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10.1038/s41598-017-08664-w http://scihub22266oqcxt.onion/10.1038/s41598-017-08664-w C5567296!5567296!28831058     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28831058|t=2017. A method for rapid high-throughput biophysical analysis of proteins |pdf=|usr=}}{{28831058}} gab.com Text A method for rapid high-throughput biophysical analysis of proteins JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28831058 #FOAvip Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently. Twit Text FOAVip A method for rapid high-throughput biophysical analysis of proteins ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28831058 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28831058 #FOAvip English Wikipedia <ref>{{Cite pmid|28831058}}</ref> A method for rapid high-throughput biophysical analysis of proteins #MMPMID28831058 Perez-Riba A; Itzhaki LS Sci Rep 2017[]; 7 (ä): ä PMID28831058show ga Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently. äA method for rapid high-throughput biophysical analysis of proteins (epmc).pdf DeepDyve Pubget Overpricing