calcium binding protein sequences is confirmed by using spectral analysis and detrended fluctuations analysis methods, as well as by Hurst exponent calculations. There are no significant differences between the correlation properties concerning these properties for the two structural subfamilies, extended and compact, of the calcium binding proteins and they are also similar with the correlation properties revealed by other investigated proteins. This result sustains the hypothesis that the long range correlation of hydrophilicity and flexibility along the chain is a common feature of proteins.

Suggested Citation

  • Craciun, Dana & Isvoran, Adriana & Avram, N.M., 2009. "Long range correlation of hydrophilicity and flexibility along the calcium binding protein chains," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 388(21), pages 4609-4618.
    • Handle: RePEc:eee:phsmap:v:388:y:2009:i:21:p:4609-4618
    DOI: 10.1016/j.physa.2009.07.042
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    References listed on IDEAS

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    1. Ciorsac, Alecu & Craciun, Dana & Ostafe, Vasile & Isvoran, Adriana, 2011. "Nonlinear correlations in the hydrophobicity and average flexibility along the glycolytic enzymes sequences," Chaos, Solitons & Fractals, Elsevier, vol. 44(4), pages 191-197.

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