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Literature DB >> 19636843

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.

Philippe S Nadaud¹, Jonathan J Helmus, Christopher P Jaroniec.

Abstract

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.

Entities: Chemical Gene

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Year: 2007 PMID： 19636843 DOI： 10.1007/s12104-007-9041-0

Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746

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Cited

8 in total

1. Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.

Authors: Eric M Jones; Bo Wu; Krystyna Surewicz; Philippe S Nadaud; Jonathan J Helmus; Shugui Chen; Christopher P Jaroniec; Witold K Surewicz
Journal: J Biol Chem Date: 2011-10-15 Impact factor: 5.157

2. Direct detection of CH/pi interactions in proteins.

Authors: Michael J Plevin; David L Bryce; Jérôme Boisbouvier
Journal: Nat Chem Date: 2010-05-02 Impact factor: 24.427

3. Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR.

Authors: Dwaipayan Mukhopadhyay; Chitrak Gupta; Theint Theint; Christopher P Jaroniec
Journal: J Magn Reson Date: 2018-10-30 Impact factor: 2.229

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.

1. Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.

2. Direct detection of CH/pi interactions in proteins.

3. Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR.

4. Measurement of ¹⁵N relaxation rates in perdeuterated proteins by TROSY-based methods.

5. Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G.

6. Nmrglue: an open source Python package for the analysis of multidimensional NMR data.

7. Density functional calculations of chemical shielding of backbone 15N in helical residues of protein G.

8. De novo protein structure generation from incomplete chemical shift assignments.