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10.1007/s12551-017-0334-y http://scihub22266oqcxt.onion/10.1007/s12551-017-0334-y C5899696!5899696!29178080     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29178080.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+Rev 2018 ; 10 (2): 145-52 Nephropedia Template TP {{tp|p=29178080|t=2018. Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis |pdf=|usr=}}{{29178080}} gab.com Text Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=29178080 #FOAvip Structural characterization of fully unfolded proteins is essential for understanding not only protein-folding mechanisms, but also the structures of intrinsically disordered proteins. Because an unfolded protein can assume all possible conformations, statistical descriptions of its structure are most appropriate. For this purpose, we applied Förster resonance energy transfer (FRET) analysis to fully unfolded staphylococcal nuclease. Artificial amino acids labeled with a FRET donor or acceptor were introduced by an amber codon and a four-base codon respectively. Eight double-labeled proteins were prepared, purified, and subjected to FRET analysis in 6 M urea. The observed behavior could be explained by a power law, R?=??N0.44, where R, and N are the distance and the number of residues between donor and acceptor, and ? is a coefficient. The index was smaller than the value expected for an excluded-volume random coil, 0.588, indicating that the fully unfolded proteins were more compact than polypeptides in good solvent. The FRET efficiency in the native state did not necessarily correlate to the distance obtained from crystal structure, suggesting that other factors such as the orientation factor made a substantial contribution to FRET. Twit Text FOAVip Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=29178080 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29178080 #FOAvip English Wikipedia <ref>{{Cite pmid|29178080}}</ref> Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis #MMPMID29178080 Yamaguchi M; Ohta E; Muto T; Watanabe T; Hohsaka T; Yamazaki Y; Kamikubo H; Kataoka M Biophys Rev 2018[Apr]; 10 (2): 145-52 PMID29178080show ga Structural characterization of fully unfolded proteins is essential for understanding not only protein-folding mechanisms, but also the structures of intrinsically disordered proteins. Because an unfolded protein can assume all possible conformations, statistical descriptions of its structure are most appropriate. For this purpose, we applied Förster resonance energy transfer (FRET) analysis to fully unfolded staphylococcal nuclease. Artificial amino acids labeled with a FRET donor or acceptor were introduced by an amber codon and a four-base codon respectively. Eight double-labeled proteins were prepared, purified, and subjected to FRET analysis in 6 M urea. The observed behavior could be explained by a power law, R?=??N0.44, where R, and N are the distance and the number of residues between donor and acceptor, and ? is a coefficient. The index was smaller than the value expected for an excluded-volume random coil, 0.588, indicating that the fully unfolded proteins were more compact than polypeptides in good solvent. The FRET efficiency in the native state did not necessarily correlate to the distance obtained from crystal structure, suggesting that other factors such as the orientation factor made a substantial contribution to FRET. äStatistical description of the denatured structure of a single protein(epmc).pdf DeepDyve Pubget Overpricing