Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Robustelli P, Cavalli A, Vendruscolo M. Determination of protein structures in the solid state from NMR chemical shifts. Structure. 2008 Dec 10;16(12):1764-9. PMID:19081052 doi:10.1016/j.str.2008.10.016
