SandboxGenetic322-5

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Abby Mandelblatt
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== Function ==
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<Structure load='Image:Lactase.jpeg' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
 
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This is a Sandbox page that you can use for creating our discussion project.
 
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I would like for you to watch the short training videos. Each is short and you can view them all in about 40 mins. These provide the basic knowledge you will need to our discussion sections.
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The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.
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I need you to get some basic familiarity with this package so you will be able to help students.
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<Structure load='1ttt' size='350' frame='true' align='right' caption='Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex' />
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Our first three discussions will focus on 'structure'. Structure of DNA, proteins, and RNA.
 
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The students will work in 2 person teams and will create a Proteopedia page on their assigned molecule and will be asked to research their molecule and create 'scenes' which are representations of the molecule that illustrates some key features.
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== Molecules it Interacts With and where ==
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There will be a work sheet the students will follow to help them through the project.
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The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
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One of the objectives is to have the students manipulate structures to appreciate the 3 dimensional nature of the molecules we are discussing and to begin to help them conceptualize how these molecule might interact etc.
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''PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER''
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''PHENYLALANINE''
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''MAGNESIUM ION''
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=='Origin'==
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It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant ''Thermus aquaticus'' (EF-Tu elongation factor, and can be synthetically manufactured.
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=='Structure'==
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It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in <scene name='75/751161/Hetero_domains/1'>Heterodimer </scene> alignment.
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Specific <scene name='75/751161/Ligand_site/1'>Ligand Sites</scene> are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.
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<scene name='75/751161/Basic_positive_residues/2'>Basic and Positive Residues</scene> which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.
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=='Molecules it Interacts With and where '==
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The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.
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''PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER''
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''PHENYLALANINE''
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''MAGNESIUM ION''

Current revision

Contents

Function

The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.

Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex

Drag the structure with the mouse to rotate


Molecules it Interacts With and where

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION


'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.


'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.


Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.

which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION

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