Biological Molecules Flashcards
What is the structure of the two glucose isomers - alpha and beta glucose?
Both have an O. Alpha glucocorticoid has 2 H’s at the top (heavens above) whereas beta glucose has one H and an OH.
What are monomers and polymers?
A monomer is a small single unit of a molecule. As polymer is a chain of monomer molecules bonded together in a chain. This i also called a polymerisation reaction.
What is a biological molecule?
An organic molecule that contains carbon
How do molecules bond and break apart ?
Condensation reactions form bonds between molecules by removing a H2O molecule to create a bond. To break the bonds the polymer is hydrolysed and water is added back in.
What is hydrogen bonding?
H bonds are individually weak but many together are very strong. They are water molecules bonding covalently due to opposite charges.
What are carbohydrates hydrolysed by?
Carbohydrase, amylase and Maltese enzymes to turn starch into glucose.
What are monosaccharides and give examples?
3 carbons = triode (glyceraldehydre)
5 carbons = Pentose (ribose)
6 carbons = hexose (glucose and galactose)
General formula = (CH2O)n -> n is 3-7.
Sweet tasting due to simple sugars.
Same number of carbon atoms to oxygen atoms.
- glucose
- fructose
- galactose
What are disaccharides and give the examples?
Monosaccharide + monosaccharide (chain oof monosaccharides) bonded by condensation reactions and and by glycosidic bonds.
Maltose = glucose + glucose
Sucrose = glucose + fructose
Lactose = glucose + galactose
What are polysaccharides and give examples?
Many glucose units bonded together because of condensation reactions and glycosidic bonds. Starch, glycogen and cellulose.
What is the structure and function of starch?
Starch is used for storage of energy/glucose in plants. It’s a mixture of two polysaccharides of alpha glucose - amylose and amylopectin.
Amylose - long, unbranched, coiled structure due to angle of glycosidic bonds. This makes it compact and good for storage.
Amylopectin - long, branched, with side branches so enzymes can break down molecule to be to glycosidic bonds easily. This means that energy can be released easily and glucose can be released.
What is the structure and function of glycogen?
It is the molecule that stones energy in animals and is a polysaccharide of alpha - glucose.
Loads of side branches so glucose can be released quickly for energy.
Very compact so good for storage.
What is the structure and function of cellulose?
Cellulose is the major component in plant cell walls.
Long, unbranched, chains of beta - glucose that are straight chains.
The chains then for layers which are linked by hydrogen bonds (stronger together).
Strong fibres formed = microfibrils that provide strength to plant cells.
What is triglyceride - function and structure?
Basic structure of a fatty acid?
It is a lipid molecule with a glycerol and 3 fatty acid molecules.
The fatty acids are hydrocarbon tails that are hydrophobic.
The basic structure of a fatty acid is 1 carbon atom with a double bond to an oxygen atom and single bonds to an R group and an HO molecule. The carbon atom links the fatty acid to the glycerol.
They are formed by condensation reactions when an H2O moleule is released.
They form ESTER bonds = the glycerol bonded to each fatty acid by at oxygen atom.
All 3 fatty acids must be bonded to form a triglyceride.
Triglycerides are used as good storage molecules because they contain lots of chemical energy.
INSOLUBLE - don’t affect water potential because they clump together with the hydrophobic heads facing inwards.
What is the difference between a saturated and an unsaturated fatty acid?
They difference is in the hydrocarbon tails.
Saturated fatty acids have NO double carbon bonds between carbon atoms. Saturated with hydrogen.
Unsaturated fatty acids have at least ONE DOUBLE BOND between carbon atoms to cause chain to kink.
What is a phospholipid and how is it different from a triglyceride?
Phospholipids found in cell membranes. They have a glycerol, 2 fatty acids and a PHOSPHATE group which is hydrophilic.
They make up the belayer of the cell surface (plasma) membrane.
Heads face out towards water on the inside and outside of the cell whereas the tails have inwards as the repel water.
What is the test for lipids?
Emulsion test!
- add ethanol to test substance
- shake well so it dissolves
- pour in water
- wait for milky white emulsion - more lipid = more milky.
Test for reducing and non-reducing sugars?
BENEDICT’S TEST!
- add reagent to sample and HEAT in water baths to boil
- positive = coloured precipitate (brick red)
- more sugar the more colour change (filter out and weight solids to compare)
- negative = NRS present.
SO…..
- NRS must be broken down into monosaccharides.
-> add dilute HCL and GENTLY heat in water bath.
- NEUTRALISE with sodium hydrogencarbonate
NOW REPEAT BENEDICT’S TEST
- positive = coloured precipitate
- still negative = stays blue (NO SUGAR)
Starch test?
IODINE TEST.
- add iodine in dissolved POTASSIUM IODINE SOLUTION to test sample.
- positive = blue/black
-negative = browny/orange
Describe the test for proteins?
BIURETS TEST! (2 STAGES)
- start with alkaline solution so add SODIUM HYDROXIDE solution.
- then add COPPER (II) SULFATE solution.
Positive = purple
Negative = stays blue
- pale so look carefully
Describe the basic structures of a protein and amino acid structures?
Long chain of amino acid monomers. Dipeptide is 2 AA’s.Polypeptide is 2 or more AA’s.
Proteins are many polypeptides together.
Amino acids structure is ….:
- carboxyl group (-COOH)
- amino group (-NH2)
- R group (variable between 20 types)
Polypeptides are linked by condensation reactions and form PEPTIDE bonds.
What are the four types of protein structure?
Primary structure:
- sequence of amino acids in polypeptide chain
Secondary structure:
- H bonds form between AA’s in a chain and cause a coil. Beta pleats form and alpha helix’s form.
Tertiary structure:
- amino acid chains coil more
- more H bonds and ionic bonds
- disulphide bonds
- 3D structure
Quaternary structure:
- many polypeptide chains held together by bonds
- like haemoglobin
Types of proteins and their functions?
Enzymes - usually spherical due to tight folding polypeptide chains. Soluble and has a role in metabolism and synthesise large molecules.
Antibodies - involved in immune response and are two light polypeptide chains and 2 heavy one. They have variable regions.
Transport proteins - channel proteins in cell membranes. Contain hydrophobic and hydrophilic amino acids which fold to form channels. Transport ions across membranes.
Structural proteins - very strong and are long polypeptide chains parallel with cross-links between them. Include keratin and collagen.
What are enzymes and their structure?
- biological catalysts
- very specific
- proteins
- complimentary to to substrate due to active site
- tertiary structure determines active sight
- form enzyme - substrate complex
Lock and key theory VS Induced fit model
Lock and key theory:
- substrate fits into enzymes active sight like a lock and key because they are complimentary
But….. the enzyme - substrate complex changes slightly fit completely fit which leads us to the induced fit model.
Substrate requires complimentary shape to specific enzyme but the active shape is also made to change shape to fit better.