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10.1103/PhysRevLett.127.098103 http://scihub22266oqcxt.onion/10.1103/PhysRevLett.127.098103 34506164!ä!34506164 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34506164&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 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\34506164.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Phys+Rev+Lett 2021 ; 127 (9): 098103 Nephropedia Template TP {{tp|p=34506164|t=2021. Dynamics-Evolution Correspondence in Protein Structures |pdf=|usr=}}{{34506164}} gab.com Text Dynamics-Evolution Correspondence in Protein Structures JO: Phys Rev Lett http://www.kidney.de/pget.php?&tw=1&pmid=34506164 #FOAvip The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the origin of such a correspondence is elucidated. It is essential that the noise- and mutation-induced deformations of the proteins are restricted on a common low-dimensional subspace, as confirmed from the data. These results suggest an evolutionary mechanism of the proteins gaining both dynamical flexibility and evolutionary structural variability. Twit Text FOAVip Dynamics-Evolution Correspondence in Protein Structures ????Phys Rev Lett http://www.kidney.de/pget.php?&tw=1&pmid=34506164 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34506164 #FOAvip English Wikipedia <ref>{{Cite pmid|34506164}}</ref> Dynamics-Evolution Correspondence in Protein Structures #MMPMID34506164 Tang QY; Kaneko K Phys Rev Lett 2021[Aug]; 127 (9): 098103 PMID34506164show ga The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the origin of such a correspondence is elucidated. It is essential that the noise- and mutation-induced deformations of the proteins are restricted on a common low-dimensional subspace, as confirmed from the data. These results suggest an evolutionary mechanism of the proteins gaining both dynamical flexibility and evolutionary structural variability. |*Models, Chemical[MESH] |Coronavirus 3C Proteases/chemistry/genetics[MESH] |Evolution, Molecular[MESH] |Genetic Association Studies[MESH] |Mutation[MESH] |Protein Conformation[MESH]Dynamics-Evolution Correspondence in Protein Structures (epmc).pdf DeepDyve Pubget Overpricing