Secondary chemical shifts in immobilized peptides and proteins: a qualitative basis for structure refinement under magic angle spinning

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...

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Bibliographic Details
Published in:Journal of biomolecular NMR 2001-08, Vol.20 (4), p.325-331
Main Authors: Luca, S, Filippov, D V, van Boom, J H, Oschkinat, H, de Groot, H J, Baldus, M
Format: Article
Language:English
Subjects:
Carbon - chemistry
Crystallography
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular - methods
Peptides
Peptides - chemistry
Polypeptides
Protein Structure, Secondary
Proteins
Proteins - chemistry
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Summary: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 psi 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.
ISSN:0925-2738
1573-5001
DOI:10.1023/A:1011278317489