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• W2091465425 abstract "We report the design and synthesis of model heterodimeric coiled‐coil proteins and the packing contribution of interchain hetero‐hydrophobic side‐chains to coiled‐coil stability. The heterodimeric coiled‐coils are obtained by oxidizing two 35‐residue polypeptide chains, each containing a cysteine residue at position 2 and differing in amino acid sequences in the hydrophobic positions (“a” and “d”) responsible for the formation and stabilization of the coiled‐coil. In each peptide, a single Ala residue was substituted for Leu at position “a” or “d”. The formation and stability of heterodimeric coiled‐coils were investigated by circular dichroism studies in the presence and absence of guanidine hydrochloride and compared to the corresponding homodimeric coiled‐coils. The coiled‐coil proteins with an Ala substitution at position “a” were less stable than those with an Ala substitution at position “d” in both the homodimeric (Ala‐Ala interchain interactions) and heterodimeric (Leu‐Ala interchain interactions) coiled‐coils. The 70‐residue disulfide bridged peptides (homoand heterodimeric coiled‐coils) can be readily separated by reversed‐phase chromatography (RPC) even though they have identical amino acid compositions as well as in the hydrophobic “a” and “d” positions. The elution of the 70‐residue peptides prior to their corresponding 35‐residue monomers suggests that these proteins are retaining a large portion of their coiled‐coil structure during RPC at pH 2 and their retention behavior correlates with protein stability." @default.
• W2091465425 created "2016-06-24" @default.
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• W2091465425 date "1992-09-01" @default.
• W2091465425 modified "2023-09-27" @default.
• W2091465425 title "Design, synthesis and structural characterization of model heterodimeric coiled-coil proteins" @default.
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• W2091465425 doi "https://doi.org/10.1111/j.1399-3011.1992.tb00290.x" @default.
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