NMR Scalar Couplings across Intermolecular Hydrogen Bonds between Zinc-Finger Histidine Side Chains and DNA Phosphate Groups.

ABSTRACT: NMR scalar couplings across hydrogen bonds represent direct evidence for the partial covalent nature of hydrogen bonds and provide structural and dynamic information on hydrogen bonding. In this article, we report heteronuclear ¹⁵N-³¹P and ¹H-³¹P scalar couplings across the intermolecular hydrogen bonds between protein histidine (His) imidazole and DNA phosphate groups. These hydrogen-bond scalar couplings were observed for the Egr-1 zinc-finger-DNA complex. Although His side-chain NH protons are typically undetectable in heteronuclear ¹H-¹⁵N correlation spectra due to rapid hydrogen exchange, this complex exhibited two His side-chain NH signals around ¹H 14.3 ppm and ¹⁵N 178 ppm at 35 °C. Through vario

SUBMITTER: Chattopadhyay A 

PROVIDER: S-EPMC5386832 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature