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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-F321-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-0B86-1
Genre: Journal Article

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 Creators:
Pratihar, S.1, Author              
Sabo, T. M.1, Author              
Ban, D., Author
Fenwick, R. B., Author
Becker, S.1, Author              
Salvatella, X., Author
Griesinger, C.1, Author              
Lee, D.1, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Kinetics; NMR spectroscopy; Protein dynamics; Relaxation dispersion
 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.

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Language(s): eng - English
 Dates: 2016-06-272016-08-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201603501
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 128 (33) Sequence Number: - Start / End Page: 9719 - 9722 Identifier: -