Nonlinear correlations in the hydrophobicity and average flexibility along the glycolytic enzymes sequences |
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| Authors: | Alecu Ciorsac Dana Craciun Vasile Ostafe Adriana Isvoran |
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| Affiliation: | 1. Politehnica University of Timisoara, Department of Physical Education and Sport, 2 P-ta Victoriei, 300006, Timisoara, Romania;2. Teacher Training Department, West University of Timisoara, 4 Boulevard V. Pirvan, Timisoara, 300223, Romania;3. Department of Chemistry, West University of Timisoara, 16 Pestallozi, 300115, Timisoara, Romania;4. Laboratory of Advanced Researches in Environmental Protection, Nicholas Georgescu-Roegen Interdisciplinary Research and Formation Platform, 4 Oituz, Timisoara, 300086, Romania;1. Department of Clinical Pharmacology, St. Olav University Hospital, Trondheim, Norway;2. Department of Laboratory Medicine, Children’s and Women’s Health, Norwegian University of Science and Technology, Trondheim, Norway;1. School of Traffic and Transportation, Beijing Jiaotong University, Beijing 100044, China;2. Department of Civil and Environmental Engineering, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China;3. State Key Laboratory of Rail Traffic Control and Safety, Beijing Jiaotong University, Beijing 100044, China;4. School of Economics and Management, China University of Geosciences, Wuhan 430074, China |
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| Abstract: | Nonlinear methods widely used for time series analysis were applied to glycolytic enzyme sequences to derive information concerning the correlation of hydrophobicity and average flexibility along their chains. The 20 sequences of different types of the 10 human glycolytic enzymes were considered as spatial series and were analyzed by spectral analysis, detrended fluctuations analysis and Hurst coefficient calculation. The results agreed that there are both short range and long range correlations of hydrophobicity and average flexibility within investigated sequences, the short range correlations being stronger and indicating that local interactions are the most important for the protein folding. This correlation is also reflected by the fractal nature of the structures of investigated proteins. |
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