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

Alexander P, Fahnestock S, Lee T, Orban J, Bryan P (1992) Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry 31:3597–3603 Balayssac S, Bertini I, Falber K, Fragai M, Jehle S, Lelli M, Luchinat C, Oschkinat H, Yeo KJ (2007) Solid-state NMR of matrix metalloproteinase 12: an approach complementary to solution NMR. Chem Biochem 8:486–489 Baldus M, Petkova AT, Herzfeld J, Griffin RG (1998) Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems. Mol Phys 95:1197–1207 Bennett AE, Rienstra CM, Auger M, Lakshmi KV, Griffin RG (1995) Heteronuclear decoupling in rotating solids. J Chem Phys 103:6951–6957 Bockmann A, Lange A, Galinier A, Luca S, Giraud N, Juy M, Heise H, Montserret R, Penin F, Baldus M (2003) Solid state NMR sequential resonance assignments and conformational analysis of the 2 × 10.4 kDa dimeric form of the Bacillus subtilis. J Biomol NMR 27:323–339 Boyle MDP (1990) Bacterial immunoglobulin binding proteins. Academic Press, New York, NY, USA Clore GM, Schwieters CD (2004) Amplitudes of protein backbone dynamics and correlated motions in a small α/β protein: correspondence of dipolar coupling and heteronuclear relaxation measurements. Biochemistry 43:10678–10691 Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302 Derrick JP, Wigley DB (1994) The third IgG-binding domain from streptococcal protein G: An analysis by X-ray crystallography of the structure alone and in a complex with Fab. J Mol Biol 243:906–918 Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM (2005) Magic-angle spinning solid-state NMR spectroscopy of the β1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. J Am Chem Soc 127:12291–12305 Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM (1991) A novel, highly stable form of the immunoglobulin binding domain of streptococcal protein G. Science 253:657–661 Hall JB, Fushman D (2003) Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. J Biomol NMR 27:261–275 Hughes CE, Baldus M (2005) Magic-angle spinning solid-state NMR applied to polypeptides and proteins. Annu Rep NMR Spect 55:121–158 Igumenova TI, Wand AJ, McDermott AE (2004) Assignment of the backbone resonances for microcrystalline ubiquitin. J Am Chem Soc 126:5323–5331 McDermott AE (2004) Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. Curr Opin Struct Biol 14:554–561 Morcombe CR, Gaponenko V, Byrd RA, Zilm KW (2004) Diluting abundant spins by isotope edited radio frequency field assisted diffusion. J Am Chem Soc 126:7196–7197 Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H (2001) Backbone and side-chain 13C and 15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla. Chem Biochem 2:272–281 Takegoshi K, Nakamura S, Terao T (2001) 13C–1H dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem Phys Lett 344:631–637 Ulmer TS, Ramirez BE, Delaglio F, Bax A (2003) Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J Am Chem Soc 125:9179–9191