Cohesion
Attraction between water molecules due to hydrogen bonding; allows water columns to move up xylem vessels without breaking.
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1.1.2
Adhesion
Attraction between water molecules and other surfaces (e.g., xylem walls); helps water rise against gravity through capillarity.
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1.1.2
Surface Tension
Property of water that allows it to form a "skin" at the surface due to hydrogen bonding; affects water infiltration and supports small insects.
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1.1.2
Heat Capacity
Water's ability to absorb or release heat slowly without changing temperature much; protects plants from temperature extremes.
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1.1.2
Universal Solvent
Water's ability to dissolve more substances than any other liquid due to its polarity; essential for nutrient transport in plants.
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1.1.2
Carbohydrate
Organic molecules composed of carbon, hydrogen, and oxygen (CH₂O)ₙ; include sugars, starches, and cellulose.
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1.2.1
Monosaccharide
Single sugar unit; the simplest form of carbohydrate. Examples: glucose, fructose, galactose.
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1.2.1
Disaccharide
Two sugar units linked by a glycosidic bond. Example: sucrose (glucose + fructose).
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1.2.1
Polysaccharide
Many sugar units linked together; used for energy storage (starch) or structure (cellulose).
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1.2.1
Starch
Primary energy storage polysaccharide in plants; consists of amylose (linear) and amylopectin (branched).
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1.2.1
Cellulose
Structural polysaccharide in plant cell walls; consists of β-1,4 linked glucose units; indigestible by humans (dietary fiber).
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1.2.1
Pectin
Complex polysaccharide in middle lamella; acts as glue holding plant cells together; important for fruit texture and jam making.
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1.2.1
Brix (°Bx)
Measure of soluble solids (primarily sugars) in fruits and vegetables; 1°Bx = 1g sucrose per 100g solution.
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1.2.2
Lipid
Hydrophobic organic molecules; include fats, oils, waxes, phospholipids, and sterols. Used for energy storage, membrane structure, and protection.
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1.2.3
Fatty Acid
Long hydrocarbon chain with a carboxyl group; building block of many lipids. Can be saturated (no double bonds) or unsaturated (with double bonds).
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1.2.3
Saturated Fatty Acid
Fatty acid with no double bonds; straight chain; solid at room temperature. Example: palmitic acid.
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1.2.3
Unsaturated Fatty Acid
Fatty acid with one or more double bonds; bent chain; liquid at room temperature. Example: oleic acid.
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1.2.3
Triglyceride
Glycerol + three fatty acids; main form of energy storage in plants (oils in seeds).
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1.2.3
Phospholipid
Glycerol + two fatty acids + phosphate group; amphipathic molecule that forms bilayers in cell membranes.
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1.2.3
Amphipathic
Having both hydrophilic (water-loving) and hydrophobic (water-fearing) regions; characteristic of phospholipids.
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1.2.3
Wax
Ester of long-chain fatty acid and long-chain alcohol; forms protective coating (cuticle) on leaves and fruits.
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1.2.3
Cuticle
Waxy layer covering leaves, fruits, and non-woody stems; reduces water loss and provides protection.
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1.2.3
Carotenoid
Lipid-soluble pigments (yellow, orange, red); function in photosynthesis and as antioxidants. Examples: β-carotene, lycopene.
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1.2.3
Amino Acid
Building block of proteins; contains amino group, carboxyl group, hydrogen, and variable R group.
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1.3.1
Peptide Bond
Covalent bond formed between carboxyl group of one amino acid and amino group of another; releases water (condensation reaction).
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1.3.1
Primary Structure
Linear sequence of amino acids in a protein; determined by DNA.
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1.3.1
Secondary Structure
Local folding patterns (α-helix, β-sheet) stabilized by hydrogen bonds between backbone atoms.
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1.3.1
Tertiary Structure
Overall three-dimensional shape of a protein; stabilized by interactions between R groups (hydrophobic, ionic, disulfide bridges).
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1.3.1
Quaternary Structure
Arrangement of multiple polypeptide subunits; example: rubisco (16 subunits).
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1.3.1
Enzyme
Protein catalyst that speeds up biochemical reactions by lowering activation energy.
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1.3.2
Activation Energy
Energy barrier that must be overcome for a reaction to proceed; enzymes lower this barrier.
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1.3.2
Active Site
Region of enzyme where substrate binds and catalysis occurs; has specific three-dimensional shape.
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1.3.2
Substrate
Molecule upon which an enzyme acts.
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1.3.2
Lock and Key Model
Model of enzyme action where active site is exactly complementary to substrate shape.
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1.3.2
Induced Fit Model
Model where active site changes shape slightly upon substrate binding, becoming complementary after binding.
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1.3.2
Denaturation
Loss of protein's three-dimensional structure (unfolding) due to heat, pH, or chemicals; loss of function.
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1.3.3
Competitive Inhibition
Inhibitor resembles substrate and binds to active site; can be overcome by increasing substrate concentration.
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1.3.3
Non-competitive Inhibition
Inhibitor binds to allosteric site, changing enzyme shape; cannot be overcome by adding more substrate.
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1.3.3
Cofactor
Inorganic ion (e.g., Mg²⁺, Zn²⁺) required for enzyme activity.
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1.3.2
Coenzyme
Organic molecule (often vitamin-derived) required for enzyme activity; e.g., NAD⁺, FAD.
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1.3.2