Proteopedia - User contributions [en]

Myosin

2010-04-13T02:55:46Z

Laurel Koopmans:

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>
'''
{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger" /> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger" /> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger" />

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger" />

1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed

2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit

3. the binding site is closed, strengthening the myosin-actin binding

4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

Myosin

2010-04-13T02:55:08Z

Laurel Koopmans:

Myosin

2010-04-13T02:54:24Z

Laurel Koopmans: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how...

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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
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{{STRUCTURE_3cin | PDB=3cin | SCENE= }}

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''
{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger" /> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger" /> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger" />

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger" />

1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed

2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit

3. the binding site is closed, strengthening the myosin-actin binding

4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

Sandbox 171

2010-04-01T06:01:13Z

Laurel Koopmans:

Sandbox 171

2010-04-01T06:00:35Z

Laurel Koopmans:

Sandbox 171

2010-04-01T05:59:54Z

Laurel Koopmans:

Sandbox 171

2010-04-01T05:59:22Z

Laurel Koopmans:

Sandbox 171

2010-04-01T05:57:46Z

Laurel Koopmans:

Sandbox 171

2010-04-01T05:56:54Z

Laurel Koopmans:

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''
{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''

Sandbox 171

2010-04-01T05:55:24Z

Laurel Koopmans:

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''
{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>
==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''

Sandbox 171

2010-04-01T05:51:10Z

Laurel Koopmans:

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''
{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>
==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
'''
'''
[[Image:Example.jpg]]

Sandbox 171

2010-04-01T05:49:04Z

Laurel Koopmans:

Sandbox 171

2010-04-01T05:48:39Z

Laurel Koopmans:

{{STRUCTURE_2mys| PDB=2mys| Scene =Sandbox_171/Newscene/1'>active site }}
==Overview==
Myosin is one of three major classes of molecular motor proteins: myosin, dynein, and kinesin. As the most abundant of these proteins myosin plays a structural and enzymatic role in muscle contraction and intracellular motility. Myosin was first discovered in muscle in the 19th century. <ref name="Spudich">PMID: 8824453 </ref>

===Crystallization and X-ray diffraction===
Myosin is found in abundance, therefore it can be prepared in gram quantities. <ref name="Rayment">PMID: 8316857</ref> For nearly 30 years the myosin head was resistant to crystallization, yet by 1993 researchers discovered a mechanism to obtain x-ray quality crystals. <ref name="Rayment" /> The process modified the protein by reductive methylation. <ref name="Rayment" /> X-ray data was used to determine the tertiary structure of the protein. <ref name="Rayment" />

==Structure==
[[Image:Myosin_head.gif|thumb|alt=Alt text|Myosin head]]
[[Image:Myosin_chains.gif|thumb|alt=Alt text|Myosin filament]]
Myosin has a molecular size of approximately 520 kilodaltons with a total of six subunits. It has two 220 kD heavy chains which make the majority of the overall structure and two pairs of light chains which vary in size.<ref name="Rayment" /> The molecule is asymmetric, having a long tail and two globular heads. <ref name="Rayment" /> Each heavy chains composes the bulk of one of the globular heads. <ref name="Rayment" /> Subfragment-1(S1) also termed the myosin head consists of ATP, actin, and two light chain binding sites.<ref name="Rayment" /> Each globular head has a heavy chain and two light chains for a combined molecular size of about 130 kD. <ref name="Rayment" />

The myosin head is assymetrical with a length of 165 Angstroms and 65 Angstroms in width, with a total thickness of about 40 Angstroms. <ref name="Rayment" /> About 48% of the amino acid residues in the myosin head are dominated by α helices. <ref name="Rayment" /> At the carboxyl terminus one long α helix of about 85 Angstroms extends in a left-handed coil. <ref name="Rayment" /> This particular helix forms the light chain binding region of the globular domain <ref name="Rayment" /> The amino terminus of each heavy chain has a large globular domain containing the site of ATP hydrolysis.

==Function==
Molecules of myosin aggregate in muscle cells to form thick filaments. <ref name="Lehninger">Nelson, D. and Cox, M.(2005). Lehninger Principles of Biochemistry. 4th ed. p.1119. </ref> The rodlike structure of these thick filaments act as the core in the muscle contractile unit. <ref name="Lehninger" /> The aggregation of several hundred myosin forms a bipolar structure which stacks in regular arrays. Muscles consist of another protein called actin. Actin forms the thin filament in muscle fibers. Myosin and actin interact through weak bonds. Without ATP bound, the myosin head binds tightly to actin. <ref name="Lehninger"> With ATP bound, myosin releases the actin subunit and interacts with another subunit further down the thin filament. <ref name="Lehninger"> This process continues in cycle, producing movement. Interaction of myosin and actin is regulated by two other proteins, tropomyosin and troponin. <ref name="Lehninger">

The cycle of myosin-actin interaction is outlined as follows: <ref name="Lehninger">
1. ATP binds to myosin and a binding site opens on myosin head to disrupt the actin-myosin interaction, actin is released. ATP is hydrolyzed
2. a conformational change moving the protein to a "high-energy" state causes the myosin head to change orientation moving it to bind with the actin subunit closer the a region called the Z disk than the previous actin subunit
3. the binding site is closed, strengthening the myosin-actin binding
4. a power stroke quickly follows and the myosin head undergoes an additional conformational change bringing it back to the resting state in which it began

Click the link to access DNAtube video "A Moving Myosin Motor Protein"
http://www.dnatube.com/video/389/A-Moving-Myosin-Motor-Protein-myosin-actin-interaction

==Literature Cited==
<references/>

<table style="background-color:#ffffc0" cellpadding="8" width="95%" border="0"><tr><td>Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. [[User:Andrea Gorrell|Andrea Gorrell]].</td></tr>
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Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

2010-04-01T04:21:44Z

Laurel Koopmans:

Sandbox 171

2010-04-01T04:16:51Z

Laurel Koopmans:

Sandbox 171

2010-04-01T04:16:14Z

Laurel Koopmans:

Sandbox 171

2010-04-01T04:05:15Z

Laurel Koopmans:

Sandbox 171

2010-04-01T03:48:00Z

Laurel Koopmans:

Sandbox 171

2010-04-01T03:41:04Z

Laurel Koopmans:

Sandbox 171

2010-04-01T03:40:07Z

Laurel Koopmans:

File:Myosin chains.gif

2010-04-01T03:38:55Z

Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

2010-04-01T03:36:46Z

Laurel Koopmans:

Sandbox 171

2010-04-01T03:35:04Z

Laurel Koopmans:

File:Myosin head.gif

2010-04-01T03:34:08Z

Laurel Koopmans: uploaded a new version of "Image:Myosin head.gif"

File:Myosin head.gif

2010-04-01T03:33:06Z

Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

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Laurel Koopmans:

Sandbox 171

2010-03-27T00:25:32Z

Laurel Koopmans:

Sandbox 171

2010-03-27T00:19:51Z

Laurel Koopmans:

Sandbox 171

2010-03-27T00:04:59Z

Laurel Koopmans:

Sandbox 171

2010-03-26T23:54:56Z

Laurel Koopmans:

Sandbox 171

2010-03-26T23:48:22Z

Laurel Koopmans:

Sandbox 171

2010-03-23T01:36:27Z

Laurel Koopmans:

Sandbox 171

2010-03-23T01:21:28Z

Laurel Koopmans:

Sandbox 171

2010-03-23T01:03:11Z

Laurel Koopmans:

Sandbox 171

2010-02-02T00:05:03Z

Laurel Koopmans:

Sandbox 171

2010-02-01T23:58:08Z

Laurel Koopmans: