title: Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
abstract: Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1-antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. From measurements of site-specific15N relaxation rates including relaxation dispersion we obtain snapshots of dynamics spanning nine orders of magnitude in terms of the time scale. A comparison of measurements for GB1 in either environment reveals that while many of the dynamic features of the protein are conserved between them (in particular for the fast picosecond-nanosecond motions), much greater differences occur for slow motions with motions in the >500 ns range being more prevalent in the complex. The data suggest that GB1 can potentially undergo a small-amplitude overall anisotropic motion sampling the interaction interface in the complex.
authors.affiliation: Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL (UK).
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Lamley
authors.affiliation: Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL (UK).
authors.forename: Carl
authors.initials: C
authors.lastname: Öster
authors.affiliation: Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL (UK).
authors.forename: Rebecca A
authors.initials: RA
authors.lastname: Stevens
authors.affiliation: Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL (UK).
authors.forename: Józef R
authors.initials: JR
authors.lastname: Lewandowski
keywords: NMR‐Spektroskopie; Proteindynamik; Protein‐Antikörper‐Komplexe; Protein‐Protein‐Wechselwirkungen; Rotation um den magischen Winkel