Biochemistry /OCR Biology A - 2.1.2 - Biological Molecules Part 5

OCR Biology A - 2.1.2 - Biological Molecules Part 5

Biochemistry25 CardsCreated 11 days ago

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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TermDefinition
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