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10.1073/pnas.1524864113 http://scihub22266oqcxt.onion/10.1073/pnas.1524864113 C4812744!4812744!26957601     free     free     free       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (12): 3159-63 Nephropedia Template TP {{tp|p=26957601|t=2016. Energy landscape in protein folding and unfolding |pdf=|usr=}}{{26957601}} gab.com Text Energy landscape in protein folding and unfolding JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26957601 #FOAvip Protein folding represents an open question in science, and the free-energy landscape framework is one way to describe it. In particular, the role played by water in the processes is of special interest. To clarify these issues we study, during folding?unfolding, the temperature evolution of the magnetization for hydrophilic and hydrophobic groups of hydrated lysozyme using NMR spectroscopy. Our findings confirm the validity of the theoretical scenario of a process dominated by different energetic routes, also explaining the water role in the protein configuration stability. We also highlight that the protein native state limit is represented by the water singular temperature that characterizes its compressibility and expansivity and is the origin of the thermodynamical anomalies of its liquid state. Twit Text FOAVip Energy landscape in protein folding and unfolding ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26957601 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26957601 #FOAvip English Wikipedia <ref>{{Cite pmid|26957601}}</ref> Energy landscape in protein folding and unfolding #MMPMID26957601 Mallamace F; Corsaro C; Mallamace D; Vasi S; Vasi C; Baglioni P; Buldyrev SV; Chen SH; Stanley HE Proc Natl Acad Sci U S A 2016[Mar]; 113 (12): 3159-63 PMID26957601show ga Protein folding represents an open question in science, and the free-energy landscape framework is one way to describe it. In particular, the role played by water in the processes is of special interest. To clarify these issues we study, during folding?unfolding, the temperature evolution of the magnetization for hydrophilic and hydrophobic groups of hydrated lysozyme using NMR spectroscopy. Our findings confirm the validity of the theoretical scenario of a process dominated by different energetic routes, also explaining the water role in the protein configuration stability. We also highlight that the protein native state limit is represented by the water singular temperature that characterizes its compressibility and expansivity and is the origin of the thermodynamical anomalies of its liquid state. äEnergy landscape in protein folding and unfolding (epmc).pdf DeepDyve Pubget Overpricing