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10.1016/j.jmr.2014.11.015 http://scihub22266oqcxt.onion/10.1016/j.jmr.2014.11.015 C4372479!4372479 !25681966     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25681966 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       J+Magn+Reson 2015 ; 253 (?): 129-37 Nephropedia Template TP {{tp|p=25681966 |t=2015. Solid-state NMR and membrane proteins |pdf=|usr=}}{{25681966 }} gab.com Text Solid-state NMR and membrane proteins JO: J Magn Reson http://www.kidney.de/pget.php?&tw=1&pmid=25681966 #FOAvip The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects of solid-state NMR, and the chemical shift and homo- and hetero-nuclear dipole-dipole interactions. Solid-state NMR has advanced sufficiently to enable the structures of membrane proteins to be determined under near-native conditions in phospholipid bilayers. Twit Text FOAVip Solid-state NMR and membrane proteins ????J Magn Reson http://www.kidney.de/pget.php?&tw=1&pmid=25681966 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25681966 #FOAvip English Wikipedia <ref>{{Cite pmid|25681966 }}</ref> Solid-state NMR and membrane proteins #MMPMID25681966 Opella SJ J Magn Reson 2015[Apr]; 253 (?): 129-37 PMID25681966 show ga The native environment for a membrane protein is a phospholipid bilayer. Because the protein is immobilized on NMR timescales by the interactions within a bilayer membrane, solid-state NMR methods are essential to obtain high-resolution spectra. Approaches have been developed for both unoriented and oriented samples, however, they all rest on the foundation of the most fundamental aspects of solid-state NMR, and the chemical shift and homo- and hetero-nuclear dipole-dipole interactions. Solid-state NMR has advanced sufficiently to enable the structures of membrane proteins to be determined under near-native conditions in phospholipid bilayers. |Amino Acid Sequence [MESH] |Binding Sites [MESH] |Lipid Bilayers/*chemistry [MESH] |Membrane Proteins/*chemistry/*ultrastructure [MESH] |Molecular Sequence Data [MESH] |Nuclear Magnetic Resonance, Biomolecular/*methods [MESH] |Phospholipids/*chemistry [MESH] |Protein Binding [MESH] |Protein Conformation [MESH]Solid-state NMR and membrane proteins (epmc).pdf DeepDyve Pubget Overpricing