The effect of ring currents on carbon chemical shifts in cytochromes

Calculations suggest that some carbon chemical shifts in proteins should have large ring current shifts (> 1 ppm). We present 13C, 15N and 1H assignments for cytochrome C2 from Rhodospirillum rubrum, compare these with shifts for other cytochromes c, and show that the calculated ring current shif...

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Bibliographic Details
Published in:Journal of biomolecular NMR 1997-06, Vol.9 (4), p.389-395
Main Authors: Blanchard, L, Hunter, C N, Williamson, M P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Carbon Isotopes
Cytochrome c Group - chemistry
Cytochromes c2
Hydrogen - chemistry
Magnetic Resonance Spectroscopy - methods
Molecular Sequence Data
Nitrogen Isotopes
NMR
Nuclear magnetic resonance
Protein Structure, Secondary
Rhodospirillum rubrum - chemistry
Species Specificity
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Summary:Calculations suggest that some carbon chemical shifts in proteins should have large ring current shifts (> 1 ppm). We present 13C, 15N and 1H assignments for cytochrome C2 from Rhodospirillum rubrum, compare these with shifts for other cytochromes c, and show that the calculated ring current shifts are similar to experimentally observed shifts, but that there remain substantial conformation-dependent shifts of side-chain carbons. Ring current shifts as large as 6 ppm are observed. We show that the ring current effects do not seriously affect the Chemical Shift Index method for delineating secondary structure, but may have an impact on more precise methods for generating structural constraints.
ISSN:0925-2738
1573-5001
DOI:10.1023/A:1018394410613