@article{bibcite_15378,
  author = {Piotr Weber and Piotr Be{\l}dowski and Krzysztof Domino and Damian Ledzi{\'n}ski and Adam Gadomski},
  title = {Changes of Conformation in Albumin Protein with Temperature},
  abstract = {This work presents the analysis of the conformation of albumin in the temperature range of 300K {\textendash} 312K , i.e., in the physiological range. Using molecular dynamics simulations, we calculate values of the backbone and dihedral angles for this molecule. We analyze the global dynamic properties of albumin treated as a chain. In this range of temperature, we study parameters of the molecule and the conformational entropy derived from two angles that reflect global dynamics in the conformational space. A thorough rationalization, based on the scaling theory, for the subdiffusion Flory{\textendash}De Gennes type exponent of 0.4 unfolds in conjunction with picking up the most appreciable fluctuations of the corresponding statistical-test parameter. These fluctuations coincide adequately with entropy fluctuations, namely the oscillations out of thermodynamic equilibrium. Using Fisher{\textquoteright}s test, we investigate the conformational entropy over time and suggest its oscillatory properties in the corresponding time domain. Using the Kruscal{\textendash}Wallis test, we also analyze differences between the root mean square displacement of a molecule at various temperatures. Here we show that its values in the range of 306K {\textendash} 309K are different than in another temperature. Using the Kullback{\textendash}Leibler theory, we investigate differences between the distribution of the root mean square displacement for each temperature and time window.},
  year = {2020},
  journal = {Entropy},
  volume = {405},
  month = {03/2020},
  issn = {1099-4300},
  url = {https://www.mdpi.com/1099-4300/22/4/405},
  doi = {https://doi.org/10.3390/e22040405},
  language = {eng},
}