Proteopedia - User contributions [en]

User:Ben Solis-Cohen

2012-04-11T15:55:51Z

Ben Solis-Cohen:

I worked the the Fieldston Smart Team on creating a model and presentation on an E-Coli clc Channel. Mr. Cairo, a chemistry teacher at Fieldston, supervised us and Dr. Alessio Accardi, a scientist researching the channel, helped us as well. We are going to publish a page on the protein and have most of the information ready to go. We are also well versed in its functions and structure as well as several experiments done using it.

User:Ben Solis-Cohen

2012-04-11T15:55:01Z

Ben Solis-Cohen:

I worked the the Fieldston Smart Team on creating a model and presentation on an E-Coli clc Channel. Mr. Cairo, a chemistry teacher at Fieldston, supervised us and Dr. Alessio Accardi, a scientist researching the channel, helped us as well. We are going to publish a page on the protein and have most of the information ready to go. We are also well versed in its func<Structure load='Insert PDB code or filename here' size='500' frame='true' align='right' caption=’THREE DIMENSIONS 0000000000' scene='Insert optional scene name here' />tions and structure as well as several experiments done using it.

Sandboxjg

2011-08-31T17:15:08Z

Ben Solis-Cohen: /* ClC Transporter */

==ClC Transporter ==

<Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' />
The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential for the maintenance of proper membrane potential in muscle cells and some neurons, for the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.

Roderick MacKinnon and his team determined the structure of the protein and concluded that it was an ion channel. Accardi and Miller established that the protein also functioned as a transporter, by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.

The CLC-ec1 transporter is a protein dimer made up of two independently functioning anti-parallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helical dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore.

Each pore has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>Glu 148</scene> functions as a gate to mediate the transport of chloride ions into and out of the protein, and the other <scene name='Sandboxjg/Glu_203/1’>Glu 203</scene> is thought to be involved in hydrogen ion selectivity. There are 3 chloride binding sites in each channel, an exterior binding site, a central binding site, and an interior binding site. When the protein is inactive Glu 148 occupies the exterior binding site. When the protein is active Glu 148 leaves the site and allows ion exchange to occur.

One of the interesting properties of this protein is that it can function as either a channel or a transporter. For instance, with certain mutations concerning the Glu 148,hydrogen ion activity is impaired, but chloride ions can still move freely through the protein. Other mutations can have the potential to cause diseases like cystic fibrosis, myotonia congenita, epilepsy, and others.
To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene>

Sandboxjg

2011-08-31T17:06:17Z

Ben Solis-Cohen: /* ClC Transporter */

==ClC Transporter ==

<Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' />
The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential for the maintenance of proper membrane potential in muscle cells and some neurons, for the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.

Roderick MacKinnon and his team determined the structure of the protein and concluded that it was an ion channel. Accardi and Miller established that the protein also functioned as a transporter, by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.

The CLC-ec1 transporter is a protein dimer made up of two independently functioning anti-parallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helical dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore.

Each pore has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>Glu 148</scene> functions as a gate to mediate the transport of chloride ions into and out of the protein, and the other (Glu 203) is thought to be involved in hydrogen ion selectivity. There are 3 chloride binding sites in each channel, an exterior binding site, a central binding site, and an interior binding site. When the protein is inactive Glu 148 occupies the exterior binding site. When the protein is active Glu 148 leaves the site and allows ion exchange to occur.

One of the interesting properties of this protein is that it can function as either a channel or a transporter. For instance, with certain mutations concerning the Glu 148,hydrogen ion activity is impaired, but chloride ions can still move freely through the protein. Other mutations can have the potential to cause diseases like cystic fibrosis, myotonia congenita, epilepsy, and others.
To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene>

Sandboxjg

2011-08-31T17:04:24Z

Ben Solis-Cohen: /* ClC Transporter */

==ClC Transporter ==

<Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' />
The <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a transmembrane voltage-gated CLC transporter found in Eschrecheria Coli. It is essential for the maintenance of proper membrane potential in muscle cells and some neurons, for the transportion of electrolytes across epithelial layers, and in maintaining proper cell volume.

Roderick MacKinnon and his team determined the structure of the protein and concluded that it was an ion channel. Accardi and Miller established that the protein also functioned as a transporter, by means of a 2:1 chloride ion-hydrogen ion exchange mechanism.

The CLC-ec1 transporter is a protein dimer made up of two independently functioning anti-parallel polypeptide chains. The chains extend from the inside to the outside of the plasma membrane creating a passage. Its structure allows it to use electrostatic interactions with alpha-helical dipoles and chemical groups coordinated with nitrogen atoms and carboxyl groups in order to filter Cl- and H+ ions. Because each polypeptide chain functions independently, we will focus on the structure of one pore.

Each pore has two essential glutamate residues: one <scene name='Sandboxjg/Glu_148/1’>(Glu 148)</scene> functions as a gate to mediate the transport of chloride ions into and out of the protein, and the other (Glu 203) is thought to be involved in hydrogen ion selectivity. There are 3 chloride binding sites in each channel, an exterior binding site, a central binding site, and an interior binding site. When the protein is inactive Glu 148 occupies the exterior binding site. When the protein is active Glu 148 leaves the site and allows ion exchange to occur.

One of the interesting properties of this protein is that it can function as either a channel or a transporter. For instance, with certain mutations concerning the Glu 148,hydrogen ion activity is impaired, but chloride ions can still move freely through the protein. Other mutations can have the potential to cause diseases like cystic fibrosis, myotonia congenita, epilepsy, and others.
To see the test <scene name='Sandboxjg/Test1ots/1'>click on me</scene>

File:Alteredotswithchanges.pdb

2011-08-31T16:13:16Z

Ben Solis-Cohen:

== Licensing ==
{{subst:No license from license selector|Don't know}}

Sandboxhr

2011-06-09T19:46:41Z

Ben Solis-Cohen:

==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 it goes.

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_1ots | PDB=1ots | SCENE= }}

Sandboxhr

2011-06-09T19:45:45Z

Ben Solis-Cohen: 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...

File:1OTS.pdb

2011-06-09T19:38:50Z

Ben Solis-Cohen: