FRET analysis

FRET analysis is the analysis method for the modeling Protein complex and etc... on the basis of the distance information specific residues between the Biomacromolecule whose 3D Structure is known and FRET(Fluorescence resonance energy transfer).

References (Reports that utilize this program) :

• Murakami K., Stewart M., Nozawa K., Tomii K., Kudou N., Igarashi N., Shirakihara Y., Wakatsuki S.,Yasunaga T., and Wakabayashi T.: Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T.,　 ProNAS, 105(20), 7200-5 (2008)

• Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T. Structural basis for Ca2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. J Mol Biol. 352(1) 178-201 (2005)　

• Yasunaga T., and Wakabayashi T: Relocation of Cys374 of actin induced by labeling with fluorescent dyes, J. Biochem. (TOKYO) 129: (2) 201-204. (2001)

• Yasunaga, T., Suzuki, Y., Ohkura, R., Sutoh, K., and Wakabayashi T.: ATP-induced transconformation of myosin revealed by determining three-dimensional positions of fluorophores from fluorescence energy transfer measurements., J Struct Biol.132(1) 6-18. (2000)

• Suzuki, Y., Yasunaga, T., Ohkura, R., Wakabayashi T., Sutoh, K.: Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps., Nature. 396(6709):380-3. (1998)