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  • Title: Decreased thermodynamic stability as a crucial factor for familial amyloidotic polyneuropathy.
    Author: Niraula TN, Haraoka K, Ando Y, Li H, Yamada H, Akasaka K.
    Journal: J Mol Biol; 2002 Jul 05; 320(2):333-42. PubMed ID: 12079390.
    Abstract:
    A single mutation in the wild-type transthyretin (WT TTR) such as V30M causes a familial amyloidotic polyneuropathy disease. Comparison of the three-dimensional crystal structures of WT and V30M does not tell much about the reason. High-pressure NMR revealed that at neutral pH both WT and V30M exist as equilibrium between the native tetramer and the dissociated/unfolded monomer. The native tetramer is highly stable in WT (deltaG(0)=104 kJ/mol at 37 degrees C, pH 7.1), but the stability is significantly reduced in V30M (deltadeltaG(0)=-18 kJ/mol), increasing the fraction of the unfolded monomer by a 1000-fold. Significant reduction of thermodynamic stability of WT TTR by mutation could be a crucial factor for familial amyloidotic polyneuropathy.
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