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10.1002/prot.21160 http://scihub22266oqcxt.onion/10.1002/prot.21160 17083088!7167853!17083088     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proteins 2007 ; 66 (2): 467-79 Nephropedia Template TP {{tp|p=17083088|t=2007. Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme |pdf=|usr=}}{{17083088}} gab.com Text Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme JO: Proteins http://www.kidney.de/pget.php?&tw=1&pmid=17083088 #FOAvip The phenomenon that SARS coronavirus main protease (SARS M(pro)) dimer is the main functional form has been confirmed by experiment. However, because of the absence of structural information of the monomer, the reasons for this remain unknown. To investigate it, two molecular dynamics (MD) simulations in water for dimer and monomer models have been carried out, using the crystal structure of protomer A of the dimer as the starting structure for the monomer. During the MD simulation of dimer, three interest phenomena of protomer A have been observed: (i) the distance between NE2 of His41 and SG of Cys145 averages 3.72 A, which agrees well with the experimental observations made by X-ray crystallography; (ii) His163 and Glu166 form the "tooth" conformational properties, resulting in the specificity for glutamine at substrate P1 site; and (iii) the substrate-binding pocket formed by loop 140-146 and loop 184-197 is large enough to accommodate the substrate analog. However, during the MD simulation of the monomer complex, the three structural characteristics are all absent, which results directly in the inactivation of the monomer. Throughout the MD simulation of the dimer, the N-terminus of protomer B forms stable hydrogen bonds with Phe140 and Glu166, through which His163, Glu166, and loop 140-146 are kept active form. Furthermore, a water-bridge has been found between the N-terminus of protomer B and Gly170, which stabilizes His172 and avoids it moving toward Tyr161 to disrupt the H-bond between Tyr161 and His163, stabilizing the conformation of His163. The interactions between the N-terminus and another monomer maintain the activity of dimer. Twit Text FOAVip Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme ????Proteins http://www.kidney.de/pget.php?&tw=1&pmid=17083088 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17083088 #FOAvip English Wikipedia <ref>{{Cite pmid|17083088}}</ref> Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme #MMPMID17083088 Zheng K; Ma G; Zhou J; Zen M; Zhao W; Jiang Y; Yu Q; Feng J Proteins 2007[Feb]; 66 (2): 467-79 PMID17083088show ga The phenomenon that SARS coronavirus main protease (SARS M(pro)) dimer is the main functional form has been confirmed by experiment. However, because of the absence of structural information of the monomer, the reasons for this remain unknown. To investigate it, two molecular dynamics (MD) simulations in water for dimer and monomer models have been carried out, using the crystal structure of protomer A of the dimer as the starting structure for the monomer. During the MD simulation of dimer, three interest phenomena of protomer A have been observed: (i) the distance between NE2 of His41 and SG of Cys145 averages 3.72 A, which agrees well with the experimental observations made by X-ray crystallography; (ii) His163 and Glu166 form the "tooth" conformational properties, resulting in the specificity for glutamine at substrate P1 site; and (iii) the substrate-binding pocket formed by loop 140-146 and loop 184-197 is large enough to accommodate the substrate analog. However, during the MD simulation of the monomer complex, the three structural characteristics are all absent, which results directly in the inactivation of the monomer. Throughout the MD simulation of the dimer, the N-terminus of protomer B forms stable hydrogen bonds with Phe140 and Glu166, through which His163, Glu166, and loop 140-146 are kept active form. Furthermore, a water-bridge has been found between the N-terminus of protomer B and Gly170, which stabilizes His172 and avoids it moving toward Tyr161 to disrupt the H-bond between Tyr161 and His163, stabilizing the conformation of His163. The interactions between the N-terminus and another monomer maintain the activity of dimer. |*Computer Simulation[MESH] |*Models, Chemical[MESH] |Catalytic Domain[MESH] |Coronavirus 3C Proteases[MESH] |Cysteine Endopeptidases/chemistry/*metabolism[MESH] |Dimerization[MESH] |Hydrogen Bonding[MESH] |Hydrolysis[MESH] |Models, Molecular[MESH] |Protease Inhibitors/pharmacology[MESH] |Protein Conformation[MESH] |Protein Interaction Mapping[MESH] |Severe acute respiratory syndrome-related coronavirus/*enzymology[MESH] |Structure-Activity Relationship[MESH] |Substrate Specificity[MESH] |Viral Proteins/chemistry/*metabolism[MESH]Insight into the activity of SARS main protease: Molecular dynamics st(epmc).pdf DeepDyve Pubget Overpricing