Long Range Correlation of Hydrophilicity and Flexibility Along the Hemoglobin Chain

摘要

Within this study, we reveal the long range correlation concerning hydrophilicity and flexibility along sequences of hemoglobins belonging to different organisms and we compare them with the long range correlations properties obtained for other protein families. For all hemoglobins considered, we investigate two discrete spatial series: the hydrophilicity and flexibility respectively. We apply the nonlinear analysis methods to analyze the two spatial series by calculating the spectral coefficient β, the scaling exponent a and Hurst exponent H. The obtained values for the mentioned coefficients suggest long range correlation within the analyzed sequences of hemoglobins in good agreement with those obtained for the calcium binding proteins and hydrolases.