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NMR Spectroscopy

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KChIP Structure (large)

KChIP Structure (large)

The α-helices of the KIS domain (green) and the Kv4.3 N terminus (cyan) can bind to the same surface pocket on the KChIP core structure as shown by mapping of NMR chemical shift perturbation data onto a surface representation of KChIP.

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Sequence-specific assignment and secondary structure of the extracellular domain of GLIC

Sequence-specific assignment and secondary structure of the extracellular domain of GLIC

Sequence-specific assignment and secondary structure of the extracellular domain of GLIC (yellow: assigned, light blue: unassigned, dark blue: proline).

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KChIP Structure (small)

KChIP Structure (small)

The α-helices of the KIS domain (green) and the Kv4.3 N terminus (cyan) can bind to the same surface pocket on the KChIP core structure as shown by mapping of NMR chemical shift perturbation data onto a surface representation of KChIP.

Read More…

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