Peptide bonds: Difference between revisions
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A peptide bond is a kind of linkage between two amino acids. It is also known as an amide bond. A peptide bond connects two amino acids, forming a dipeptide, and is associated with the loss of a water molecule. This process is called a condensation reaction. One perhaps surprising fact about peptide bonds is that they are very kinetically stable, in fact a peptide bond in a solution will last 1000 years, if no catalyst is present to disrupt it. <ref> | A peptide bond is a kind of linkage between two amino acids. It is also known as an amide bond. A peptide bond connects two amino acids, forming a dipeptide, and is associated with the loss of a water molecule. This process is called a condensation reaction. One perhaps surprising fact about peptide bonds is that they are very kinetically stable, in fact a peptide bond in a solution will last 1000 years, if no catalyst is present to disrupt it. <ref>Berg, Tymoczko, Stryer, Biochemistry 6th ed, W.H. Freeman and Company, 2007</ref> | ||
Many amino acids can be connected via peptide bonds, making a polypeptide. Each amino acid is then called a residue as it forms part of the polypeptide. | Many amino acids can be connected via peptide bonds, making a polypeptide. Each amino acid is then called a residue as it forms part of the polypeptide. | ||
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Revision as of 19:54, 6 January 2011
A peptide bond is a kind of linkage between two amino acids. It is also known as an amide bond. A peptide bond connects two amino acids, forming a dipeptide, and is associated with the loss of a water molecule. This process is called a condensation reaction. One perhaps surprising fact about peptide bonds is that they are very kinetically stable, in fact a peptide bond in a solution will last 1000 years, if no catalyst is present to disrupt it. [1]
Many amino acids can be connected via peptide bonds, making a polypeptide. Each amino acid is then called a residue as it forms part of the polypeptide.
- ↑ Berg, Tymoczko, Stryer, Biochemistry 6th ed, W.H. Freeman and Company, 2007