Biotinyl-EpsilonAhx-Omega-Conotoxin GVIA attaches a biotin tag via an EpsilonAhx spacer to a cysteine-rich conotoxin with a compact disulfide framework. The modification preserves native folding while enabling affinity capture. Its structure interacts selectively with calcium-channel subtypes. Research uses include ion-channel mapping, toxin-binding studies, and structural motif analysis.
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