What Drives ¹⁵N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail.

ABSTRACT: Backbone (¹⁵N) NMR relaxation is one of the main sources of information on dynamics of disordered proteins. Yet, we do not know very well what drives ¹⁵N relaxation in such systems, i.e., how different forms of motion contribute to the measurable relaxation rates. To address this problem, we have investigated, both experimentally and via molecular dynamics simulations, the dynamics of a 26-residue peptide imitating the N-terminal portion of the histone protein H4. One part of the peptide was found to be fully flexible, whereas the other part features some transient structure (a hairpin stabilized by hydrogen bonds). The following motional modes proved relevant for ¹⁵N relaxation. 1) Sub-picosecond librations attenuate relaxation rates according to S^2</

SUBMITTER: Kampf K 

PROVIDER: S-EPMC6302223 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature