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10.1002/pro.2865 http://scihub22266oqcxt.onion/10.1002/pro.2865 C4815411!4815411!26683260     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Sci 2016 ; 25 (3): 734-47 Nephropedia Template TP {{tp|p=26683260|t=2016. Dimensions, energetics, and denaturant effects of the protein unstructured state |pdf=|usr=}}{{26683260}} gab.com Text Dimensions, energetics, and denaturant effects of the protein unstructured state JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=26683260 #FOAvip Determining the energetics of the unfolded state of a protein is essential for understanding the folding mechanics of ordered proteins and the structure?function relation of intrinsically disordered proteins. Here, we adopt a coil?globule transition theory to develop a general scheme to extract interaction and free energy information from single?molecule fluorescence resonance energy transfer spectroscopy. By combining protein stability data, we have determined the free energy difference between the native state and the maximally collapsed denatured state in a number of systems, providing insight on the specific/nonspecific interactions in protein folding. Both the transfer and binding models of the denaturant effects are demonstrated to account for the revealed linear dependence of inter?residue interactions on the denaturant concentration, and are thus compatible under the coil?globule transition theory to further determine the dimension and free energy of the conformational ensemble of the unfolded state. The scaling behaviors and the effective ??state are also discussed. Twit Text FOAVip Dimensions, energetics, and denaturant effects of the protein unstructured state ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=26683260 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26683260 #FOAvip English Wikipedia <ref>{{Cite pmid|26683260}}</ref> Dimensions, energetics, and denaturant effects of the protein unstructured state #MMPMID26683260 Li M; Liu Z Protein Sci 2016[Mar]; 25 (3): 734-47 PMID26683260show ga Determining the energetics of the unfolded state of a protein is essential for understanding the folding mechanics of ordered proteins and the structure?function relation of intrinsically disordered proteins. Here, we adopt a coil?globule transition theory to develop a general scheme to extract interaction and free energy information from single?molecule fluorescence resonance energy transfer spectroscopy. By combining protein stability data, we have determined the free energy difference between the native state and the maximally collapsed denatured state in a number of systems, providing insight on the specific/nonspecific interactions in protein folding. Both the transfer and binding models of the denaturant effects are demonstrated to account for the revealed linear dependence of inter?residue interactions on the denaturant concentration, and are thus compatible under the coil?globule transition theory to further determine the dimension and free energy of the conformational ensemble of the unfolded state. The scaling behaviors and the effective ??state are also discussed. äDimensions, energetics, and denaturant effects of the protein unstruct(epmc).pdf DeepDyve Pubget Overpricing