Abstract
Resonance assignments recently obtained on immobilized polypeptides and a membrane protein aggregate under Magic Angle Spinning are compared to random coil values in the liquid state. The resulting chemical shift differences (secondary chemical shifts) are evaluated in light of the backbone torsion angle ψ previously reported using X-ray crystallography. In all cases, a remarkable correlation is found suggesting that the concept of secondary chemical shifts, well established in the liquid state, can be of similar importance in the context of multiple-labelled polypeptides studied under MAS conditions.
Original language | English (US) |
---|---|
Pages (from-to) | 325-331 |
Number of pages | 7 |
Journal | Journal of Biomolecular NMR |
Volume | 20 |
Issue number | 4 |
DOIs | |
State | Published - 2001 |
Externally published | Yes |
Keywords
- Chemical shifts
- Magic angle spinning
- Membrane proteins
- Protein aggregates
- Secondary structure
- Solid-state NMR
ASJC Scopus subject areas
- Biochemistry
- Spectroscopy