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Myoglobin and hemoglobin quaternary structures. Reprinted from

Myoglobin and the heme-CO coordinate system

Myoglobin concentration in various modem species, indicating the much higher ratio present in humans. The cluster of lines at the bottom of the graph come from eight modern species

Myoglobin has been successfully immobilized into a mesoporous MOF with hierarchical pore sizes, which demonstrates interesting size-selective biocatalysis performance

Myoglobin reactions Mb

Myoglobin-ligand interaction contour map in the xy plane aty 0.5 A see

Myoglobin-ligand interaction contour maps in the heme showing protein relaxation a cross marks the iron atom projection onto the plane. Distances are in A and contours in kcal the values shown correspond to 45,10,0, and - 3 kcal mol relative to the ligand at infinity. The highest contours are closest to the atoms whose projections onto the plane of the figure are denoted by circles. Panel I

Myoglobin-ligand interaction contour maps in the heme xy plane at z 3.2 A showing protein relaxation a cross marks the iron atom projection onto the plane. Distances are in A and contours in kcal the values shown correspond to 90, 45,10, 0, and —3 kcal mol relative to the ligand at infinity. The highest contours are closest to the atoms whose projections onto the plane of the figure are denoted by circles. Panel I

Myoglobin. After J. . Kroschwitz and M. Winokur, Chemistry

Myoglobin. Taken from Stryer, Biochemistry, 3rd edn, Freeman , with permission.

Myohemerythrin as an example of an up-and-down helix bundle, schematic drawing of the backbone structure, from the same viewpoint as in a.

Myophosphorylase deficiency

Myosin and actin molecules and myosin crossbridges. Each kind of filament is composed of a different protein

Myosin Dissection. Treatment of muscle myosin with proteases forms stable fragments, including subfragments SI and S2 and light meromyosin. Each SI fragment includes the head .

Myosin filament structure. Dit rams of myosin monomer packing in non-helical side-polar and helical bipolar filaments. For simplicity, only one myosin head per monomer is shown. A bare zone is observed at the center of the bi-polar filament, and at each end of the side-polar filament

Myosin fragmentation by papain and trypsin

Myosin isoforms and SMC phenotypes during rabbit development, d.a., ductus arteriosus ao., aorta.

Myosin Lever Arm Length. Examination of the rates of actin movement supported by a set of myosin mutants with different numbers of light-chain binding sites revealed a linear relation the greater the number of light-chain binding sites

Myosin lever-arm length.

Myosin light chain kinase is phosphorylated during microcystin-evoked contraction in both control and PDBu downregulated tissues. Control and downregu-lated tissues were incubated in calcium-free solution containing 10 mM EGTA and then stimulated with 1 pM microcystin for 1 hr in the presence of P-ATP, homogenized, and subjected to immunoprecipitation with an antibody against MLCK. A

Myosin Light Chains. The structures of the essential and regulatory light chains from muscle myosin are compared with the structure of calmodulin. Each of these homologous proteins binds an a helix by wrapping around it.

Myosin motion along actin. A myosin head . The release of P, 5 accompanying this binding increases the strength of the interaction between myosin and actin and resets the orientation of the lever arm.

Myosin structure at high resolution, The structure of the 51 fragment from muscle myosin reveals the presence of a P-loop NTPase domain . Notice that an a helix that extends from this domain is the binding site for the two light chains. Drawn fron i IDFLpdb.

Myosin Structure at High Resolution. The structure of the SI fragment from muscle myosin reveals the presence of a P-loop NTPase domain . An a helix that extends from this domain is the binding site for the two light chains.

Myosin Structure at Low Resolution. Electron micrographs of myosin molecules reveal a two-headed structure with a long, thin tail. Courtesy of Dr. Paula Flicker, Dr. Theo Walliman, and Dr. Peter Vihert.



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