Biochemistry /OCR Biology A - 2.1.2 - Biological Molecules Part 5
OCR Biology A - 2.1.2 - Biological Molecules Part 5
This deck covers key concepts related to biological molecules, focusing on the structure and function of lipids, proteins, and carbohydrates.
Unsaturated fats
Liquid at room temp Double carbon bonds Bent (linked) Found in plants Lower melting point
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Key Terms
Term
Definition
Unsaturated fats
Liquid at room temp Double carbon bonds Bent (linked) Found in plants Lower melting point
Function of lipids in the body
Energy store Thermal insulation Repel water Shock absorbent Buoyant Waterproof
How do phospholipids differ in their structure from triglycerides
Phosphate group replaces one fatty acid
Why are lipids useful storage molecules
Insoluble molecules | High energy yield (2x as much as carbohydrates)
What factors do substances need to have to be 'transport' carbohydrates
Small Soluble Not reactive
What causes the colour change in the Benedict's test
The copper is reduced by the reducing sugars to form ions
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Term | Definition |
---|---|
Unsaturated fats | Liquid at room temp Double carbon bonds Bent (linked) Found in plants Lower melting point |
Function of lipids in the body | Energy store Thermal insulation Repel water Shock absorbent Buoyant Waterproof |
How do phospholipids differ in their structure from triglycerides | Phosphate group replaces one fatty acid |
Why are lipids useful storage molecules | Insoluble molecules | High energy yield (2x as much as carbohydrates) |
What factors do substances need to have to be 'transport' carbohydrates | Small Soluble Not reactive |
What causes the colour change in the Benedict's test | The copper is reduced by the reducing sugars to form ions |
Why can't humans digest all polysaccharides | We do not possess the appropriate enzymes |
How to reverse condensation reactions | Hydrolysis reactions | Adding acid |
Functions of proteins | Signalling Catalysis Structure and movement Defence and survival Transport |
How do plants make amino acids | From photosynthesis and nitrate/mmonium |
How many amino acids do human need | Twenty but we cannot make any of the 8/10 essential and 12/10 non essential amino acids |
Why is the R group important | The Residual group is the only thing that differs in amino acids |
Formation of peptide bond | Water is removed (condensation reaction) | Peptide bond is formed (covalent C-N bond) |
Dipeptide | 2 amino acids |
Polypeptide/ protein | Many amino acids |
Primary structure of proteins | Subunits held together by peptide bonds | Order determined by base sequences in DNA |
Secondary structure of proteins | Folding or coiling of polypeptide chains for stabilisation | Hydrogen bonds cause polypeptide to coil into alpha helix or fold into beta sheets |
What breaks hydrogen bonds | High temperature | pH change |
How does a breakage of bonds affect the protein | It affects the shape and function |
Tertiary structure of proteins | The secondary structure is folded into a more complex 3D shape |
What is the tertiary structure stabilised by | Disulphide bonds between sulfur containing R groups Ionic bonds between R groups Hydrogen bonds between polar R groups Hydrophobic/ hydrophilic interaction |
Quaternary structure of proteins | Made up from multi sub-unit proteins Held together by same bonds in 3' Most proteins only have one polypeptide chain and so no quaternary structure |
Globular proteins | Spherical and usually soluble Hydrophobic R groups in centre, hydrophilic R groups point outside Activity in metabolism relies on 3D shape Shape and activity sensitive to high temp. |
Why is haemoglobin a conjugated protein | It has a prosthetic group |
What is a prosthetic group in a protein | An attachment not made from protein e.g. Haem |