Effects of Arg167His, Arg167Gly and Lys168Glu mutations in tropomyosin were studied.
Polarized fluorescence reported orientation of tropomyosin, actin and myosin heads.
Mutant tropomyosins were shifted from the normal position on the actin filament.
Arg167His decreased but Arg167Gly and Lys168Glu increased the switching on of actin monomers.
Arg167Gly or Lys168Glu increased fraction of myosin bound in rigor.