Abstract
C-terminal fragment of the Botulinum neurotoxin A comprises two sub-domains including HC-N and HC-C. Here, the conformational change of HC-N was studied by spectroscopic techniques. The results indicated that the partially unfolded state forms during unfolding of HC-N. This finding may shed light on poorly – known features of the protein.
Keywords: H, -N, botulinum neurotoxin A, circular dichroism, fluorescence spectroscopy, molten globule like state