1. Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger–DNA Interactions
- Author
-
Ross H. Luu, Catherine A. Kemme, B. Montgomery Pettitt, Junji Iwahara, Channing C. Pletka, and Chuanying Chen
- Subjects
010304 chemical physics ,Relaxation (NMR) ,Nuclear magnetic resonance spectroscopy ,Nuclear Overhauser effect ,010402 general chemistry ,01 natural sciences ,0104 chemical sciences ,Surfaces, Coatings and Films ,chemistry.chemical_compound ,Crystallography ,Heteronuclear molecule ,chemistry ,0103 physical sciences ,Materials Chemistry ,Side chain ,Imidazole ,Physical and Theoretical Chemistry ,Histidine ,DNA - Abstract
Due to chemical exchange, the mobility of histidine (His) side chains of proteins is typically difficult to analyze by NMR spectroscopy. Using an NMR approach that is uninfluenced by chemical exchange, we investigated internal motions of the His imidazole NH groups that directly interact with DNA phosphates in the Egr-1 zinc-finger–DNA complex. In this approach, the transverse and longitudinal cross-correlation rates for 15N chemical shift anisotropy and 15N–1H dipole–dipole relaxation interference were analyzed together with 15N longitudinal relaxation rates and heteronuclear Overhauser effect data at two magnetic field strengths. We found that the zinc-coordinating His side chains directly interacting with DNA phosphates are strongly restricted in mobility. This makes a contrast to the arginine and lysine side chains that retain high mobility despite their interactions with DNA phosphates in the same complex. The entropic effects of side-chain mobility on the molecular association are discussed.
- Published
- 2019
- Full Text
- View/download PDF