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1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100 beta.

The homodimeric S100 protein calcyclin has been studied in the apo state by two-dimensional 1H NMR spectroscopy. Using a combination of scalar correlation and NOE experiments, sequence-specific 1H NMR assignments were obtained for all but one backbone and > 90% of the side-chain resonances. To ou...

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Bibliografski detalji
Glavni autori: Potts, B. C., Carlström, G., Okazaki, K., Hidaka, H., Chazin, W. J.
Format: Artigo
Jezik:Inglês
Izdano: Cold Spring Harbor Laboratory Press 1996
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143283/
https://ncbi.nlm.nih.gov/pubmed/8931135
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