Backbone amide ¹⁵N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study.

ABSTRACT: Chemical shift tensors (CSTs) are an exquisite probe of local geometric and electronic structure. ¹⁵N CST are very sensitive to hydrogen bonding, yet they have been reported for very few proteins to date. Here we present experimental results and statistical analysis of backbone amide ¹⁵N CSTs for 100 residues of four proteins, two E. coli thioredoxin reassemblies (1-73-(U-¹³C,¹⁵N)/74-108-(U-¹⁵N) and 1-73-(U-¹⁵N)/74-108-(U-¹³C,¹⁵N)), dynein light chain 8 LC8, and CAP-Gly domain of the mammalian dynactin. The ¹⁵N CSTs were measured by a symmetry-based CSA recoupling method, ROCSA. Our results show that the principal component δ₁₁ is very sensitive to the presence of hydrogen bonding

SUBMITTER: Paramasivam S 

PROVIDER: S-EPMC6261280 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature