1. Bertrand R, Chaussepied P, Audemard E, Kassab R (1989) Functional characterization of skeletal F-actin labeled on the N-terminal segment of residues 1–28. Eur J Biochem 181: 745–754
2. Bremel RD, Weber A (1972) Cooperation within actin filament in vertebrate skeletal muscle. Nature 238: 97–101
3. Chalovich J, Eisenberg E (1982) Inhibition of actomyosin ATPase activity by troponin- tropomyosin without blocking the binding of myosin to actin. J Biol Chem 257: 2432–2437
4. dos Remedios CG, Miki M, Barden, JA (1987) Fluorescence resonance energy transfer measurements of distances in actin and myosin. A critical evaluation. J Muscle Res Cell Motil 8: 97–117
5. dos Remedios CG, Moens PDJ (1995a) Fluorescence resonance energy transfer spectroscopy is a reliable “ruler” for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. J Struct Biol 115: 175–185