TY - JOUR
T1 - Three recent breakthroughs in molecular motor research
T2 - recombinant myosin, monomolecular in vitro motility assay and atomic structure of S1
AU - Uyeda, Taro Q.P.
PY - 1994/12
Y1 - 1994/12
N2 - Muscle contraction results from ATP-dependent sliding between actin filaments and S1 domain of myosin, but its molecular mechanism of chemomechanical energy transformation is still elusive despite decades of extensive research. There were three major breakthroughs in this field during the last few years, however; recombinant myosin technology, monomolecular in vitro motility assay, and atomic structure of S1. This article briefly reviews what is currently under dispute in this field, and introduces how molecular biologists, with these new tools in hand, are approaching those questions.
AB - Muscle contraction results from ATP-dependent sliding between actin filaments and S1 domain of myosin, but its molecular mechanism of chemomechanical energy transformation is still elusive despite decades of extensive research. There were three major breakthroughs in this field during the last few years, however; recombinant myosin technology, monomolecular in vitro motility assay, and atomic structure of S1. This article briefly reviews what is currently under dispute in this field, and introduces how molecular biologists, with these new tools in hand, are approaching those questions.
KW - Atomic structure
KW - Motor research
KW - Myosin
UR - http://www.scopus.com/inward/record.url?scp=0028740978&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028740978&partnerID=8YFLogxK
U2 - 10.1016/0928-4931(94)90022-1
DO - 10.1016/0928-4931(94)90022-1
M3 - Article
AN - SCOPUS:0028740978
VL - 2
SP - 1
EP - 11
JO - Materials Science and Engineering C
JF - Materials Science and Engineering C
SN - 0928-4931
IS - 1-2
ER -