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4 Cards in this Set
- Front
- Back
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isoelectric point (pI)
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net charge (algebraic sum of all charged groups) of an amino acid or protein is zero
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disulfide bond
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The primary alcohol of serine and threonine as well as the thiol (–SH) of cysteine allow these amino acids to act as nucleophiles during enzymatic catalysis. Additionally, the thiol of cysteine is able to form a disulfide bond with other cysteines:
Cysteine-SH + HS-Cysteine <——> Cysteine-S-S-Cysteine This simple disulfide is identified as cystine. The formation of disulfide bonds between cysteines present within proteins is important to the formation of active structural domains in a large number of proteins. Disulfide bonding between cysteines in different polypeptide chains of oligomeric proteins plays a crucial role in ordering the structure of complex proteins, e.g. the insulin receptor. |
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dipeptide
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two peptides joined by peptide bond formed in condensation reaction of carboxyl group with amino group with concomitant elimination of water.
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carbohydrates
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carbon compounds with lots of hydroxyl groups
classified as oligo, mono, or polysaccharides |
