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Contents 1 genetics is ok 2 'Molecules it Interacts With and where ' 3 'Origin' 4 'Structure' 5 'Molecules it Interacts With and where ' 6 'Origin' 7 'Structure' 8 'Function" 9 References

genetics is ok

'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

'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.

which play a crucial role in binding to the ribosome during translation.

'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.

spinqualitylabelsall models Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Heterodimer </scene> 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 '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. which play a crucial role in binding to the ribosome during translation.

Zach and Rohith's molecule page.

Our molecule is 1aoi.

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Introduction:

This is a core component of the nucleosome. The nucleosome is the basic packaging unit of DNA. It consists of histone proteins and DNA wrapped around it. A typical nucleosome has an octamer of eight histone proteins that are in contact with a 146 bp long DNA fragment. When the chromatin needs to be more condensed, the nucleosomes fold onto themselves to create a tightly packed structure.

References