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10.3390/v10060309 http://scihub22266oqcxt.onion/10.3390/v10060309 C6024848!6024848!29882827     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 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 Deprecated: Implicit conversion from float 267.2 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 Deprecated: Implicit conversion from float 267.2 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 Deprecated: Implicit conversion from float 267.2 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 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Viruses 2018 ; 10 (6): ä Nephropedia Template TP {{tp|p=29882827|t=2018. Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal ?-Helix with the Proposed Role in Activity against Live Bacterial Cells |pdf=|usr=}}{{29882827}} gab.com Text Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal -Helix with the Proposed Role in Activity against Live Bacterial Cells JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=29882827 #FOAvip Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of Acinetobacter baumannii AB 5075 genome. Recombinant protein expressed in E. coli exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1.5?2 log colony forming units (CFU)/mL. However the protein becomes rapidly inactivated and enables the bacteria to restore the population. AcLys structure determined by X-ray crystallography reveals a predominantly ??helical fold similar to bacteriophage P22 lysozyme. The ?-terminal part of AcLys polypeptide chains forms an ??helix enriched by Lys and Arg residues exposed outside of the protein globule. Presumably this type of structure of the C-terminal ??helix has evolved evolutionally enabling the endolysin to pass the inner membrane during the host lysis or, potentially, to penetrate the outer membrane of the Gram-negative bacteria. Twit Text FOAVip Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal -Helix with the Proposed Role in Activity against Live Bacterial Cells ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=29882827 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29882827 #FOAvip English Wikipedia <ref>{{Cite pmid|29882827}}</ref> Structure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a C-Terminal ?-Helix with the Proposed Role in Activity against Live Bacterial Cells #MMPMID29882827 Sykilinda NN; Nikolaeva AY; Shneider MM; Mishkin DV; Patutin AA; Popov VO; Boyko KM; Klyachko NL; Miroshnikov KA Viruses 2018[Jun]; 10 (6): ä PMID29882827show ga Proteins that include enzymatic domain degrading the bacterial cell wall and a domain providing transport through the bacterial outer membrane are considered as prospective compounds to combat pathogenic Gram-negative bacteria. This paper presents an isolation and study of an enzyme of this class naturally encoded in the prophage region of Acinetobacter baumannii AB 5075 genome. Recombinant protein expressed in E. coli exhibits an antimicrobial activity with respect to live cultures of Gram-negative bacteria reducing the population of viable bacteria by 1.5?2 log colony forming units (CFU)/mL. However the protein becomes rapidly inactivated and enables the bacteria to restore the population. AcLys structure determined by X-ray crystallography reveals a predominantly ??helical fold similar to bacteriophage P22 lysozyme. The ?-terminal part of AcLys polypeptide chains forms an ??helix enriched by Lys and Arg residues exposed outside of the protein globule. Presumably this type of structure of the C-terminal ??helix has evolved evolutionally enabling the endolysin to pass the inner membrane during the host lysis or, potentially, to penetrate the outer membrane of the Gram-negative bacteria. äStructure of an Acinetobacter Broad-Range Prophage Endolysin Reveals a(epmc).pdf DeepDyve Pubget Overpricing