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- W2005969596 abstract "The two-chain coiled-coil structural motif is found in fibrous muscle proteins and leucine zippers. Unfolding/refolding studies abound, but none establishes the time scale or mechanism of structural assembly from separated, unfolded chains. Stopped-flow circular dichroism studies of such refolding of alpha-tropomyosin chains are reported here. The backbone spectral region (222 nm) reveals a fast phase (less than 0.04 s), yielding an intermediate possessing approximately 70% of the equilibrium helix content. A subsequent slow phase is first order [k-1 (20 degrees C) = 1.67 s, Ea = 12.7 kcal.mol-1 (1 kcal = 4.18 kJ)], so dimerization is fast. The same rate constant characterizes folding in the Cys-190 crosslinked chains, so the intermediate has parallel and nearly registered chains. The tyrosine spectral region (280 nm) reveals only a fast phase, so these six chain sites are native in the intermediate." @default.
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- W2005969596 date "1991-02-01" @default.
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- W2005969596 title "Kinetics of self-assembly of alpha alpha-tropomyosin coiled coils from unfolded chains." @default.
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- W2005969596 doi "https://doi.org/10.1073/pnas.88.3.916" @default.
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