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10.1007/s12551-012-0087-6 http://scihub22266oqcxt.onion/10.1007/s12551-012-0087-6 C5418404!5418404!28510078     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 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 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2012 ; 4 (3): 189-203 Nephropedia Template TP {{tp|p=28510078|t=2012. Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data |pdf=|usr=}}{{28510078}} gab.com Text Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510078 #FOAvip The sophistication of the force fields, algorithms and hardware used for molecular dynamics (MD) simulations of proteins is continuously increasing. No matter how advanced the methodology, however, it is essential to evaluate the appropriateness of the structures sampled in a simulation by comparison with quantitative experimental data. Solution nuclear magnetic resonance (NMR) data are particularly useful for checking the quality of protein simulations, as they provide both structural and dynamic information on a variety of temporal and spatial scales. Here, various features and implications of using NMR data to validate and bias MD simulations are outlined, including an overview of the different types of NMR data that report directly on structural properties and of relevant simulation techniques. The focus throughout is on how to properly account for conformational averaging, particularly within the context of the assumptions inherent in the relationships that link NMR data to structural properties. Twit Text FOAVip Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510078 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28510078 #FOAvip English Wikipedia <ref>{{Cite pmid|28510078}}</ref> Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data #MMPMID28510078 Allison JR Biophys Rev 2012[Sep]; 4 (3): 189-203 PMID28510078show ga The sophistication of the force fields, algorithms and hardware used for molecular dynamics (MD) simulations of proteins is continuously increasing. No matter how advanced the methodology, however, it is essential to evaluate the appropriateness of the structures sampled in a simulation by comparison with quantitative experimental data. Solution nuclear magnetic resonance (NMR) data are particularly useful for checking the quality of protein simulations, as they provide both structural and dynamic information on a variety of temporal and spatial scales. Here, various features and implications of using NMR data to validate and bias MD simulations are outlined, including an overview of the different types of NMR data that report directly on structural properties and of relevant simulation techniques. The focus throughout is on how to properly account for conformational averaging, particularly within the context of the assumptions inherent in the relationships that link NMR data to structural properties. äAssessing and refining molecular dynamics simulations of proteins with(epmc).pdf DeepDyve Pubget Overpricing