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10.1021/acs.biochem.5b00845 http://scihub22266oqcxt.onion/10.1021/acs.biochem.5b00845 C4820058!4820058 !26332921     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26332921 &cmd=llinks): Failed to open stream: HTTP request failed! 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Restricting the ? Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis |pdf=|usr=}}{{26332921 }} gab.com Text Restricting the Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26332921 #FOAvip Protein motion is intimately linked to enzymatic catalysis, yet the stereoelectronic changes that accompany different conformational states of a substrate are poorly defined. Here we investigate the relationship between conformation and stereoelectronic effects of a scissile amide bond. Structural studies have revealed that the C-terminal glycine of ubiquitin and ubiquitin-like proteins adopts a syn (? ? 0°) or gauche (? ? ±60°) conformation upon interacting with deubiquitinases/ubiquitin-like proteases. We used hybrid density functional theory and natural bond orbital analysis to understand how the stereoelectronic effects of the scissile bond change as a function of ? and ? torsion angles. This led to the discovery that when ? is between 30° and -30° the scissile bond becomes geometrically and electronically deformed. Geometric distortion occurs through pyramidalization of the carbonyl carbon and amide nitrogen. Electronic distortion is manifested by a decrease in the strength of the donor-acceptor interaction between the amide nitrogen and antibonding orbital (?*) of the carbonyl. Concomitant with the reduction in nN ? ?* delocalization energy, the sp(2) hybrid orbital of the carbonyl carbon becomes richer in p-character, suggesting the syn configuration causes the carbonyl carbon hybrid orbitals to adopt a geometry reminiscent of a tetrahedral-like intermediate. Our work reveals important insights into the role of substrate conformation in activating the reactive carbonyl of a scissile bond. These findings have implications for designing potent active site inhibitors based on the concept of transition state analogues. Twit Text FOAVip Restricting the Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26332921 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26332921 #FOAvip English Wikipedia <ref>{{Cite pmid|26332921 }}</ref> Restricting the ? Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis #MMPMID26332921 Strieter ER ; Andrew TL Biochemistry 2015[Sep]; 54 (37 ): 5748-56 PMID26332921 show ga Protein motion is intimately linked to enzymatic catalysis, yet the stereoelectronic changes that accompany different conformational states of a substrate are poorly defined. Here we investigate the relationship between conformation and stereoelectronic effects of a scissile amide bond. Structural studies have revealed that the C-terminal glycine of ubiquitin and ubiquitin-like proteins adopts a syn (? ? 0°) or gauche (? ? ±60°) conformation upon interacting with deubiquitinases/ubiquitin-like proteases. We used hybrid density functional theory and natural bond orbital analysis to understand how the stereoelectronic effects of the scissile bond change as a function of ? and ? torsion angles. This led to the discovery that when ? is between 30° and -30° the scissile bond becomes geometrically and electronically deformed. Geometric distortion occurs through pyramidalization of the carbonyl carbon and amide nitrogen. Electronic distortion is manifested by a decrease in the strength of the donor-acceptor interaction between the amide nitrogen and antibonding orbital (?*) of the carbonyl. Concomitant with the reduction in nN ? ?* delocalization energy, the sp(2) hybrid orbital of the carbonyl carbon becomes richer in p-character, suggesting the syn configuration causes the carbonyl carbon hybrid orbitals to adopt a geometry reminiscent of a tetrahedral-like intermediate. Our work reveals important insights into the role of substrate conformation in activating the reactive carbonyl of a scissile bond. These findings have implications for designing potent active site inhibitors based on the concept of transition state analogues. |Glycine/chemistry [MESH] |Models, Molecular [MESH] |Peptide Hydrolases/*chemistry [MESH] |Protein Conformation [MESH] |Quantum Theory [MESH] |Ubiquitin-Specific Proteases/chemistry [MESH] |Ubiquitin/chemistry [MESH]Restricting the ? Torsion Angle Has Stereoelectronic Consequences on a(epmc).pdf DeepDyve Pubget Overpricing