Biological molecules Flashcards
Hydrogen bonds in water
- Oxygen attracts the electrons towards itself, becoming slightly negative
- The hydrogen molecules become slightly positive
- Hydrogen bonds form between slightly negative oxygens and slightly positive hydrogens
Hydrogen bonds and properties of water
- good solvent, as can interact with other polar/charged molecules due to hydrogen bonds
- cohesive, as hydrogen bonds stick water molecules together
- density: ice is less dense as hydrogen bonds form a lattice
- high specific heat capacity, as lots of energy is needed to raise the temperature of water
- liquid across a variety of temperatures
Importance of properties of water (6)
- good solvent: metabolic processes rely on chemical reactions occurring in solution
- liquid: good transport medium for transporting materials around organisms
- cohesive: creates surface tension as a habitat and prevents columns of water breaking
- freezing at lower density: water below is insulated (whole lake won’t freeze), provides a habitat
- thermal stability: large bodies of water have fairly constant temperatures, evaporation can cool surfaces
- metabolic: takes part in chemical processes
Structure of amino acids
H H O amino group (NH2)
N C C acid group (COOH)
H R OH R group
Forming peptide bonds
OH (from acid group) and H (from amino group) form water in a condensation reaction. End up with a peptide bond of: l C=O l N-H l
Breaking peptide bonds
Hydrolysis reaction. OH from water goes to C=O (bonds to carbon), H from water goes to N-H
Primary structure
The sequence of amino acids in a polypeptide/protein
Secondary structure
Coiling and pleating (alpha helix and beta pleated sheets) of parts of the polypeptide molecules. Held together by hydrogen bonds between carbon-nitrogen backbone (C=O—-H-N) not between R-groups.
Tertiary structure
Overall 3D structure of the final polypeptide/protein molecule. Held together by: disulfide bonds, ionic bonds, hydrogen bonds, hydrophobic and hydrophilic interactions. Hydrophobic R-groups will be held together with water excluded; hydrophilic groups will be on the outside
Quaternary structure
More than one polypeptide subunit joined together. Protein formed can’t function if not all subunits are present.
Haemoglobin as a protein
- 4 polypeptide subunits
- 1 prosthetic group on each chain: a haem group with Fe2+ ion
- Globular protein: vital tertiary structure
- Soluble in water
- Wide range of amino acids in primary structure
- Many alpha helix structures
Collagen molecule as a protein
- Fibrous protein
- Insoluble in water
- Not much variety in amino acids: 35% is glycine
- No prosthetic groups
- Many left-handed helix structures
Structure of collagen fibres
- Collagen molecules form staggered cross links with adjacent collagen molecules
- This makes collagen fibril
- Many fibrils together become collagen fibres.
Function of haemoglobin
Carry oxygen from lungs to tissues.
Function of collagen
Provide mechanical strength:
- in walls of arteries (no blood bursting from walls)
- tendons of collagen connecting skeletal muscle to bone (muscles can pull bones)
- makes up bones (with other stuff, e.g. calcium phosphate to harden them)
- Cartilage and connective tissue