title: Length of polyglutamine tract affects secondary and tertiary structures of huntingtin protein.
abstract: The role of polyglutamine (polyQ) tract on protein stability and disease pathology remains ambiguous. We monitored the unfolding/refolding patterns of huntingtin proteins with varying polyQ lengths. In the presence of urea, minor differences in unfolding and refolding efficiencies were observed. However, in the presence of guanidinium hydrochloride, the protein with a longer polyQ stretch was able to regain its secondary but not tertiary structure on step-wise removal of denaturant. Thus, in case of Huntington's disease, the higher aggregation propensity of the mutant protein is likely to be due to the lower stability of the protein due to elongated polyQ tract.
authors: Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, Punjab 160 062, India.
authors: Shivang N
authors: SN
authors: Vachharajani
authors: Rajeev Kumar
authors: RK
authors: Chaudhary
authors: Shivcharan
authors: S
authors: Prasad
authors: Ipsita
authors: I
authors: Roy
mesh_terms: D019791:Guanidine / Q000494:pharmacology; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011489:Protein Denaturation / Q000187:drug effects; D058849:Protein Refolding / Q000187:drug effects; D055550:Protein Stability / Q000187:drug effects; D017433:Protein Structure, Secondary / Q000187:drug effects; D017434:Protein Structure, Tertiary / Q000187:drug effects; D014508:Urea / Q000494:pharmacology
chemical_list: D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D010455:Peptides; C097188:polyglutamine; D014508:Urea; D019791:Guanidine