Biological Molecules Flashcards
Macronutrient
Organic compounds required in large amounts
- Proteins
- Lipids
- Carbohydrates
Protein
An organic macromolecule essential to life.
Formed from one or more polypeptides
Enzymes
Globular proteins that act as biological catalysts to increase the rate of reactions
Uses of protein
Enzymes which catalyse chemical reactions
- Forming muscle, bone and other structural features
- Emergency energy source
Elements in protein
- Carbon
- Hydrogen
- Oxygen
- Nitrogen
- Other elements like iron and sulphur
Condensation reaction
When 2 molecules join together, with water as a byproduct
Hydrolysis reaction
When 2 molecules break apart when water is added
Bonding of protein
- Peptide bonds between amino acids
- Regular covalent bonds within the amino acid
- Ionic, hydrogen, disulfide, or hydrophobic bonds on secondary and tertiary levels
Hydrogen bond
A weak interaction between a negative ion and a positive hydrogen atom
Covalent bond
A strong interaction resulting in the sharing of electrons in the outer shell.
E.g. disulfide, phosphodiester, peptide, glycosidic
Cyclic form
The shape formed by a molecule where the final atom is attached to the first
Straight line form
The shape formed by a molecule where all the atoms are in a line
Amino acid
A monomer of proteins with 20 different types
- Amphoteric and a buffer
- Composed of the same basic structure, but with a unique R group
Amphoteric
A compound that is able to react with both bases and acids.
E.g. Amino acids, water, hydrogen carbonate ions
Peptide bond
A strong chemical bond between two amino acids, formed through a condensation reaction.
- When aqueous, the amino group goes from NH₂ to NH₃⁺ (+H⁺)
- The Carboxyl group goes from COOH to COO⁻ (-H⁺)
- The carboxyl and amino acids then bind, with water as a byproduct
Amino acid structure
- Hydrogen group
- Amino group
- Carboxyl group
- R group / side chain
Carboxyl group
- COOH
- Acidic
- Found in single bonded monosaccharides
- Found in amino acids
Dipeptide
Two amino acids that have combined together with a condensation reaction between the amino and carboxyl groups, resulting in the release of water
Polypeptide
A chain of multiple amino acids
Primary structure
The order of amino acids in a protein.
Has peptide bonds between amino and carboxyl groups
Secondary structure
When chains of amino acids coil or fold
36 amino acids per 10 turns
- Two different types: α-helix, β-pleated sheet
- Lots of hydrogen bonds between -NH group and -CO group further down the chain
- Stable at optimal temperatures
Alpha helix
A form of secondary structure of amino acids where the amino acids that bind are 4 places apart. Resulting in a twirl shape
Beta pleated shee
A form of secondary structure where a zig-zag structure is formed as the chains folds over itself
Tertiary structure
When coiled chains of amino acids are folded into precise shapes, usually either supercoiled or spherical.
Mostly exhibited in globular proteins, with fibrous proteins often stopping at secondary structure
- Variety of bonds, including ionic, hydrogen,hydrophilic, hydrophobic, disulfide