title: Identification of a molten globule like state in HC-N fragment of botulinum neurotoxin A: shedding light on the poorly-known features of a conserved sub-domain.
abstract: C-terminal fragment of the Botulinum neurotoxin A comprises two sub-domains including H(C)-N and H(C)-C. Here, the conformational change of H(C)-N was studied by spectroscopic techniques. The results indicated that the partially unfolded state forms during unfolding of H(C)-N. This finding may shed light on poorly--known features of the protein.
authors.affiliation: Department of Biophysics, Faculty of Basic Sciences, Tarbiat Modares University, Tehran, Iran.
authors.forename: Leila
authors.initials: L
authors.lastname: Hasani
authors.forename: Bijan
authors.initials: B
authors.lastname: Ranjbar
authors.forename: Mahmood
authors.initials: M
authors.lastname: Tavallaie
authors.forename: Majid
authors.initials: M
authors.lastname: Sadeghizadeh
mesh_terms: D019274:Botulinum Toxins, Type A / Q000737:chemistry*; D002942:Circular Dichroism; D019791:Guanidine / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013050:Spectrometry, Fluorescence
chemical_list: D010446:Peptide Fragments; D012967:Sodium Dodecyl Sulfate; D019274:Botulinum Toxins, Type A; D019791:Guanidine