The solution state structure of κ-carrageenan is typically described as a 'random coil', to indicate a lack of defined secondary structure elements. From this starting point the assignment of an optical-rotation-detected change that follows the introduction of particular ions to such solutions as a 'coil-to-helix transition' seems unambiguous, and thus the canonical description of this important biopolymer's gelling behaviour was born. However, the notion that κ-carrageenan exists in solution as a random coil, devoid of secondary structure, has been questioned a number of times previously in the literature, particularly by the molecular modelling and NMR communities. Regrettably, there has been little desire to-date to address these largely overlooked studies or consider their implications for the nature of the so-called 'coil-to-helix transition'. Despite evidence to the contrary, the random-coil-paradigm has prevailed. Here, new data from synchrotron-enabled solution-state x-ray scattering experiments, combined with state-of-the-art atomistic molecular dynamics simulations, are used to show that the solution-state structure of κ-carrageenan in fact retains many of the helical motifs present in the solid-state, as inferred from fibre diffraction data. Furthermore, no evidence is found to suggest that single chains undergo any uni-molecular conformational transition upon the addition of ions. These findings once again challenge the paradigm that κ-carrageenan exists as a 'random coil' in the solution state, and thereby question the long held assumption that a uni-molecular 'coil-to-helix transition' precedes the dimerization of helices.
