All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.

ABSTRACT: The high density of macromolecules affecting proteins due to volume exclusion has been discussed in theory but numerous in vivo experiments cannot be sufficiently understood taking only pure entropic stabilization into account. Here, we show that the thermodynamic stability of a beta barrel protein increases equally at all atomic levels comparing crowded environments with dilute conditions by applying multidimensional high-resolution NMR spectroscopy in a systematic manner. Different crowding agents evoke a pure stabilization cooperatively and do not disturb the surface or integrity of the protein fold. The here developed methodology provides a solid base that can be easily expanded to incorporate e.g. binding partners to recognize functional consequences of crowded conditions. Our results

SUBMITTER: Kohn B 

PROVIDER: S-EPMC7666220 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature