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Journal Article

Kinetics of the antibody recognition site in the third IgG-binding domain of protein G.

MPS-Authors
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Pratihar,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Sabo,  T. M.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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2308892_Suppl.pdf
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Citation

Pratihar, S., Sabo, T. M., Ban, D., Fenwick, R. B., Becker, S., Salvatella, X., et al. (2016). Kinetics of the antibody recognition site in the third IgG-binding domain of protein G. Angewandte Chemie International Edition, 128(33), 9719-9722. doi:10.1002/anie.201603501.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-F321-7
Abstract
Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (τc ) and 40 μs (supra-τc window), strongly influence molecular recognition. This supra-τc window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high-power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 μs. For the first time, this method, performed under super-cooled conditions, enabled us to detect a global motion in the first β-turn of the third IgG-binding domain of protein G (GB3), which was extrapolated to 371±115 ns at 310 K. Furthermore, the same residues show the plasticity in the model-free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra-τc dynamics. This β-turn is involved in antibody binding, exhibiting the potential link of the observed supra-τc motion with molecular recognition.