caa a22 4500 605513341 CHVBK 20210128100659.0 cr unu---uuuuu 210128e20150501xx s 000 0 eng 10.1007/s00894-015-2659-4 doi (NATIONALLICENCE)springer-10.1007/s00894-015-2659-4 A theoretical study of the unfolding pathway of reduced Human serum albumin [Elektronische Daten] [Guillaume Paris, Christophe Ramseyer, Mironel Enescu] The unfolding of the reduced human serum albumin (HSA) was simulated by generating four molecular dynamics (MD) trajectories of 160ns each at 350, 375, 400, and 425K, respectively. A principal components analysis (PCA) was performed on the four trajectories. Based on this analysis, 17 representative protein conformers were identified and subsequently used to construct a sequence of partially unfolded structures. They were ordered according to their decreasing α-helix fractions. The structural evolution in this unfolding sequence was found to be continuous at global but also at local level supporting the hypothesis that the protein unfolding pathway is not significantly dependent on the simulation temperature. As a result, the α-helix fraction of the protein appears to be a good reaction coordinate for the unfolding process, as it was previously suggested by experiments. Based on this observation, two conformers in the unfolding sequence were predicted to be close to the equilibrium structure of reduced HSA thus providing a first theoretical model for this protein form. Springer-Verlag Berlin Heidelberg, 2015 Human serum albumin nationallicence Molecular dynamics nationallicence Principal components analysis nationallicence Unfolding nationallicence Paris Guillaume Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut Ramseyer Christophe Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut Enescu Mironel Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut Journal of Molecular Modeling Springer Berlin Heidelberg 21/5(2015-05-01), 1-8 1610-2940 21:5<1 2015 21 894 https://doi.org/10.1007/s00894-015-2659-4 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00894-015-2659-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Paris Guillaume Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut NATIONALLICENCE 700 1- Ramseyer Christophe Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut NATIONALLICENCE 700 1- Enescu Mironel Laboratoire Chrono Environnement UMR CNRS 6249, Faculté des Sciences et Techniques, La Bouloie, Université de Franche-Comté, 25030, Besançon cedex, France aut NATIONALLICENCE 773 0- Journal of Molecular Modeling Springer Berlin Heidelberg 21/5(2015-05-01), 1-8 1610-2940 21:5<1 2015 21 894