Biomolecular NMR Assignments
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Backbone assignment of crystalline E. coli maltose binding protein
Biomolecular NMR Assignments - Tập 15 - Trang 317-322 - 2021
The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets. Here, we report virtually complete (~ 90%) backbone resonance assignments obtained on a microcrystalline sample of MBP with 1H-detecte...... hiện toàn bộ
Backbone NMR assignment of the internal interaction site of ALP
Biomolecular NMR Assignments - Tập 1 Số 1 - Trang 85-87 - 2007
1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C)
Biomolecular NMR Assignments - Tập 17 - Trang 67-73 - 2023
UDP-glucuronosyltransferases are the principal enzymes involved in the glucuronidation of metabolites and xenobiotics for physiological clearance in humans. Though glucuronidation is an indispensable process in the phase II metabolic pathway, UGT-mediated glucuronidation of most prescribed drugs (> 55%) and clinical evidence of UGT-associated drug resistance are major concerns for therapeutic deve...... hiện toàn bộ
1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase
Biomolecular NMR Assignments - Tập 5 - Trang 147-149 - 2010
The 17.7 kDa R2 module from Azotobacter vinelandii mannronan C5-epimerase AlgE6 has been isotopically labeled (13C,15N) and recombinantly expressed. Here we report the 1H, 13C, 15N resonance assignment of AlgE6R2.
The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East respiratory syndrome coronavirus
Biomolecular NMR Assignments - Tập 15 - Trang 341-345 - 2021
During the past 17 years, the coronaviruses have become a global public emergency, with the first appearance in 2012 in Saudi Arabia of the Middle East respiratory syndrome. Among the structural proteins encoded in the viral genome, the nucleocapsid protein is the most abundant in infected cells. It is a multifunctional phosphoprotein involved in the capsid formation, in the modulation and regulat...... hiện toàn bộ
13C and 15N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy
Biomolecular NMR Assignments - Tập 1 - Trang 117-120 - 2007
Complete 13C and 15N assignments of the B3 IgG-binding domain of protein G (GB3) in the microcrystalline solid phase, obtained using 2D and 3D MAS NMR, are presented. The chemical shifts are used to predict the protein backbone conformation and compared with solution-state shifts.
A complete backbone spectral assignment of lipid-free human apolipoprotein E (apoE)
Biomolecular NMR Assignments - Tập 2 - Trang 207-210 - 2008
Apolipoprotein E is an exchangeable apolipoprotein that plays an important role in lipid/lipoprotein metabolism and cardiovascular diseases. Recent evidence indicates that apoE is also critical in several other important biological processes, including Alzheimer’s disease, cognitive function, immunoregulation, cell signaling and infectious diseases. Although the X-ray crystal structure of the apoE...... hiện toàn bộ
NMR assignments of juvenile hormone binding protein in complex with JH III
Biomolecular NMR Assignments - Tập 3 - Trang 73-76 - 2009
A hemolymph juvenile hormone binding protein (JHBP) shuttles hydrophobic JH, a key hormone in regulation of the insect life cycle, from the site of the JH biosynthesis to the cells of target organs. We report complete NMR chemical shift assignments of Bombyx mori JHBP in the JH III-bound state.
Assignment of Ala, Ile, LeuproS, Met, and ValproS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl–methyl NOEs, site directed mutagenesis, and pseudocontact shifts
Biomolecular NMR Assignments - Tập 16 - Trang 97-107 - 2022
The protruding domain (P-domain) of the murine norovirus (MNV) capsid protein VP1 is essential for infection. It mediates receptor binding and attachment of neutralizing antibodies. Protein NMR studies into interactions of the P-domain with ligands will yield insights not easily available from other biophysical techniques and will extend our understanding of MNV attachment to host cells. Such stud...... hiện toàn bộ
1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak
Biomolecular NMR Assignments - Tập 12 Số 2 - Trang 253-257 - 2018
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