The preference for parallelism of the two chains in tropomyosin coiled
coils is thought to result from interchain salt bridges. To examine t
his ideal, studies are presented of tropomyosin molecules reassembled
from chaotropic solvents in acid solution, where cross-links cannot ex
ist. The acid-reassembled molecules are appreciably less disulfide cro
ss-linkable in acid than native molecules, a result explainable if som
e antiparallel dimers indeed form at low pH. Physical studies (backbon
e- and tyrosine-region CD and intrinsic viscosity) indicate that refol
ding in acid yields a molecular population demonstrably different in t
yrosine-region CD from native, but having comparable (but not identica
l) helix content, thermal stability, and dimensions. Moreover, the ref
olding in acid after either thermal or chaotropic-solvent denaturation
yields the same final state, arguing that is an equilibrium state. Al
l these results are consistent with, but do not prove, that the acid-r
eassembled population includes an appreciable fraction (2/3) of antipa
rallel coiled-coil dimers. (C) 1995 John Wiley & Sons, Inc.