2k0p | pdb_00002k0p

Determination of a Protein Structure in the Solid State from NMR Chemical Shifts

spinqualitylabelsall models 2k0p, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k0p is a 1 chain structure with sequence from Streptococcus sp. group g. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ju6 Gene: spg (Streptococcus sp. group G) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Solid-state NMR spectroscopy does not require proteins to form crystalline or soluble samples and can thus be applied under a variety of conditions, including precipitates, gels, and microcrystals. It has recently been shown that NMR chemical shifts can be used to determine the structures of the native states of proteins in solution. By considering the cases of two proteins, GB1 and SH3, we provide an initial demonstration here that this type of approach can be extended to the use of solid-state NMR chemical shifts to obtain protein structures in the solid state without the need for measuring interatomic distances. Determination of protein structures in the solid state from NMR chemical shifts.,Robustelli P, Cavalli A, Vendruscolo M Structure. 2008 Dec 10;16(12):1764-9. PMID:19081052 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein G

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