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10.1007/s00775-018-1552-x http://scihub22266oqcxt.onion/10.1007/s00775-018-1552-x C6006191!6006191!29569085     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       J+Biol+Inorg+Chem 2018 ; 23 (4): 665-85 Nephropedia Template TP {{tp|p=29569085|t=2018. The NMR contribution to protein?protein networking in Fe?S protein maturation |pdf=|usr=}}{{29569085}} gab.com Text The NMR contribution to protein protein networking in Fe S protein maturation JO: J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=29569085 #FOAvip Iron?sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe?S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe?2S], [3Fe?4S] and [4Fe?4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe?S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe?S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of ?Fe?S interactomics?. This contribution was particularly effective when protein?protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies. Twit Text FOAVip The NMR contribution to protein protein networking in Fe S protein maturation ????J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=29569085 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29569085 #FOAvip English Wikipedia <ref>{{Cite pmid|29569085}}</ref> The NMR contribution to protein?protein networking in Fe?S protein maturation #MMPMID29569085 Banci L; Camponeschi F; Ciofi-Baffoni S; Piccioli M J Biol Inorg Chem 2018[]; 23 (4): 665-85 PMID29569085show ga Iron?sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe?S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe?2S], [3Fe?4S] and [4Fe?4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe?S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe?S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of ?Fe?S interactomics?. This contribution was particularly effective when protein?protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies. äThe NMR contribution to protein?protein networking in Fe?S protein mat(epmc).pdf DeepDyve Pubget Overpricing