Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin.
How close an approach is necessary for two interactive protein molecules to recognize each other before association? How strong a force field is exerted between two proteins at the recognition distance? How extensive are the association interfaces? How strong a force is necessary to pull the associated proteins apart? By means of atomic force microscopy at a truly single molecule level, these fundamental and intriguing questions were answered with the muscle proteins actin and myosin.
Nakajima
H
H
Department of Physics, Faculty of Science, Kanazawa University Kakuma-machi, Japan.
Kunioka
Y
Y
Nakano
K
K
Shimizu
K
K
Seto
M
M
Ando
T
T
D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001360:Avidin / Q000378:metabolism; D001710:Biotin / Q000031:analogs & derivatives / Q000378:metabolism; D002103:Cadaverine / Q000031:analogs & derivatives; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D018625:Microscopy, Atomic Force; D018482:Muscle, Skeletal / Q000378:metabolism; D015879:Myosin Subfragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D011503:Transglutaminases / Q000378:metabolism
D000199:Actins; D015879:Myosin Subfragments; D001360:Avidin; D001710:Biotin; D011503:Transglutaminases; D002103:Cadaverine