作者: Guo-Ping Zhou , Dong Chen , Siming Liao , Ri-Bo Huang
DOI: 10.2174/1568026615666150819104617
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摘要: All residues in an alpha helix can be characterized and dispositioned on a 2D the wenxiang diagram, which possesses following features: (1) relative locations of amino acids α-helix clearly displayed regardless how long it is; (2) direction alphahelix indicated; (3) more information regarding each constituent acid helix. Owing to its intuitionism easy visibility, diagrams have had immense influence our understanding protein structure, protein-protein interactions, effect helical structural stability conformational transitions. In this review, we summarize two recent applications incorporating NMR spectroscopy researches coiled-coil interactions related regulation contraction or relaxation states vascular smooth muscle cells, effects α-helical misfolding prion disease, hopes that gained valuable through these studies stimulate widely biology.