All Notes Needed For OCR As Biology (F212 exam)
- Created by: Amy
- Created on: 03-06-12 16:36
Biological Molecules
Water
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High Specific Heat Capacity – organisms survive in deeper warmer water; layer of ice prevents further heat loss.
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Hydrogen Bonds – creates surface tension; some small organisms can move across the surface of the water.
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Solvent – polar substances dissolve in water due to charges.
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Transport Medium – flows; blood plasma is mainly water.
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Involved in Metabolic Reactions – photosynthesis and respiration.
Proteins
Primary Structure – a sequence of amino acids.
Secondary Structure – twisting of the primary structure into alpha helix and beta pleated sheets.
Tertiary Structure – Hydrogen Bonds, Ionic Bonds, Disulfide Bridges, Hydrophobic Interactions.
Quaternary Structure – addition of prosthetic groups, carbohydrates, etc.
Haemoglobin
- Globular Protein
- Chain of amino acids
- Alpha helical secondary structure
- Hydrogen, ionic, disulfide, hydrophobic bonds in tertiary structure
- 4 polypeptide chains (2 alpha, 2 beta)
- 1 haem group per polypeptide
- Fe2+ ion in haem
Collagen
- Fibrous Protein
- High proportion of glycine
- 3 polypeptide chains
- Chains form a tight coil held by hydrogen bonds
- Ends of parallel molecules are staggered
- Covalent bonds form between adjacent molecules
- Prevents lines of weakness
Carbohydrates
Alpha Glucose – OH is below carbon 1
Beta Glucose – OH is above carbon 1
Amylose
- Energy Store (Plants)
- Polysaccharide
- Alpha Glucose
- 1,4 glycosidic links
- Non-branched
- Compact
Amylopectin
- Energy Store (Plants)
- Polysaccharide
- Alpha Glucose
- 1,6 glycosidic links
- Branched
- Insoluble to not affect water potential
- Easily hydrolysed
Cellulose
- Plant Cell Walls
- Beta Glucose
- 1,4 glycosidic links
- Each glucose molecule is rotated 180 to its neighbour
- Straight chains
- Adjacent chains held by hydrogen bonds
Glycogen
- Energy Store (Animals)
- Polysaccharide
- Alpha Glucose
- 1,4 glycosidic links and 1,6 glycosidic links
- Branched and Compact
- Insoluble to not affect water potential
Lipids
Triglyceride
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1 Glycerol Molecule
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3 Fatty Acids
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Ester Bonds
Phospholipid
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1 Glycerol Molecule
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2 Fatty Acids
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1 Phosphate
Cholesterol
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4 carbon rings
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Hydrophobic
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Hormones & Vitamin D
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Cause gallstones and atherosclerosis
Protein
- Biuret A and Biuret B
- Blue to Lilac
Reducing Sugar
- Benedicts
- Warm
- Blue to Brick Red
Non-Reducing Sugar
- Hcl
- NaOH
- Benedicts
- Warm
- Blue to Brick Red
Starch
- Iodine
- Brown to Black
Lipids
- Alcohol
- Water
- White Emulsion
Glucose Colorimetry
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Add Benedicts Solution
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Solution turns brick red
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Remove red precipitate
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Use colorimeter
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Calibrate using water
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use a red filter
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record readings of absorbance
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less absorbance = more glucose
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using known concentrations, set up calibration curve
- read concentrations off the graph
Enzymes
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Globular proteins.
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Soluble in water.
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Specific 3D shape.
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Catalyse chemical reactions inside and outside cells.
Enzymes are Specific to the Substrate they act on
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Tertiary structure form the active site.
Lock and Key Theory
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Active site has a specific shape that is complementary to the substrate.
Induced Fit Theory
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Enzyme changes shape slightly as the substrate binds with the active site.
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Makes active site fit more closely around the substrate.
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Change in shape put stress on bonds in substrate so reaction occurs more easily.
Factors Affecting Enzyme Controlled Reactions
Enzymes Concentration – Increases rate of reaction.
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More active sites available.
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More chance of substrate colliding with active site.
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More product produced.
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