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10.1007/s12551-017-0314-2 http://scihub22266oqcxt.onion/10.1007/s12551-017-0314-2 C5662050!5662050!28825203     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2017 ; 9 (5): 517-27 Nephropedia Template TP {{tp|p=28825203|t=2017. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy |pdf=|usr=}}{{28825203}} gab.com Text Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28825203 #FOAvip Circular dichroism (CD) spectroscopy is a fast, powerful, well-established, and widely used analytical technique in the biophysical and structural biology community to study protein secondary structure and to track changes in protein conformation in different environments. The use of the intense light of a synchrotron beam as the light source for collecting CD measurements has emerged as an enhanced method, known as synchrotron radiation circular dichroism (SRCD) spectroscopy, that has several advantages over the conventional CD method, including a significant spectral range extension for data collection, deeper access to the lower limit (cut-off) of conventional CD spectroscopy, an improved signal-to-noise ratio to increase accuracy in the measurements, and the possibility to collect measurements in highly absorbing solutions. In this review, we discuss different applications of the SRCD technique by researchers from Latin America. In this context, we specifically look at the use of this method for examining the secondary structure and conformational behavior of proteins belonging to the four main classes of the hierarchical protein domain classification CATH (Class, Architecture, Topology, Homology) database, focusing on the advantages and improvements associated with SRCD spectroscopy in terms of characterizing proteins composed of different structural elements. Twit Text FOAVip Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28825203 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28825203 #FOAvip English Wikipedia <ref>{{Cite pmid|28825203}}</ref> Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy #MMPMID28825203 Kumagai PS; Araujo APU; Lopes JLS Biophys Rev 2017[Oct]; 9 (5): 517-27 PMID28825203show ga Circular dichroism (CD) spectroscopy is a fast, powerful, well-established, and widely used analytical technique in the biophysical and structural biology community to study protein secondary structure and to track changes in protein conformation in different environments. The use of the intense light of a synchrotron beam as the light source for collecting CD measurements has emerged as an enhanced method, known as synchrotron radiation circular dichroism (SRCD) spectroscopy, that has several advantages over the conventional CD method, including a significant spectral range extension for data collection, deeper access to the lower limit (cut-off) of conventional CD spectroscopy, an improved signal-to-noise ratio to increase accuracy in the measurements, and the possibility to collect measurements in highly absorbing solutions. In this review, we discuss different applications of the SRCD technique by researchers from Latin America. In this context, we specifically look at the use of this method for examining the secondary structure and conformational behavior of proteins belonging to the four main classes of the hierarchical protein domain classification CATH (Class, Architecture, Topology, Homology) database, focusing on the advantages and improvements associated with SRCD spectroscopy in terms of characterizing proteins composed of different structural elements. äGoing deep into protein secondary structure with synchrotron radiation(epmc).pdf DeepDyve Pubget Overpricing