Proteopedia - User contributions [en]

Sandbox Reserved 1001

2015-02-07T06:57:58Z

Anna Lohning:

{{Sandbox_Reserved_Anna_Lohning_1}}
==Your Heading Here (maybe something like 'Structure of Human Hexokinase')==
<StructureSection load='2nzt' size='340' side='right' caption='This is human hexokinase II' scene=''>
This is some default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. (Think of these as bookends enclosing important functionality, as in HTML)
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Introduction ==
You can include here details about your protein. Its a good idea to start the page with an image already loaded. Then include some green links (molecular scenes) to change the image.
== Disease if relevant ==

== Structural highlights ==

This is a sample scene created with Scene Authoring Tools (SAT) to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
Simply click on the 'show' button below while in edit mode. Go to Editing Help for assistance. There are also some great videos to watch on how to create special features.

The most important thing in this section is that you explain some structural detail about how your protein functions and link this to its structure as visually as possible. Zooming in on individual amino acids for example.
Good luck and have fun!

</StructureSection>
== References ==
<references/>

Sandbox Reserved 1001

2015-02-06T20:09:17Z

Anna Lohning:

Sandbox Reserved Anna Lohning 1

2015-02-06T20:02:51Z

Anna Lohning:

{| style="background-color:#ffffe0;" border="1" cellpadding="5"
| This Sandbox is Reserved from February 10 to April 30, 2015 for use in a Medical Biochemistry Course assignment taught by [[User:Anna Lohning|Anna Lohning]] at Bond University of Gold Coast, QLD, Australia. This reservation includes '''Sandbox Reserved 1001''' through '''Sandbox Reserved 1050'''.
|-
| To get started:
* Click the ''edit this page'' tab at the top. Save the page after each step, then edit it again.
* Click the '''3D''' button (when editing, above the wikitext box) to insert Jmol.
* '''show''' the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
* Add a description of your scene. Use the buttons above the wikitext box for''' bold''', ''italics'', [[#|links]], <big><big>headlines</big></big>, etc.
More help: [[Help:Editing]]
|}

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved Anna Lohning 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved Anna Lohning 1

2015-02-06T04:07:57Z

Anna Lohning:

{| style="background-color:#ffffe0;" border="1" cellpadding="5"
| This Sandbox is Reserved from February 10 to April 30, 2015 for use in a Medical Biochemistry Course assignment taught by [[User:Anna Lohning|Anna Lohning]] at Bond University of Gold Coast, QLD, Australia. This reservation includes '''Sandbox Reserved 101''' through '''Sandbox Reserved 150'''.
|-
| To get started:
* Click the ''edit this page'' tab at the top. Save the page after each step, then edit it again.
* Click the '''3D''' button (when editing, above the wikitext box) to insert Jmol.
* '''show''' the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
* Add a description of your scene. Use the buttons above the wikitext box for''' bold''', ''italics'', [[#|links]], <big><big>headlines</big></big>, etc.
More help: [[Help:Editing]]
|}

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved Anna Lohning 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Template:Sandbox Reserved Anna Lohning 1

2015-02-06T03:51:13Z

Anna Lohning: New page: {| style="background-color:#ffffe0;" border="1" cellpadding="5" | This Sandbox is Reserved from February 6 - April 15th, 2015 for use in a Medical Biochemistry assignment taught by [[User:...

{| style="background-color:#ffffe0;" border="1" cellpadding="5"
| This Sandbox is Reserved from February 6 - April 15th, 2015 for use in a Medical Biochemistry assignment taught by [[User:Anna Lohning|Anna Lohning]] at Bond University, Gold Coast QLD Australia. This reservation includes '''Sandbox Reserved 101''' through '''Sandbox Reserved 150'''.
|-
| To get started:
* Click the ''edit this page'' tab at the top. Save the page after each step, then edit it again.
* Click the '''3D''' button (when editing, above the wikitext box) to insert Jmol.
* '''show''' the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
* Add a description of your scene. Use the buttons above the wikitext box for''' bold''', ''italics'', [[#|links]], <big><big>headlines</big></big>, etc.
More help: [[Help:Editing]]
|}

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved Anna Lohning 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Sandbox Reserved Anna Lohning 1

2015-02-06T03:44:09Z

Anna Lohning: New page: {| style="background-color:#ffffe0;" border="1" cellpadding="5" | This Sandbox is Reserved from February 6 to April 15, 2015 for use in a Medical Biochemistry Course assignment taught by [...

{| style="background-color:#ffffe0;" border="1" cellpadding="5"
| This Sandbox is Reserved from February 6 to April 15, 2015 for use in a Medical Biochemistry Course assignment taught by [[User:Lynmarie K Thompson|Lynmarie Thompson]] at Bond University of Gold Coast, QLD, Australia. This reservation includes '''Sandbox Reserved 101''' through '''Sandbox Reserved 150'''. 
|-
| To get started:
* Click the ''edit this page'' tab at the top. Save the page after each step, then edit it again.
* Click the '''3D''' button (when editing, above the wikitext box) to insert Jmol.
* '''show''' the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
* Add a description of your scene. Use the buttons above the wikitext box for''' bold''', ''italics'', [[#|links]], <big><big>headlines</big></big>, etc.
More help: [[Help:Editing]]
|}

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox Reserved Anna Lohning 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Elizeu/sandbox/citocromo c

2015-02-04T09:42:48Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==

<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb'/>
<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-02-04T09:42:23Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
{{55/559112/Oxyhb/1/55/559112/A_chain_haeme/1/1 }}
== Introduction ==

<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-02-04T09:41:56Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb'/>

<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-02-04T09:41:05Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
{{55/559112/Oxyhb/1/55/559112/A_chain_haeme/1/1 }}
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb'/>

<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-01-23T02:02:59Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
<scene name='55/559112/Oxyhb/1'>Haemoglobin</scene> is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-01-23T02:02:05Z

Anna Lohning: OxyHb

==The Structure Function Relationship of Haemoglobin==
<scene name='55/559112/Oxyhb/1'>TextToBeDisplayed</scene>
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-01-21T23:04:38Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical α subunits and 2 identical β subunits. The strongest inter-subunit interactions exist between the α and β subunits so Hb could be considered to be a dimer of α/β subunits. The α subunits have 141 residues while β subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

The key to Hb's success is conformational changes which increase or decrease its affinity for O2. Hb exists in 2 main conformations, the relaxed, R-state (oxyHb) and the tense. T-state (deoxyHb).
What factors induce this change in conformation? Hb exploits the changes in its environment, such as pH, CO2 and 2,3-BPG. These small molecules are called allosteric effectors because they bind to Hb at sites away from the O2 binding site and effect a change in conformation of Hb.

Elizeu/sandbox/citocromo c

2015-01-21T22:56:42Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical &alpha subunits and 2 identical &beta subunits. The strongest inter-subunit interactions exist between the &alpha and &beta subunits so Hb could be considered to be a dimer of &alpha/&beta subunits. The α subunits have 141 residues while &beta subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T22:54:54Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing O2 to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
Haemoglobin (Hb) consists of 2 identical &alpha subunits and 2 identical &beta subunits. The strongest inter-subunit interactions exist between the &alpha and &beta subunits so Hb could be considered to be a dimer of &alpha/&beta subunits. The &alpha subunits have 141 residues while &beta subunits have 146 residues. Each monomer contains a haeme prosthetic group facilitating O2 coordination.

On the right is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T09:08:03Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.
This is <scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.

== Exploring the Structure ==
[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T09:06:59Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.
This is oxyhaemoglobin. Embedded in each monomer is the haeme prosthetic group with bound (ferrous) iron. Iron makes 6 coordination bonds. Four in the plane of the haeme to 4 nitrogens (blue); one to the proximal Histidine imidizole nitrogen and one reserved for oxygen.
<scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>
== Exploring the Structure ==
[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T08:52:31Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
<scene name='55/559112/A_chain_haeme/1'>OxyHaemoglobin</scene>
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T08:51:05Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
<scene name='55/559112/A_chain_haeme/1'>TextToBeDisplayed</scene>
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T08:29:30Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==
[[Image:oxyHb.png]]

Elizeu/sandbox/citocromo c

2015-01-21T08:29:04Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
[[Image:oxyHb.png]]
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==

Elizeu/sandbox/citocromo c

2015-01-21T08:27:59Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
[[Image:oxyhaemoglobin.pdb]]
== Introduction ==
<Structure load='Oxyhaemoglobin.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==

Elizeu/sandbox/citocromo c

2015-01-21T08:27:02Z

Anna Lohning:

Elizeu/sandbox/citocromo c

2015-01-21T08:14:09Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==
[[Image:oxyHb.png]]
== Introduction ==
<Structure load='1hho_mm1.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==

Elizeu/sandbox/citocromo c

2015-01-21T08:13:47Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

<Structure load='1hho.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
[[Image:oxyHb.png]]
== Introduction ==
<Structure load='1hho_mm1.pdb' size='350' frame='true' align='right' caption='OxyHb='Insert optional scene name here' />
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==

Elizeu/sandbox/citocromo c

2015-01-21T08:11:30Z

Anna Lohning:

==The Structure Function Relationship of Haemoglobin==

<Structure load='1hho.pdb' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
[[Image:oxyHb.png]]
== Introduction ==
Haemoglobin is a tetrameric globular protein able to transport small molecules such as oxygen and carbon dioxide around the body to support life. Its a great example of how a protein's binding affinity to its ligand can change in response to changes in its environment. This is facilitated by small conformational changes that occur in and between subunits in a cooperative manner ultimately allowing oxygen to be picked up in the lungs and delivered to the tissues.

== Exploring the Structure ==

Elizeu/sandbox/citocromo c

2015-01-21T08:06:45Z

Anna Lohning:

File:OxyHb.pdb

2015-01-21T07:58:34Z

Anna Lohning:

Elizeu/sandbox/citocromo c

2015-01-21T07:57:35Z

Anna Lohning: The Structure Function Relationship of Haemoglobin

==The Structure Function Relationship of Haemoglobin)==

== Introduction ==

== Exploring the Structure ==

File:Oxyhaemoglobin.pdb

2015-01-21T07:50:24Z

Anna Lohning: Oxyhaemoglobin (OxyHb)

Oxyhaemoglobin (OxyHb)