Folding is coupled to dimerization of tetex-1 dynein light chain

The Drosophia Tetex-1 is shown as a two-state unfolding dimer whose unfolding and dissociation are tightly coupled and this unfolding mechanism offers insight into functional differences between Tetex-1 and its structural homologue LC8. The rates and mechanisms for protein folding, for monomeric proteins depend largely on the complexity of the native structure topology rather than the details of the amino acid sequence and that protein folding mechanisms are better conserved than amino acid sequences.