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10.1073/pnas.1522946113 http://scihub22266oqcxt.onion/10.1073/pnas.1522946113 C4780631!4780631!26884173     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       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (9): 2490-5 Nephropedia Template TP {{tp|p=26884173|t=2016. CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks |pdf=|usr=}}{{26884173}} gab.com Text CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26884173 #FOAvip Bacteria colonizing the oropharynx must adhere despite mechanical challenges from coughing, sneezing, and chewing; however, little is known about how Gram-positive organisms achieve this feat. We studied the pilus adhesive proteins from two Gram-positive organisms and report a conserved mechanism for dissipating the energy of a mechanical perturbation. The two proteins are stable up to forces of 525 pN and 690 pN, respectively, making these proteins the most mechanically stable proteins known. After a perturbation, the proteins refold rapidly at low force, resulting in a large hysteresis with most of the unfolding energy lost as heat. The work presents an initial model whereby transient unfolding at forces of 500?700 pN dissipates mechanical energy and protects covalent bonds from cleavage. Twit Text FOAVip CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26884173 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26884173 #FOAvip English Wikipedia <ref>{{Cite pmid|26884173}}</ref> CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks #MMPMID26884173 Echelman DJ; Alegre-Cebollada J; Badilla CL; Chang C; Ton-That H; Fernández JM Proc Natl Acad Sci U S A 2016[Mar]; 113 (9): 2490-5 PMID26884173show ga Bacteria colonizing the oropharynx must adhere despite mechanical challenges from coughing, sneezing, and chewing; however, little is known about how Gram-positive organisms achieve this feat. We studied the pilus adhesive proteins from two Gram-positive organisms and report a conserved mechanism for dissipating the energy of a mechanical perturbation. The two proteins are stable up to forces of 525 pN and 690 pN, respectively, making these proteins the most mechanically stable proteins known. After a perturbation, the proteins refold rapidly at low force, resulting in a large hysteresis with most of the unfolding energy lost as heat. The work presents an initial model whereby transient unfolding at forces of 500?700 pN dissipates mechanical energy and protects covalent bonds from cleavage. äCnaA domains in bacterial pili are efficient dissipaters of large mech(epmc).pdf DeepDyve Pubget Overpricing