Assignment of proton, nitrogen-15, and backbone carbon-13 resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: A model for the coat protein monomer

Autor: Wymenga Ss, van de Ven Fj, M. L. Remerowski, Ruud N.H. Konings, C. W. Hilbers, van Os Jw, Aelen Jm

Publikováno v: Biochemistry. 32:8322-8328

The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectr

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https://doi.org/10.1021/bi00083a036

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Ligand effects of NHC-iridium catalysts for signal amplification by reversible exchange (SABRE).

Autor: van Weerdenburg BJ; Radboud University Nijmegen, Institute for Molecules and Materials, Heyendaalseweg 135, 65625 AJ Nijmegen, The Netherlands., Glöggler S, Eshuis N, Engwerda AH, Smits JM, de Gelder R, Appelt S, Wymenga SS, Tessari M, Feiters MC, Blümich B, Rutjes FP

Publikováno v: Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2013 Aug 28; Vol. 49 (67), pp. 7388-90.

Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.

Autor: van de Ven FJ; Laboratory of Biophysical Chemistry, NSR Center, University of Nijmegen, The Netherlands., van Os JW, Aelen JM, Wymenga SS, Remerowski ML, Konings RN, Hilbers CW

Publikováno v: Biochemistry [Biochemistry] 1993 Aug 17; Vol. 32 (32), pp. 8322-8.