F212 Biological Molecules Flashcards
Water
Polar Molecule
There is a slight positive charge (from the hydrogen nuclei) on the hydrogen atoms in a water molecule
There is a slight negative charge (from the electrons around the oxygen) on the oxygen atom in a water molecule
Water
Molecule
H2O
Each hydrogen atom shares its electron with the outer shell of the oxygen atom which stabilises the oxygen
Water
Intermolecular Hydrogen Bonds
Hydrogen bonds occur between the negatively charged oxygen atom of one molecule and the positively charged hydrogen atom of another molecule
Water
Liquid at Room Temperature
The intermolecular bonds between water molecules at room temperature hold the molecules together making water a liquid at room temperature rather than a gas
This allows water to act as a liquid transport medium in living things
E.g. blood in animals, the vascular system in plants
Water
Solvent
As water is a polar molecule it is a good solvent for other polar molecules and ionic compounds
When the attraction of the water is stronger than the intramolecular forces of the solute then the solute will be pulled apart e.g. ionic compound
In a polar molecule the charged parts of the water surround the charged parts of the solute separating the molecules and keeping them dissolved
Metabolic processes in all living organisms rely on chemicals being able to react in solution
Water
Thermal Stability
The hydrogen bonds between water mean that a relatively large amount of energy is required to increase the temperature
Large bodies of water provide fairly stable environments
Makes evaporation of sweat a very effective cooling mechanism
Water
Cohesion
Water molecules stick together because of the intramolecular hydrogen bonds, it also causes surface tension
Transport of water in the xylem relies on water molecules sticking to each other as they are transported up the xylem in the transpiration system
Water
Chemical Reactions
Waters thermal stability and solvent properties make it an ideal environment for chemical reactions
Water is also a reactant e.g. hydrolysis reactions and photosynthesis
Hydrophobic
Water repelling
Hydrophilic
Associates easily with water molecules
Proteins
Function
Structure Transport Enzymes Antibodies Most hormones
Proteins
Monomer
Amino Acids
Proteins
Polymer
Polypeptides
Amino Acid
Structure
Amine group H-N-H
|
Residual R-C-H
|
Carboxylic Acid group O=C-OH
Breaking A Peptide Bond
With a hydrolysis reaction - adding water
Residual
Differentiates between different amino acids
Forming A Peptide Bond
A condensation reaction removes OH from the carboxylic acid group of one amino acid and the H from the amine group of another amino acid
-a water molecule (h2O) is released and the bond forms
Dipeptide
Two amino acids joined together by a peptide bond
Polypeptide
A chain of amino acids joined together by peptide bonds
Primary Structure
The sequence of amino acids in a polypeptide chain
Protease Enzyme
An enzyme that breaks down proteins
Secondary Structure
Assumed in the rough endoplasmic reticulum The coiling of an amino acid chain into an alpha helix held together by hydrogen bonds
Polypeptide chains can link together with hydrogen bonds holding the parallel chains in beta pleated sheets
Both alpha helices and beta pleated sheets can occur in the same protein
Tertiary Structure
The secondary structure of the polypeptide chain bends and folds to produce a precise 3D structure
This is held together by:
Hydrogen Bonds
Ionic Bonds
Disulphide Bonds
Quaternary Structure
Several polypeptide chains linked together
Denaturation
An irreversible change in the tertiary structure of a protein molecule
Leading to a loss of function in most proteins
Haemoglobin
A transport protein
Haemoglobin
Structure
Water soluble
Globular protein
Made up of four separate polypeptide chains, a quaternary structure
Two called alpha chains and two called beta chains
Haemoglobin
Function
High affinity for oxygen
Bonds oxygen in the lungs and carries it to the tissues where it releases it
An oxygen atom can bind to the iron in a haem group
haemoglobin + oxygen = oxyhemoglobin
One complete haemoglobin molecule can bind up to four oxygen molecules
Tertiary Structure
Disulphide Bond
Forms between two sulphur containing R groups
A covalent bond
Collagen
Structure
A collagen molecule is made up of three polypeptide chains wound around each other like a twisted rope
Each chain is made up of around 1000 amino acids
Hydrogen bonds between the chains giving the structure strength
Each collagen molecule forms covalent bonds, cross links, with the molecules next to it
This structure is a fibril many fibrils together form a collagen fibre
Collagen
Function
To provide mechanical strength
Walls of the arteries have a layer of collagen to prevent blood being pumped at high pressure from bursting the walls
Tendons are mostly collagen
Bones are formed from collagen and reinforced with calcium phosphate
Cartilage and connective tissue are made of collagen
Collagen
A structural protein
Proteins
Test
Biuret Test
- Add Biuret reagent which contains sodium hydroxide and copper sulphate to the sample
- These chemicals react with the peptide bonds found in proteins
- If protein is present the colour changes from blue to purple/lilac
Tertiary Structure
Ionic Bonds
From between polar R groups
R groups are polar if the electrons are unevenly distributed
Non polar R groups will be at the centre of the protein because they are hydrophobic and the protein is formed inside a cell so is surrounded by water