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&nbsp;
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&nbsp;  


<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|amino acids]]. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule.  


<br>
Due to the [[Molecule|molecules]] charge it can sometimes be found located in the functional part of a [[Proteins|protein]] conforming a pore<ref>The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003</ref>.


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


'''<u>References</u>'''
=== <references /><br> ===
 
The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003&nbsp;<br>

Revision as of 12:24, 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[1].

References

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