Arginine: Difference between revisions

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<u>'''Abreviation'''</u>'''&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;'''<u>'''Single Letter Code'''</u>
<u>'''Abreviation'''</u>'''&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;'''<u>'''Single Letter Code'''</u>  


Arg&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; R
Arg&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; R


<u</u>
<u>'''Infomation'''</u>  


<u>'''Infomation'''</u>
Arginine is one of the twenty&nbsp;amino acids. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule.


Arginine is one of the twenty&nbsp;amino acids. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule.
<br>


Due to the molecules charge it can sometimes be found located in the functional part of a protein conforming a pore.


 
'''<u>References</u>'''  
Due to the molecules charge it can sometimes be found located in the functional part of a protein conforming a pore.
 
'''<u>References</u>'''


The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003&nbsp;<br>
The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003&nbsp;<br>

Revision as of 11:42, 11 November 2010

Abreviation               Single Letter Code

Arg                             R

Infomation

Arginine is one of the twenty amino acids. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule.


Due to the molecules charge it can sometimes be found located in the functional part of a protein conforming a pore.

References

The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003 

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