Focus on protein structure and its importance in food and biology.
Protein affects: solubility, elasticity, emulsifiers, and texture.
Chemically, proteins are polymers with repeating biological units.
Example of a polymer: Styrene leading to polystyrene.
A biopolymer has similar repeating units that are biological.
Amino acids form peptides (short chains) and ultimately proteins (polypeptides).
Primary structure: linear sequence of amino acids connected by covalent bonds.
Secondary structure: larger components formed by hydrogen bonds, including beta sheets and alpha helices.
Tertiary structure: overarching shape of a single protein molecule.
Quaternary structure: assembly of multiple protein molecules into a larger unit (e.g., enzymes, ribosomes).
Amino acids connected through condensation reactions, forming peptide bonds.
Peptide bond formation: carboxylic acid + amine, losing water; reversible through hydrolysis.
Peptide bonds exhibit resonance structures, contributing to rigidity.
Peptide bond characteristics: partial double bond prevents free rotation, affecting hydrogen bonding capability.
Comparison of various amino acids:
Glycine (simplest), hydrophilic (OH groups), charged (acidic/basics), aliphatic (hydrophobic), and aromatic (not water-friendly).
Interactions between amino acids affect their placement in proteins based on charge and hydrophilicity.
Representation of amino acids: full names, three-letter codes, one-letter codes.
Examples of one-letter codes: A (Alanine), D (Aspartic acid), K (Lysine), L (Leucine), R (Arginine), E (Glutamic acid), G (Glycine), Q (Glutamine).
Protein sequences represented from N-terminus to C-terminus (amino end to acid end).
Example of protein variant: beta-casein in milk (A1 vs A2 variant) showing importance of single amino acid changes.
Impact of mutations (e.g., coronavirus variant D614G) on protein functionality and transmission efficiency.
A small difference in amino acids can lead to significant physiological effects.