Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G

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,...

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Bibliographic Details
Published in:Angewandte Chemie 2016-08, Vol.128 (33), p.9719-9722
Main Authors: Pratihar, Supriya, Sabo, T. Michael, Ban, David, Fenwick, R. Bryn, Becker, Stefan, Salvatella, Xavier, Griesinger, Christian, Lee, Donghan
Format: Article
Language:eng ; ger
Subjects:
Antibodies
Binding
Chemistry
Coupling (molecular)
Dynamics
Experimental methods
Extrapolation
Immunoglobulin G
Kinetics
NMR-Spektroskopie
Order parameters
Protein G
Proteindynamik
Proteins
Reaktionskinetik
Recognition
Relaxationsdispersion
Residues
Windows (intervals)
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Summary: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. Übergänge innerhalb des Grundzustandsensembles und molekulare Erkennung hängen zusammen: Mittels Hochleistungsrelaxationsdispersionsexperimenten in stark unterkühltem Wasser kann die Supra‐ ‐Dynamik der dritten IgG‐Bindedomäne von Protein G mit deren molekularer Erkennung in Verbindung gebracht werden.
ISSN:0044-8249
1521-3757
DOI:10.1002/ange.201603501