unit 1 section 2 - Digestive system

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What happens in digestion
we break down larger molecules into small molecules.
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Give two examples of polymers in our food.
Proteins and carbohydrates.
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What is hydrolysis?
Breaking down using water
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Describe the oesophagus' role in digestion.
A muscular tube which takes the food from the mouth to the stomach by using waves of muscle contractions and mucus.
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Describe the Stomach's role in digestion.
Walls produce gastric juice, walls churn the food mechanically, gastric juice contains HCL, pepsin and mucus.
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What is the mixture that leaves the stomach called?
Chyme.
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Describe the Small Intestine's role in digestion.
Chyme pushed along using muscular contractions, bile and pancreatic juices neutralise chyme, small molecules absorbed through villi.
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Describe the Large intestine's role in digestion.
Absorb water and salt and minerals, bacteria here helps decompose undigested food, folded wall helps increase surface area.
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Describe the rectums' roll in digestion.
To store faeces.
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Describe the pancreas' roles in digestion.
To release pancreatic juices which contain a lot of enzymes and neutralise HCL
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Two amino acids together are called what?
A dipeptide
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More than two amino acids together are called what?
A polypeptide.
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What are the 3 groups of an amino acid and what do they contain?
Amine group contains NH2, R group is the variable group, carboxy group contains COOH.
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The bond between two amino acids is called what?
A peptide bond.
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What type of reaction occurs when two amino acids bond?
A condensation reaction where h20 is removed.
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Describe the Primary structure of a protein.
A sequence of amino acids in a polypeptide chain.
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Describe the Secondary structure of a protein.
Hydrogen bonds start to form between the chain, making it coil into an alpha helix or beta pleeted sheet
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Describe the tertiary structure of a protein.
Coiled up further with more hydrogen bonds forming at different points, for proteins made of single polypeptide chains, this is there final 3d form.
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Describe the Quaternary structure of a protein.
The different polypeptide chains are all coiled up together very tight.
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Describe the test for proteins.
Add sodium hydroxide, add copper sulfate solution, if there is a protein a purple layer will appear.
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What are the monomers that make up carbohydrates?
monosaccharides
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Give 3 examples of monosaccharides.
Glucose, fructose and Galactose.
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On an alpha glucose is the hydrogen at the top of the bottom?
Top.
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On a beta glucose is the hydrogen on the top or bottom?
Bottom.
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What is bonded to the 6th carbon atom on glucose?
CH2OH
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On carbon 3 is the hydrogen on the top or the bottom?
Top
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On Carbon 4 is the hydrogen on the top or bottom?
Bottom.
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What type of reaction occurs when two monosaccharides bond?
A condensation reaction.
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What is the bond between two monosaccharides called?
A glycosidic bond.
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On an alpha glucose, which carbons bond?
Carbon 1,4.
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What is maltose hydrolysed into?
Glucose + glucose
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What is Sucrose hydrolysed into?
Glucose + Fructose.
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What is lactose hydrolysed into?
Glucose + Galactose.
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Describe the test for reducing sugars.
Add Benedicts solution and then heat it up, if a reducing sugar is present then it will go from blue to brick red.
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What is starch made from?
Long chains of glucose linked together by glycosidic bonds.
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How is starch broken down?
Broken into maltose by amylase, then broken down into glucose by maltase.
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What is the test for startch?
Add iodine dissolved in the potassium iodide solution, it will go from brown/orange to blue/black.
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What do enzymes do to a reaction in terms of energy?
The lower the activation energy so less energy in needed to start the reaction.
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How do enzymes lower the activation energy?
substrates bond to the enzymes active site, the enzyme applies pressure/strain which means the substrate is easier to break apart.
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Describe the lock and key model.
The enzyme is a fixed/rigid structure that has an active site the exact shape of the substrate.
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Give two limitations of the lock and key model.
Suggests the enzyme is rigid when its fluid, suggest enzyme has only one bonding site.
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Give two strengths of the lock and key model.
Simple to understand, Gives basic understanding of how enzymes work.
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Describe the induced fit model.
Enzyme active site will mould around the substrate as they go to bond because the enzyme is fluid.
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Give a limitation of this model.
More complicated to understand,
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Give two strengths of this model.
Gives more accurate picture, more detailed.
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What is a competitive inhibitor?
same shape as the substarte so bonds with the active site stopping the substrate from bonding
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what is a non competitive inhibitor?
Bonds to somewhere else on the enzyme, this changes the overall shape of the enzyme so the substrate cant bond to the active site still.
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Card 2

Front

Give two examples of polymers in our food.

Back

Proteins and carbohydrates.

Card 3

Front

What is hydrolysis?

Back

Preview of the front of card 3

Card 4

Front

Describe the oesophagus' role in digestion.

Back

Preview of the front of card 4

Card 5

Front

Describe the Stomach's role in digestion.

Back

Preview of the front of card 5
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