Histidine

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Histidine (commonly abbreviated to His or H) <ref>^ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic and Biochemical Nomenclature, Symbols and Terminology etc. Retrieved 2007-05-17.</ref> &nbsp;is one of the twenty naturally-occurring [[Amino acids|amino acids]]. Of these amino acids it is one of ten [[Polarity|polar]] and one of three positively-charged amino acids&nbsp;<ref name="Amino Acid Chart">http://www.detectingdesign.com/images/Abiogenesis/Amino%20Acid%20Chart.jpg</ref>. &nbsp;The [[Codon|codons]] of His are CAU or CAC.&nbsp;  
 
Histidine (commonly abbreviated to His or H) <ref>^ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic and Biochemical Nomenclature, Symbols and Terminology etc. Retrieved 2007-05-17.</ref> &nbsp;is one of the twenty naturally-occurring [[Amino acids|amino acids]]. Of these amino acids it is one of ten [[Polarity|polar]] and one of three positively-charged amino acids&nbsp;<ref name="Amino Acid Chart">http://www.detectingdesign.com/images/Abiogenesis/Amino%20Acid%20Chart.jpg</ref>. &nbsp;The [[Codon|codons]] of His are CAU or CAC.&nbsp;  
  
Histidine is an [[Aromatic_ring|aromatic]] amino acid, which acts as an [[acid|acid]] when [[Proton|protonated]]. When unprotonated it has a positively charged [[imidazole|imidazole]] functional group and acts as a general base. It plays an important role in stabilising the folding structures of proteins and active sites of [[enzymes|enzymes]] <ref>http://www.biology.arizona.edu/biochemistry/problem_sets/aa/histidine.html</ref> . This ability is due to its binding properties with metals and the basic properties of the nitrogen [[atoms|atoms]] in the ring. It is only found as an L- isomer and it plays an important role in growth and repair of tissues in the body.  
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Histidine is an [[Aromatic ring|aromatic]] amino acid, which acts as an [[Acid|acid]] when [[Proton|protonated]]. When unprotonated it has a positively charged [[Imidazole|imidazole]] functional group and acts as a general base. It plays an important role in stabilising the folding structures of proteins and active sites of [[Enzymes|enzymes]] <ref>http://www.biology.arizona.edu/biochemistry/problem_sets/aa/histidine.html</ref> . This ability is due to its binding properties with metals and the basic properties of the nitrogen [[Atoms|atoms]] in the ring. It is only found as an [[L-isomer|L-isomer]] and it plays an important role in growth and repair of tissues in the body<ref>Berg, J. M., Tymoczko, J. L., &amp; Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.</ref>.  
  
[[Image:Histidine.png]]
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[[Image:Histidine.png]]  
  
 
=== References  ===
 
=== References  ===
  
Berg, J. M., Tymoczko, J. L., &amp; Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.<br>
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<references /><br>

Latest revision as of 03:38, 30 November 2013

Histidine (commonly abbreviated to His or H) [1]  is one of the twenty naturally-occurring amino acids. Of these amino acids it is one of ten polar and one of three positively-charged amino acids [2].  The codons of His are CAU or CAC. 

Histidine is an aromatic amino acid, which acts as an acid when protonated. When unprotonated it has a positively charged imidazole functional group and acts as a general base. It plays an important role in stabilising the folding structures of proteins and active sites of enzymes [3] . This ability is due to its binding properties with metals and the basic properties of the nitrogen atoms in the ring. It is only found as an L-isomer and it plays an important role in growth and repair of tissues in the body[4].

Histidine.png

References

  1. ^ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature. "Nomenclature and Symbolism for Amino Acids and Peptides". Recommendations on Organic and Biochemical Nomenclature, Symbols and Terminology etc. Retrieved 2007-05-17.
  2. http://www.detectingdesign.com/images/Abiogenesis/Amino%20Acid%20Chart.jpg
  3. http://www.biology.arizona.edu/biochemistry/problem_sets/aa/histidine.html
  4. Berg, J. M., Tymoczko, J. L., & Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman.

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