Carbohydrates, lipids, proteins and nucleic acids form the biochemical foundation of every living cell, and this deck of 20 flashcards walks through each macromolecule class in depth. You'll cover monomer-polymer relationships and the condensation/hydrolysis r...
Carbohydrates, lipids, proteins and nucleic acids form the biochemical foundation of every living cell, and this deck of 20 flashcards walks through each macromolecule class in depth. You'll cover monomer-polymer relationships and the condensation/hydrolysis reactions that build and break them down, then move through carbohydrate structure (starch, glycogen, cellulose), lipid structure (triglycerides, saturated vs. unsaturated fats, phospholipids), and the four levels of protein structure from primary sequence to quaternary assembly. The deck also explains DNA and RNA nucleotide structure and base pairing, and finishes with a section on enzymes — the lock-and-key and induced-fit models, factors affecting enzyme activity, and competitive versus non-competitive inhibition. Ideal for A-Level and AP Biology or introductory biochemistry courses, these cards focus on the structural details and vocabulary most commonly tested in exams.
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Carbohydrates, lipids, proteins, and nucleic acids.
A monomer is a single repeating subunit; a polymer is a large molecule made of many monomers joined together (e.g. amino acids form proteins).
Condensation (dehydration synthesis) joins monomers by releasing water; hydrolysis breaks polymers apart by adding water.
Monosaccharides, such as glucose, fructose and galactose.
All are glucose polymers: starch is the plant energy store, glycogen is the animal energy store, and cellulose is a structural component of plant cell walls.
One glycerol molecule bonded to three fatty acid chains via ester bonds.
Saturated fatty acids have no double bonds between carbons (straight chains, solid at room temp); unsaturated have one or more double bonds (kinked chains, liquid at room temp).
A lipid with a phosphate head and two fatty acid tails; its amphipathic nature (hydrophilic head, hydrophobic tails) makes it the main component of cell membranes.
Amino acids, joined by peptide bonds to form polypeptide chains.
The sequence of amino acids (primary structure) and the interactions between their side chains (R groups), including hydrogen bonds, ionic bonds, disulfide bridges and hydrophobic interactions.
The loss of a protein's 3D structure and function due to heat, pH change, or other stress, disrupting the bonds that maintain its shape.
Nucleotides, each composed of a phosphate group, a five-carbon sugar, and a nitrogenous base.
DNA (deoxyribonucleic acid, sugar = deoxyribose) and RNA (ribonucleic acid, sugar = ribose).
Adenine pairs with thymine (A-T), and cytosine pairs with guanine (C-G), held together by hydrogen bonds.
A biological catalyst, usually a protein, that speeds up the rate of a chemical reaction without being consumed.
Lock-and-key: the substrate fits the enzyme's active site precisely. Induced-fit: the active site changes shape slightly to better fit the substrate upon binding.
Temperature, pH, substrate concentration, and the presence of inhibitors or cofactors.
Competitive inhibitors bind the active site, blocking the substrate. Non-competitive inhibitors bind elsewhere, changing the enzyme's shape and reducing activity.
A non-protein helper molecule (metal ion or organic coenzyme, e.g. vitamins) required for an enzyme to function properly.
