Abstract
Chemical-shift-selective (13C, 13C) polarization transfer is analyzed in uniformly labeled biomolecules. It is shown that the spin system dynamics remain sensitive to the distance of interest and can be well reproduced within a quantum-mechanical multiple-spin analysis. These results lead to a general approach on how to describe chemical-shift-selective transfer in uniformly labeled systems. As demonstrated in the case of ubiquitin, this methodology can be used to detect long-range distance constraints in uniformly labeled proteins.
Original language | English (US) |
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Pages (from-to) | 100-110 |
Number of pages | 11 |
Journal | Journal of Magnetic Resonance |
Volume | 166 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2004 |
Externally published | Yes |
Keywords
- Distances
- MAS
- Polypeptides
- Solid-state
- Structure determination
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Nuclear and High Energy Physics
- Condensed Matter Physics