Article
A topologically conserved aliphatic residue in alpha-helix 6 stabilizes the hydrophobic core in domain II of glutathione transferases and is a structural determinant for the unfolding pathway.
The Biochemical journal - 1 Dec 1998
Wallace L A, Blatch G L, Dirr H W
Abstract excerpt
A topologically conserved residue in alpha-helix 6 of domain II of human glutathione transferase (hGST) A1-1 was mutated to investigate its contribution to protein stability and the unfolding pathway. The replacement of Leu-164 with alanine (L164A) did not impact on the functional and gross structural properties of native hGST A1-1. The wild-type protein unfolds via a three-state pathway in which only folded...
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