Module 2: Biological Molecules Flashcards
Condensation reaction
Links monomers together
A water molecule is released
A covalent bond is formed
A larger molecule is formed
Hydrolysis reactions
Splits molecules apart
A water is used
A covalent bond is broken
Smaller molecules are formed
Hydrogen bonds
Hydrogen bonds hold polymers in shape. This shape allows them to carry out a function.
Hydrogen bonds form when a slightly negative and a slightly positive charge come class together.
They are weak and easily broken
What are carbohydrates made up of?
C, H and O
For every one carbon there are two hydrogens and one oxygen
Simple sugars= monosaccharides
- contain 3-6 carbons
- soluble in water
- sweet tasting
- form crystals
Carbohydrates- disaccharides
2 monosaccharides will join in a condensation reaction to form a disaccharide.
We call this covalent bond between monosaccharides a glycosidic bond.
a and B glucose
ADD PICTURE
Carbohydrates- storage
Plants and animals are only capable of breaking down a glucose, not B glucose due to the difference in structure.
B glucose can’t be respired so they are not used for storage.
Polysaccharides- Amylose
a glucose + a glucose= maltose (disaccharide)
This reaction occurs thousands of times to form amylose.
The a glucose molecules are held together by a 1-4 glycosidic bond.
Amylose forms a spring shape due to the shape of glucose and glycosidic bonds.
Amylose is unbranched an compact. It is insoluble.
Polysaccharides- Starch
Plant energy storage:
Starch is a mixture of amylose molecules and amylopectin molecules.
Amylopectin- branches of a glucose chains with 1-4 glycosidic bonds joined at ends to another chain by a 1-6 glycosidic bond.
It is a store of energy because it can be broken down into a glucose by enzymes in hydrolysis reactions.
Polysaccharides- Glycogen
Animal energy storage:
Polysaccharide of a glucose
- Glycogen is broken down by enzymes in hydrolysis reactions to form glucose for respiration.
- Found in glycogen granules in animal cells e.g. in live and muscles
- More compact than starch
1-4 linked chains are shorter and more branched than 1-6 chains (starch)
More branches= more ends to be broken off= faster break down= faster energy release
Starch and glycogen similarities
Insoluble in water- don’t reduce the water potential in cells.
Store glucose molecules in chains so they can be easily broken off and the glucose can be used in respiration.
Cellulose
Cellulose is a structural unit found in plant cell walls.
Polysaccharide of 1000s of B glucose joined together by condensation reactions. Forms with 1-4 glycosidic bonds in a long, straight, unbranched chain.
Every B glucose is flipped 180 degrees to form a glycosidic bond.
Hydrogen bonds form between neighbouring cellulose chains and the chains become cross-linked to form a microfibril. Microfibrils are held together by hydrogen bonds to form macrofibrils.
- Micro and macrofibrils control cell shape.
- Macrofibril arrangement in guard cells cause the opening and closing of stomata.
Macrofibrils
Macrofibrils are embedded with pectin which glues them together in a criss-cross structure to form cell walls.
The criss-cross structure allows water to pass through- Macrofibrils are very strong so that water moving in doesn’t cause them to burst.
Other Carbohydrate Polymers are used by a number of other organisms to provide support. For example…
Chitin- insect exoskeleton
Peptidoglycan- bacterial cell walls
What are amino acids?
Monomers of proteins
There are 20 different amino acid- each have a different R group.
Amino acids are joined together through a condensation reaction. The covalent bond formed is called a peptide bond.
2 amino acids joined= dipeptide
A polymer of amino acids is called a polypeptide (protein)
The backbone will always have the same pattern:
NCC,NCC,NCC,NCC,NCC…
Peptide bonds are broken through a hydrolysis reaction.
Dipeptides are broken down into 2 amino acids. When proteins are digested, hydrolysis reactions break apart the amino acids.
Function of proteins
Proteins are polymers of amino acids.
Functions:
- Structural- muscle & bone
- Protein channels
- Enzymes
- Many hormones
- Antibodies
Proteins are crucial for growth and repair and metabolic activity.
Making proteins…
To make proteins organisms need amino acids.
Plants make their own using nitrates in the soil.
Animals need to consume protein in their diet. The polypeptide is broken down in digestion and built back up again to make protein for the body.
Primary structure of proteins
Every protein has a different sequence of amino acids- this is it’s primary structure.
This determines it’s structure which determines it’s properties and function.
Breaking apart proteins
Enzymes that beak apart peptide bonds are proteases.
E.g. digestion, hormones so that their effect isn’t constant.
Transcription- GCSE understanding
Taking the DNA code and making messenger RNA (mRNA).
1) An enzyme unwinds the double helix of DNA.
2) The two strands are separated so that free nucleotides can fit in.
3) Free nucleotides attach to he complementary base pairs.
4) mRNA moves away from the DNA helix and another enzyme zips the strands together.
5) The mRNA is small enough to leave the nuclear membrane.
Translation- GCSE understanding
Taking the message from mRNA and translating it into a chain of amino acids.
1) The mRNA enters the ribosome.
2) Transfer RNA (tRNA) enters the ribosome and brings with it a specific amino acid that corresponds with the codon on the mRNA strand.
3) tRNA has an anti-codon that matches the codon on mRNA so they pair together using complementary base pair rules.
4) The amino acid that is brought by the first tRNA binds to the second amino acid by a peptide bond.
5) When all the amino acids have been joined together, the mRNA leaves the ribosome and a new protein has been made.
Secondary structure of proteins
As polypeptides form, to prevent them from tangling they are stabilised by being coiled (alpha helix) or pleated (beta pleated sheet). These are held in place by hydrogen bonds. This coiling/pleating is the proteins secondary structure.
Why is the secondary structure dependent on the primary structure?
The primary structure of a protein is a sequence of amino acids.
Different proteins have different sequence of amino acids which have different R groups with different properties.
These different properties mean that hydrogen bonds form in different places of the pleats/coils meaning that some or more/less pleated/ coiled than others.
Tertiary structure of proteins
The tertiary structure of a protein is the overall 3D structure of the protein.
This is when the coil/pleat coils or folds into the final shape (this folding is dependant on the primary structure).
The tertiary structure is key to the protein’s function (e.g. hormone needs to fit into complementary receptor/enzyme’s active site).