Arginine: Difference between revisions
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Arginine is one of the twenty [[Amino acids|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 [[Amino acids|amino acids]]. It is most commonly found in its stereotypical L-isomeric formation and is a polar, positively charged molecule. | ||
Due to the [[Molecule| | Due to the [[Molecule|molecule's]] 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>. | ||
Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. | Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. Its side chain contains a complex guanidinium cap on an aliphatic 3 carbon chain. Multiple [[Hydrogen_bonds|H-bonds]] are able to form due to the conjugation of [[double bond|double bonds]] and [[lone pair|lone pairs]] on the [[Nitrogen|nitrogen]] atoms. | ||
'''<u>References</u>''' | '''<u>References</u>''' | ||
<references /><br> | <references /><br> | ||
Revision as of 20:06, 7 December 2011
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 molecule's charge, it can sometimes be found located in the functional part of a protein conforming a pore[1].
Arginine displays basic properties in most basic, acidic and neutral environments due to the nature of its side chain or R-group. Its side chain contains a complex guanidinium cap on an aliphatic 3 carbon chain. Multiple H-bonds are able to form due to the conjugation of double bonds and lone pairs on the nitrogen atoms.
References
- ↑ The Biology Project,Department of Biochemistry and Molecular Biophysics, University of Arizona. 2003