Kinetics of the Antibody Recognition Site in the Third IgG‐Binding Domain of Protein G |
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| Authors: | Supriya Pratihar Prof. Dr. T. Michael Sabo Dr. David Ban Dr. R. Bryn Fenwick Dr. Stefan Becker Prof. Dr. Xavier Salvatella Prof. Dr. Christian Griesinger Prof. Dr. Donghan Lee |
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| Affiliation: | 1. Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, G?ttingen, Germany;2. Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, KY, USA;3. Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Spain;4. Department of Integrative Structural and Computational Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA;5. Institució Catalana de Recerca i Estudis Avan?ats (ICREA), Barcelona, Spain |
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| 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 ( ) and 40 μs (supra‐ window), strongly influence molecular recognition. This supra‐ 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‐ dynamics. This β‐turn is involved in antibody binding, exhibiting the potential link of the observed supra‐ motion with molecular recognition. |
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| Keywords: | kinetics NMR spectroscopy protein dynamics relaxation dispersion |
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