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Myosins

About 20 different myofibrillar proteins are known. Myosin, actin and titin quantitatively predominate, acounting for 65-70% of the total protein. The remaining proteins are the tropomyosins and troponins, which are important for contraction, and various cytoskeletal proteins, which are involved in the stabilization of the sarcomere. [Pg.568]

Myosin molecules form the thick filaments and make up about 50% of the total proteins present in the contractile apparatus. Myosin can be isolated from muscle tissue with a high ionic strength buffer, for example, 0.3mol/lKCl/0.15mol/1 phosphate buffer, pH 6.5. The molecular weight of myosin is approx. 500kdal. Myosin consists [Pg.568]

Assembly of the actin network merely by interaction with these binding proteins can itself account for pseudopodia formation and propulsive movement. However, there is some evidence to suggest that F-actin-myosin interactions are required for vectorial movement hence it has been demonstrated that pseudopodia contain filament networks comprising actin and myosin. Myosin plays a role in the contractile movement of neutrophils in a [Pg.136]


Globulins. Proteins insoluble in water, soluble in dilute salt solutions. They include such proteins as myosin from muscle, fibrinogen from blood and edcstin from hemp. [Pg.331]

Figure Bl.17.6. A protein complex (myosin SI decorated filamentous actin) embedded in a vitrified ice layer. Shown is a defociis series at (a) 580 mn, (b) 1130 mn, (c) 1700 mn and (d) 2600 mn underfocus. The pictures result from averagmg about 100 individual images from one electron micrograph the decorated filament length shown is 76.8 nm. Figure Bl.17.6. A protein complex (myosin SI decorated filamentous actin) embedded in a vitrified ice layer. Shown is a defociis series at (a) 580 mn, (b) 1130 mn, (c) 1700 mn and (d) 2600 mn underfocus. The pictures result from averagmg about 100 individual images from one electron micrograph the decorated filament length shown is 76.8 nm.
Figure Bl.17.12. Time-resolved visualization of the dissociation of myosin SI from filamentous actin (see also figure Bl.17.6). Shown are selected filament images before and after the release of a nucleotide analogue (AMPPNP) by photolysis (a) before flashing, (b) 20 ms, (c) 30 ms, (d) 80 ms and (e) 2 s after flashing. Note the change in obvious order (as shown by the diffraction insert in (a)) and the total dissociation of the complex in (e). The scale bar represents 35.4 mn. Picture with the courtesy of Academic Press. Figure Bl.17.12. Time-resolved visualization of the dissociation of myosin SI from filamentous actin (see also figure Bl.17.6). Shown are selected filament images before and after the release of a nucleotide analogue (AMPPNP) by photolysis (a) before flashing, (b) 20 ms, (c) 30 ms, (d) 80 ms and (e) 2 s after flashing. Note the change in obvious order (as shown by the diffraction insert in (a)) and the total dissociation of the complex in (e). The scale bar represents 35.4 mn. Picture with the courtesy of Academic Press.
Payment i, Hoiden H M, Whittacker M, Yohn C B, Lorenz M, Hoimes K C and Miiiigan R A 1993 Structure of the actin-myosin compiex and its impiications for muscie contraction Science 261 58-65... [Pg.1651]

Schroder R R, Jahn W, Manstein D, Hoimes K C and Spudich J A 1993 Three-dimensionai atomic modei of F-actin decorated with Dictyostelium myosin SI Nature 364 171-4... [Pg.1651]

Warshaw D M, Hayes E, Gaffney D, Lauzon A-M, Wu J, Kennedy G, Trybus K, Lowey S and Berger C 1998 Myosin conformational states determined by single fluorophore polarization Proc. Natl Acad. Sc/. USA 95 8034-9... [Pg.2511]

Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, Tanaka H and Yanagida T 1998 Simultaneous observation of individual ATPase and mechanical events by a single myosin molcule during interaction with actin Ce//92 161-71... [Pg.2848]

Funatsu T, Flarada Y, Tokunaga M, Saito K and Yanagida T 1995 Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution Nature 374 555-9... [Pg.2850]

Which of the two models for the mode of ATP interaction with myosin do these data support Explain your answer by quantitative interpretation of the light-scattering data. [Pg.719]

Microfilaments and Microtubules. There are two important classes of fibers found in the cytoplasm of many plant and animal ceUs that are characterized by nematic-like organization. These are the microfilaments and microtubules which play a central role in the determination of ceU shape, either as the dynamic element in the contractile mechanism or as the basic cytoskeleton. Microfilaments are proteinaceous bundles having diameters of 6—10 nm that are chemically similar to actin and myosin muscle ceUs. Microtubules also are formed from globular elements, but consist of hoUow tubes that are about 30 nm in diameter, uniform, and highly rigid. Both of these assemblages are found beneath the ceU membrane in a linear organization that is similar to the nematic Hquid crystal stmcture. [Pg.202]

Contraction of muscle follows an increase of Ca " in the muscle cell as a result of nerve stimulation. This initiates processes which cause the proteins myosin and actin to be drawn together making the cell shorter and thicker. The return of the Ca " to its storage site, the sarcoplasmic reticulum, by an active pump mechanism allows the contracted muscle to relax (27). Calcium ion, also a factor in the release of acetylcholine on stimulation of nerve cells, influences the permeabiUty of cell membranes activates enzymes, such as adenosine triphosphatase (ATPase), Hpase, and some proteolytic enzymes and facihtates intestinal absorption of vitamin B 2 [68-19-9] (28). [Pg.376]

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. [Pg.211]

In the presence of calcium, the primary contractile protein, myosin, is phosphorylated by the myosin light-chain kinase initiating the subsequent actin-activation of the myosin adenosine triphosphate activity and resulting in muscle contraction. Removal of calcium inactivates the kinase and allows the myosin light chain to dephosphorylate myosin which results in muscle relaxation. Therefore the general biochemical mechanism for the muscle contractile process is dependent on the avaUabUity of a sufficient intraceUular calcium concentration. [Pg.125]

Alpha helices are sufficiently versatile to produce many very different classes of structures. In membrane-bound proteins, the regions inside the membranes are frequently a helices whose surfaces are covered by hydrophobic side chains suitable for the hydrophobic environment inside the membranes. Membrane-bound proteins are described in Chapter 12. Alpha helices are also frequently used to produce structural and motile proteins with various different properties and functions. These can be typical fibrous proteins such as keratin, which is present in skin, hair, and feathers, or parts of the cellular machinery such as fibrinogen or the muscle proteins myosin and dystrophin. These a-helical proteins will be discussed in Chapter 14. [Pg.35]

Fibrous proteins can serve as structural materials for the same reason that other polymers do they are long-chain molecules. By cross-linking, interleaving and intertwining the proper combination of individual long-chain molecules, bulk properties are obtained that can serve many different functions. Fibrous proteins are usually divided in three different groups dependent on the secondary structure of the individual molecules coiled-coil a helices present in keratin and myosin, the triple helix in collagen, and P sheets in amyloid fibers and silks. [Pg.283]

The leucine zipper DNA-binding proteins, described in Chapter 10, are examples of globular proteins that use coiled coils to form both homo- and heterodimers. A variety of fibrous proteins also have heptad repeats in their sequences and use coiled coils to form oligomers, mainly dimers and trimers. Among these are myosin, fibrinogen, actin cross-linking proteins such as spectrin and dystrophin as well as the intermediate filament proteins keratin, vimentin, desmin, and neurofilament proteins. [Pg.287]

Muscle fibers contain myosin and actin which slide against each other during muscle contraction... [Pg.290]

Figure 14.10 A muscle viewed under the microscope is seen to contain many myofibrils that show a cross-striated appearance of alternating light and darkbands, arranged in repeating units called sarcomeres. The dark bands comprise myosin filaments and are interupted by M (middle) lines, which link adjacent myosin filaments to each other. Figure 14.10 A muscle viewed under the microscope is seen to contain many myofibrils that show a cross-striated appearance of alternating light and darkbands, arranged in repeating units called sarcomeres. The dark bands comprise myosin filaments and are interupted by M (middle) lines, which link adjacent myosin filaments to each other.
Myosin heads form cross-bridges between the actin and myosin filaments... [Pg.291]

Within each sarcomere the relative sliding of thick and thin filaments is brought about by "cross-bridges," parts of the myosin molecules that stick out from the myosin filaments and interact cyclically with the thin actin filaments, transporting them hy a kind of rowing action. During this process, the hydrolysis of ATP to ADP and phosphate couples the conformational... [Pg.291]

Figure 14.11 The sliding filament model of muscle contraction. The actin (red) and myosin (green) filaments slide past each other without shortening. Figure 14.11 The sliding filament model of muscle contraction. The actin (red) and myosin (green) filaments slide past each other without shortening.
Figure 14.12 The swinging cross-bridge model of muscle contraction driven by ATP hydrolysis, (a) A myosin cross-bridge (green) binds tightly in a 45 conformation to actin (red), (b) The myosin cross-bridge is released from the actin and undergoes a conformational change to a 90 conformation (c), which then rebinds to actin (d). The myosin cross-bridge then reverts back to its 45° conformation (a), causing the actin and myosin filaments to slide past each other. This whole cycle is then repeated. Figure 14.12 The swinging cross-bridge model of muscle contraction driven by ATP hydrolysis, (a) A myosin cross-bridge (green) binds tightly in a 45 conformation to actin (red), (b) The myosin cross-bridge is released from the actin and undergoes a conformational change to a 90 conformation (c), which then rebinds to actin (d). The myosin cross-bridge then reverts back to its 45° conformation (a), causing the actin and myosin filaments to slide past each other. This whole cycle is then repeated.

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A-Myosin

Actin cytoskeleton dynamics myosin

Actin filaments myosin

Actin filaments myosin heads

Actin filaments myosin interactions with

Actin myosin ATPase activation

Actin myosin complex

Actin myosin interactions, phosphorylation

Actin myosin reaction with

Actin-myosin

Actin-myosin cross-bridges

Actin-myosin interaction

Actin-myosin interaction regulators

Actin-myosin muscle system

Activation energy myosin-actin interaction

Acto-myosin interactions

Amino myosin

Asthma, myosin light chain Kinase

Axonal transport myosin

Calcium myosin phosphorylation, other

Calcium/calmodulin-dependent protein kinases myosin light chain kinase phosphorylation

Caldesmon myosin interactions

Calmodulin myosin light chain kinase binding

Calmodulin-binding peptides myosin light-chain kinase

Cell locomotion myosins

Coiled-coil myosin

Contraction myosin phosphorylation

Contraction myosin regulatory light chain

Cooperativity myosin-actin interaction

Coupling myosin light chain phosphorylation

Cross-bridge cycling myosin isoforms

Cross-bridges with myosin

Crystal structures, myosin

Denaturation of myosins

Dictyostelium myosin

Diffraction pattern from myosin head array

Enzymes myosin

Enzymes myosin light chain kinase

F-actin filament with myosin heads

Fetal heavy-chain myosin

Force regulation, myosin light chain

Frozen storage myosin

Frozen storage myosin, changes during

Hearing myosin

Heavy chains myosin

Heavy meromyosin myosin interactions

How Is It Coupled to the Interaction between Myosin and Actin

Light chains myosin

Meat proteins myosin

Molecular structure of the myosin molecule

Motor proteins myosin

Muscle contraction myosin

Muscle contraction myosin light chain kinase

Muscle contraction myosin-based

Muscle myosin

Muscle myosin, filament

Muscle structure myosin

Myofibrillar myosin

Myosin 52 regions

Myosin ATP and

Myosin ATPase

Myosin ATPase activity

Myosin ATPase course

Myosin ATPase dependence

Myosin ATPase product dissociation

Myosin ATPase, mechanism

Myosin II motor

Myosin Interaction

Myosin P light chains

Myosin Phosphorylation in Smooth Muscle

Myosin SI fragment

Myosin Subject

Myosin actin binding

Myosin actin complex, structure

Myosin activation

Myosin activation kinetics

Myosin actomyosin

Myosin adenosine triphosphatase activity

Myosin aggregation

Myosin amino acid composition

Myosin amino acid sequence

Myosin analysis

Myosin and

Myosin antibody preparation

Myosin assay

Myosin assembly

Myosin assembly control

Myosin assembly/polymerization

Myosin binding proteins

Myosin binding region structure

Myosin calcium sensitivity

Myosin calmodulin binding domain

Myosin catalysis

Myosin chains

Myosin cloning

Myosin coiled coil structure

Myosin complex structure

Myosin components

Myosin concentration, muscle

Myosin contraction

Myosin contraction cycling

Myosin cooperativity

Myosin cross-bridge cycling, rates

Myosin cross-bridges

Myosin crossbridge

Myosin crystalline

Myosin denaturation

Myosin diffusion constant

Myosin drawing

Myosin electrophoretic mobilities

Myosin enzymatic activity

Myosin enzyme activity

Myosin essential chain

Myosin extractability, effect

Myosin fibers

Myosin figure

Myosin filament assembly

Myosin filament cross-bridge

Myosin filament perpendicular

Myosin filament structure

Myosin filaments

Myosin filaments in muscle

Myosin filaments of scallop, figure

Myosin fragment expression

Myosin function

Myosin head

Myosin head contraction

Myosin head cooperativity

Myosin head domain

Myosin head region

Myosin heads, structure

Myosin heavy

Myosin heavy and light chains

Myosin heavy chain interactions

Myosin heavy chain isoforms, expression

Myosin heavy chain kinase

Myosin heavy chain phosphorylation

Myosin heavy chain splicing

Myosin heavy chain staining

Myosin heavy chains familial hypertrophic cardiomyopathy

Myosin hydrolyzing

Myosin inhibitors

Myosin isoelectric point

Myosin isoforms

Myosin isolation

Myosin kinase

Myosin length

Myosin light

Myosin light chain interacting protein

Myosin light chain interactions

Myosin light chain kinase

Myosin light chain kinase MLCK)

Myosin light chain kinase calcium sensitivity

Myosin light chain kinase, phosphorylation

Myosin light chain phosphatase

Myosin light chain phosphatase (MLCP

Myosin light chain phosphatase inhibitors

Myosin light chain phosphatase regulation

Myosin light chain phosphatase subunits

Myosin light chain phosphatase targeting

Myosin light chain removal effects

Myosin light chains calcium free

Myosin light chains calcium sensitivity

Myosin light chains cycling

Myosin light chains dephosphorylation

Myosin light chains initial

Myosin light chains measurement

Myosin light chains mechanisms

Myosin light chains muscle

Myosin light chains regulation

Myosin light chains regulatory chain

Myosin light chains steady state

Myosin machine

Myosin mechanical experiments

Myosin molecular structure

Myosin molecular weight

Myosin molecule

Myosin molecule schematic

Myosin monomer

Myosin motor domain

Myosin motor domain stereo view

Myosin muscle physiology

Myosin myofibrillar proteins

Myosin organization

Myosin overview

Myosin peptide chains

Myosin pharmacomechanical coupling

Myosin phosphatases

Myosin phosphate turnover rate

Myosin phosphorylation

Myosin phosphorylation effects

Myosin phosphorylation, calcium sensitivity

Myosin photoaffinity label

Myosin physiological properties

Myosin polarity

Myosin polymerization

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Myosin regulatory proteins

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Myosin striated muscle

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Myosin telokin

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Myosin translation

Myosin triphosphatase

Myosin tropomyosin

Myosin tryptic digestion

Myosin, 3-methylhistidine

Myosin, amino acids

Myosin, and actin

Myosin, enzymatic hydrolysis

Myosin, rabbit skeletal

Myosin, self-assembly

Myosin, subfragments

Myosin, thyroid hormones

Myosin-actin interaction dissociation-association

Myosin-actin interaction technique

Myosin-actin interaction, troponin

Myosin-actin interaction, troponin inhibitory action

Myosin-adenosine triphosphatase

Myosin-adenosine triphosphatase ATPase) activity

Myosin-containing filaments

Myosin/paramyosin

Myosine light chain kinase

Myosins actin interactions with

Papain myosin fragmentation

Phosphorylation myosin light chains

Phosphorylation of Smooth Muscle Myosin Heavy Chains

Photoaffinity labels of myosin

Platelet activation myosin light chain

Protein kinase myosin light chain

Proteins) myosin

Regulatory proteins myosin-associated

Relaxation phosphorylation, myosin light

S-Myosin

Sarcomeres myosin filaments

Smooth Muscle Myosin Phosphatase

Smooth muscle myosin heavy chain

Striated muscle actin-myosin interactions

Striated muscle myosin molecules

Studying acto-myosin interactions

The Catalytic Strategy of P-O Bond-Cleaving Enzymes Comparing EcoRV and Myosin

The myosin motor

Trypsin myosin fragmentation

Unconventional myosins

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