Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy. Angew Chem Weinheim Bergstr Ger. 2015 Dec 14;127(51):15594-15598 Authors: Lamley JM, ึster C, Stevens RA, Lewandowski JR 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-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. PMID: 27478273 [PubMed - as supplied by publisher] More... |
All times are GMT. The time now is 05:54 PM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013