Chlorotoxin is a 36 residue disulfide rich peptide isolated from the venom of the scorpion Leiurus quinquestriatus. This peptide was shown to have the remarkable property of selectively binding to brain tumours (gliomas). The target of chlorotoxin remains under some debate with conflicting literature reports. The structure of the peptide was elucidated by homonuclear NMR spectroscopy over two decades ago, and revealed the peptide fold as a cysteine-stabilised α/β-toxin fold. The structure also indicated that the loop connecting the N-terminal section of the peptide to the α-helix (loop 2) was highly dynamic. This structural data has formed the basis of all subsequent analysis of this extraordinary peptide. Here, we sought to develop a high-yield bacterial expression system that would enable isotope labelling and subsequent heteronculear NMR studies including studies of structure and dynamics. Our heteronuclear structural data reveals a very compact structure and our multi-field relaxation analysis shows motion across multiple timescales throughout the molecule. Although loop 2 appears to be dynamic, the extent of disorder is more restricted than what had been deduced from the previous structural data alone. We further find evidence of correlated nanosecond motion across one of the disulfide bonds whilst the remaining disulfide bonds show varying degrees of conformational exchange. The combined structural and dynamics data point to three putative protein-protein interaction interfaces. Two basic patches (R14/K15/K23 and K25/K27/R36) and a hydrophobic patch including the dynamic loop 2 (F6/T7/T8/H10).