CLASSIFICATION OF PROTEINS.

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CLASSIFICATION OF PROTEINS

Functions / impotance of Proteins Type Examples Structural tendons, cartilage, hair, nails Contractile muscles Transport hemoglobin, albumin Storage ferritin Hormonal eg. insulin, growth hormone Enzyme eg. hydroxylases Protection immunoglobulins Energy 4.1 k.cal/gm

Peptide bond In proteins, amino acids are joined covalently by peptide bonds, which are amide linkages between the á-carboxyl group of one amino acid and the á-amino group of another. For example, valine and alanine can form the dipeptide valylalanine through the formation of a peptide bond. Peptide bonds are not broken by conditions that denature proteins, such as heating or high concentrations of urea

PEPTIDES AND PROTEINS Oligopeptide :a few amino acids ≤ 100 Carboxyl terminal- C-terminal Amino terminal- N-terminal- Oligopeptide :a few amino acids ≤ 100 Polypeptide : many amino acids ≥ 100

TETRAPEPTIDE Acid-base behavior of a peptide: N-terminal, C-terminal, R-groups 2. Peptides have a characteristic titration curve and a characteristic pI value

Characteristics of the peptide bond: The peptide bond has a partial double-bond character, that is, it is shorter than a single bond, and is rigid and planar . This prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond. However, the bonds between the á-carbons and the á-amino or á-carboxyl groups can be freely rotated (although they are limited by the size and character of the R-groups). This allows the polypeptide chain to assume a variety of possible configurations..