AbstractLimited digestion of filamentous myosin with chymotrypsin at 0°C in the absence of divalent cations generates two forms of subfragment 1 (S1), with heavy chains of 95 kDa and 98 kDa. The difference is at the C-terminal end of the chain. The 98 kDa form prevails, in contrast to the preparations obtained by digestion at room temperature which consist of the shorter species and only traces of the longer one. The results support the idea of a temperature-dependent conformational transition at the head-rod junctional region of the myosin heavy chain
<div><p>Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (...
The thermal unfolding of Dictyostelium discoideum myosin head fragments with alterations in the acti...
AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ...
AbstractThe degree of helical order of the thick filament of mammalian skeletal muscle is highly dep...
AbstractThe thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of...
We compared thermally induced denaturation and aggregation of two isoforms of the isolated myosin he...
AbstractPast biochemical work on myosin subfragment 1 (S1) has shown that the bent α-helix containin...
The tryptophan fluorescence of unmodified myosin subfragment 1 (S1) from rabbit and chicken skeletal...
AbstractThe thick filaments of mammalian and avian skeletal muscle fibers are disordered at low temp...
Copyright © 2010 Park-media, Ltd. This is an open access article distributed under the Creative Comm...
AbstractTemperature-jump measurements were carried out on myosin subragment 1 (S1) labeled at Cys-70...
AbstractThe structure of the myosin subfragment-1 (SI) from rabbit skeletal muscle was studied using...
The thermal unfolding of two recombinant fragments of the head of Dictyostelium discoideum myosin II...
High-resolution proton nuclear magnetic resonance (1H NMR) measurements were made on myosin, heavy m...
ABSTRACT Myosin subfragment 1 (S1) with SH1 (Cys707) and SH2 (Cys697) groups cross-linked by p-pheny...
<div><p>Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (...
The thermal unfolding of Dictyostelium discoideum myosin head fragments with alterations in the acti...
AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ...
AbstractThe degree of helical order of the thick filament of mammalian skeletal muscle is highly dep...
AbstractThe thermal denaturation of the myosin subfragment 1 (S1) from rabbit skeletal muscle and of...
We compared thermally induced denaturation and aggregation of two isoforms of the isolated myosin he...
AbstractPast biochemical work on myosin subfragment 1 (S1) has shown that the bent α-helix containin...
The tryptophan fluorescence of unmodified myosin subfragment 1 (S1) from rabbit and chicken skeletal...
AbstractThe thick filaments of mammalian and avian skeletal muscle fibers are disordered at low temp...
Copyright © 2010 Park-media, Ltd. This is an open access article distributed under the Creative Comm...
AbstractTemperature-jump measurements were carried out on myosin subragment 1 (S1) labeled at Cys-70...
AbstractThe structure of the myosin subfragment-1 (SI) from rabbit skeletal muscle was studied using...
The thermal unfolding of two recombinant fragments of the head of Dictyostelium discoideum myosin II...
High-resolution proton nuclear magnetic resonance (1H NMR) measurements were made on myosin, heavy m...
ABSTRACT Myosin subfragment 1 (S1) with SH1 (Cys707) and SH2 (Cys697) groups cross-linked by p-pheny...
<div><p>Myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (...
The thermal unfolding of Dictyostelium discoideum myosin head fragments with alterations in the acti...
AbstractMyosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ...