Premium
Intermolecular Interactions and Protein Dynamics by Solid‐State NMR Spectroscopy
Author(s) -
Lamley Jonathan M.,
Öster Carl,
Stevens Rebecca A.,
Lewandowski Józef R.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201509168
Subject(s) - chemical physics , protein dynamics , nanosecond , intermolecular force , picosecond , relaxation (psychology) , molecular dynamics , dynamics (music) , crystallography , chemistry , biological system , biophysics , physics , computational chemistry , molecule , biology , optics , laser , organic chemistry , neuroscience , acoustics
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‐specific 15 N 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.