Unit 4: Amino Acids and Proteins

Table of Contents

Amino Acids: Structure and Properties

Amino acids are the monomers (building blocks) of proteins. There are 20 standard amino acids used to build proteins in humans.

General Structure

Every amino acid has a central alpha-carbon (α-carbon) bonded to four different groups:

  1. A Hydrogen Atom (H)
  2. An Amino Group (-NH2), which is basic.
  3. A Carboxyl Group (-COOH), which is acidic.
  4. A Side Chain (R-group), which is different for every amino acid and determines its properties.

Chemical Properties

Classification

Amino acids are classified based on the properties of their R-group.

Class Property of R-group Examples
Nonpolar, Aliphatic Hydrocarbon chains (hydrophobic) Glycine, Alanine, Valine, Leucine, Isoleucine
Polar, Uncharged Contains an -OH or -SH group (hydrophilic) Serine, Threonine, Cysteine, Glutamine
Aromatic Contains a ring structure (mostly hydrophobic) Phenylalanine, Tyrosine, Tryptophan
Acidic (Negatively Charged) Contains a second -COOH group (hydrophilic) Aspartate (Aspartic Acid), Glutamate (Glutamic Acid)
Basic (Positively Charged) Contains a second amino group (hydrophilic) Lysine, Arginine, Histidine
Exam Tip: You must know the essential amino acids. These are the ones the human body cannot synthesize and must be obtained from the diet.
Mnemonic: PVT TIM HALL (Phenylalanine, Valine, Threonine, Tryptophan, Isoleucine, Methionine, Histidine, Arginine*, Leucine, Lysine). *Arginine is semi-essential.

Proteins: Structure and Function

Proteins are large, complex polymers of amino acids linked together. They perform almost all functions in a cell.

The Peptide Bond

Levels of Protein Structure

A protein's function depends on its unique 3D shape, which is described in four levels:

  1. Primary (1°) Structure:
    • Definition: The unique sequence (order) of amino acids in the polypeptide chain.
    • Example: ...-Ala-Gly-Leu-Val-...
    • Stabilized by: Peptide bonds (strong covalent bonds).
  2. Secondary (2°) Structure:
    • Definition: Local, repeating folding patterns of the polypeptide backbone.
    • Examples: The α-helix (a coil) and the β-pleated sheet (folded strands).
    • Stabilized by: Hydrogen bonds between the C=O and N-H groups of the backbone (not the R-groups).
  3. Tertiary (3°) Structure:
    • Definition: The overall 3D folding of a single polypeptide chain, bringing distant R-groups together.
    • This is the final, functional shape for many proteins.
  4. Quaternary (4°) Structure:
    • Definition: The assembly of two or more separate polypeptide chains (subunits) to form a larger, functional protein complex.
    • Example: Hemoglobin is made of four subunits (two alpha, two beta).

Stabilizing Bonds in Protein Structure

The Tertiary (and Quaternary) structures are stabilized by several types of interactions, all involving the R-groups:

Carbohydrates

Carbohydrates are biomolecules consisting of carbon, hydrogen, and oxygen, usually with a hydrogen-oxygen ratio of 2:1 (like water, Cn(H2O)n). They are the primary energy source for most organisms.

Structure, Properties, and Function of Monosaccharides

Disaccharides and Polysaccharides