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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-specific 15N?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.

SUBMITTER: Lamley JM 

PROVIDER: S-EPMC4954056 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.

Lamley Jonathan M JM   Öster Carl C   Stevens Rebecca A RA   Lewandowski Józef R JR  

Angewandte Chemie (Weinheim an der Bergstrasse, Germany) 20151102 51


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 <sup>15</sup>N relaxation rates including relaxation dispersion we obt  ...[more]

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