title: Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G.
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.
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
authors.forename: Supriya
authors.initials: S
authors.lastname: Pratihar
authors.affiliation: Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St, Louisville, KY, 40202, USA.
authors.forename: T Michael
authors.identifier: 0000-0002-9573-145X
authors.initials: TM
authors.lastname: Sabo
authors.affiliation: Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St, Louisville, KY, 40202, USA.
authors.forename: David
authors.identifier: 0000-0002-4993-7983
authors.initials: D
authors.lastname: Ban
authors.affiliation: Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.|Department of Integrative Structural and Computational Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA, 92037, USA.
authors.forename: R Bryn
authors.identifier: 0000-0002-0925-7422
authors.initials: RB
authors.lastname: Fenwick
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.affiliation: Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain.|Institució Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain.
authors.forename: Xavier
authors.identifier: 0000-0002-8371-4185
authors.initials: X
authors.lastname: Salvatella
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany. cigr@nmr.mpibpc.mpg.de.
authors.forename: Christian
authors.identifier: 0000-0002-1266-4344
authors.initials: C
authors.lastname: Griesinger
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany. donghan.lee@louisville.edu.|Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St, Louisville, KY, 40202, USA. donghan.lee@louisville.edu.
authors.forename: Donghan
authors.initials: D
authors.lastname: Lee
mesh_terms: D007074:Immunoglobulin G / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs
chemical_list: D007074:Immunoglobulin G
keywords: NMR spectroscopy; kinetics; protein dynamics; relaxation dispersion