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10.1073/pnas.1524864113 http://scihub22266oqcxt.onion/10.1073/pnas.1524864113 C4812744!4812744 !26957601     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26957601 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       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 We use (1)H NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme ? reversible unfolded (intermediate) ? irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range 295 < T < 365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability. 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 PMID26957601 show ga We use (1)H NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme ? reversible unfolded (intermediate) ? irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range 295 < T < 365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability. |*Protein Folding [MESH] |Muramidase/chemistry [MESH] |Protein Denaturation [MESH] |Proton Magnetic Resonance Spectroscopy [MESH]Energy landscape in protein folding and unfolding (epmc).pdf DeepDyve Pubget Overpricing