Article
Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.
The journal of physical chemistry. B - 27 Feb 2014
Yu Xueting, Lorigan Gary A
Abstract excerpt
Phospholamban (PLB) is a membrane protein that regulates heart muscle relaxation rates via interactions with the sarcoplasmic reticulum Ca(2+) ATPase (SERCA). When PLB is phosphorylated or Arg9Cys (R9C) is mutated, inhibition of SERCA is relieved. (13)C and (15)N solid-state NMR spectroscopy is utilized to investigate conformational changes of PLB upon phosphorylation and R9C mutation. (13)C═O NMR spectra of the...
Topics
- Calcium-Binding Proteins
- Magnetic Resonance Spectroscopy
- Mutation
- Phospholipids
- Phosphorylation
- Protein Structure, Secondary
- Protein Structure, Tertiary