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10.1016/j.jim.2016.02.016 http://scihub22266oqcxt.onion/10.1016/j.jim.2016.02.016 C4837003!4837003!26906089     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Immunol+Methods 2016 ; 432 (ä): 95-101 Nephropedia Template TP {{tp|p=26906089|t=2016. Differential scanning fluorimetry based assessments of the thermal and kinetic stability of peptide-MHC complexes |pdf=|usr=}}{{26906089}} gab.com Text Differential scanning fluorimetry based assessments of the thermal and kinetic stability of peptide-MHC complexes JO: J Immunol Methods http://www.kidney.de/pget.php?&tw=1&pmid=26906089 #FOAvip Measurements of thermal stability by circular dichroism (CD) spectroscopy have been widely used to assess the binding of peptides to MHC proteins, particularly within the structural immunology community. Although thermal stability assays offer advantages over other approaches such as IC50 measurements, CD-based stability measurements are hindered by large sample requirements and low throughput. Here we demonstrate that an alternative approach based on differential scanning fluorimetry (DSF) yields results comparable to those based on CD for both class I and class II complexes. As they require much less sample, DSF-based measurements reduce demands on protein production strategies and are amenable for high throughput studies. DSF can thus not only replace CD as a means to assess peptide/MHC thermal stability, but can complement other peptide-MHC binding assays used in screening, epitope discovery, and vaccine design. Due to the physical process probed, DSF can also uncover complexities not observed with other techniques. Lastly, we show that DSF can also be used to assess peptide/MHC kinetic stability, allowing a single experimental setup to probe both binding equilibria and kinetics. Twit Text FOAVip Differential scanning fluorimetry based assessments of the thermal and kinetic stability of peptide-MHC complexes ????J Immunol Methods http://www.kidney.de/pget.php?&tw=1&pmid=26906089 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26906089 #FOAvip English Wikipedia <ref>{{Cite pmid|26906089}}</ref> Differential scanning fluorimetry based assessments of the thermal and kinetic stability of peptide-MHC complexes #MMPMID26906089 Hellman LM; Yin L; Wang Y; Blevins SJ; Riley TP; Belden OS; Spear TT; Nishimura MI; Stern LJ; Baker BM J Immunol Methods 2016[May]; 432 (ä): 95-101 PMID26906089show ga Measurements of thermal stability by circular dichroism (CD) spectroscopy have been widely used to assess the binding of peptides to MHC proteins, particularly within the structural immunology community. Although thermal stability assays offer advantages over other approaches such as IC50 measurements, CD-based stability measurements are hindered by large sample requirements and low throughput. Here we demonstrate that an alternative approach based on differential scanning fluorimetry (DSF) yields results comparable to those based on CD for both class I and class II complexes. As they require much less sample, DSF-based measurements reduce demands on protein production strategies and are amenable for high throughput studies. DSF can thus not only replace CD as a means to assess peptide/MHC thermal stability, but can complement other peptide-MHC binding assays used in screening, epitope discovery, and vaccine design. Due to the physical process probed, DSF can also uncover complexities not observed with other techniques. Lastly, we show that DSF can also be used to assess peptide/MHC kinetic stability, allowing a single experimental setup to probe both binding equilibria and kinetics. äDifferential scanning fluorimetry based assessments of the thermal and(epmc).pdf DeepDyve Pubget Overpricing