5jxv

Solid-state MAS NMR structure of immunoglobulin beta 1 binding domain of protein G (GB1)

spinqualitylabelsall models 5jxv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jxv is a 1 chain structure with sequence from Streptococcus dysgalactiae subsp. equisimilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that, at 100-kHz MAS and above, spectral resolution is high enough to detect resolved correlations from amide and side-chain protons of all residue types, and to reliably measure a dense network of (1)H-(1)H proximities that define a protein structure. The high data quality allowed the correct identification of internuclear distance restraints encoded in 3D spectra with automated data analysis, resulting in accurate, unbiased, and fast structure determination. Additionally, we find that narrower proton resonance lines, longer coherence lifetimes, and improved magnetization transfer offset the reduced sample size at 100-kHz spinning and above. Less than 2 weeks of experiment time and a single 0.5-mg sample was sufficient for the acquisition of all data necessary for backbone and side-chain resonance assignment and unsupervised structure determination. We expect the technique to pave the way for atomic-resolution structure analysis applicable to a wide range of proteins. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.,Andreas LB, Jaudzems K, Stanek J, Lalli D, Bertarello A, Le Marchand T, Cala-De Paepe D, Kotelovica S, Akopjana I, Knott B, Wegner S, Engelke F, Lesage A, Emsley L, Tars K, Herrmann T, Pintacuda G Proc Natl Acad Sci U S A. 2016 Aug 16;113(33):9187-92. doi:, 10.1073/pnas.1602248113. Epub 2016 Aug 3. PMID:27489348 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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