Abstract：
:The subunit composition of the myosin molecule which is built up from 3 pairs of identical polypeptide chains (2 heavy chains and 2 pairs of light chains), gives it the appearance of having symmetric structure. This homodimeric arrangement in the molecule is in fact asymmetric in its construction as a result of the natural folding of the chains. There are also heterodimers which result from combinations of pairs of heavy chains and/or light chains which are not identical in their amino acid sequence. Enzyme kinetics and ligand binding are characterised by homogeneous processes in studies on isolated myosin heads. With the double-headed molecular species, myosin and its water-soluble fragment heavy meromyosin, the enzyme kinetics, nucleotide and metal ion binding exhibit negative cooperativity. Binding of Mg-ADP to active centres induces site-site and therefore head-head interaction, thus intact myosin is designed to be able to function asymmetrically. It is suggested that the ligand-induced asymmetry between the heads plays a central role in crossbridge function. The two heads, even in rest, adopt non-equivalent conformations and it is argued that this built-in constraint complements the asymmetric mode of interaction they subsequently undergo with their reaction partners on the actin filament. It is concluded that the enzyme is so constructed that during contraction the heads can perform their function in an alternating cooperative way.
journal_name
Biochimiejournal_title
Biochimieauthors
Schaub MC,Watterson JGdoi
10.1016/s0300-9084(81)80117-4subject
Has Abstractpub_date
1981-04-01 00:00:00pages
291-9issue
4eissn
0300-9084issn
1638-6183pii
S0300-9084(81)80117-4journal_volume
63pub_type
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