Chapter 2: Biological molecules

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51 Terms

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Water

A polar molecule with hydrogen bonds; has high specific heat capacity

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Hydrogen Bond

A weak electrostatic attraction between a slightly positive hydrogen atom and a slightly negative atom

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Cohesion

The attraction between water molecules due to hydrogen bonding

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Adhesion

The attraction between water molecules and other polar surfaces

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Polarity

Unequal charge distribution within a molecule; polar molecules like water interact with other charged or polar substances.

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Inorganic Ion

Charged atoms or molecules involved in biological functions

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Monosaccharide

Simple sugar and monomer of carbohydrates

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α-glucose

Isomer of glucose with the -OH group on carbon 1 below the ring; forms starch and glycogen.

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β-glucose

Isomer of glucose with the -OH group on carbon 1 above the ring; forms cellulose.

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Disaccharide

Two monosaccharides joined by a glycosidic bond

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Polysaccharide

Polymer of many monosaccharides; used for storage (starch

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Glycosidic Bond

Covalent bond between two monosaccharides formed by a condensation reaction.

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Condensation Reaction

A reaction where two molecules join together with the removal of a water molecule.

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Hydrolysis

A reaction where a molecule is broken down by the addition of water.

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Starch

Plant storage polysaccharide of α-glucose; made of amylose and amylopectin

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Glycogen

Animal storage polysaccharide of α-glucose; highly branched for rapid energy release.

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Cellulose

Structural polysaccharide of β-glucose; forms strong fibres for plant cell walls.

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Benedict’s Test

Test for reducing sugars; positive result turns brick-red after heating with Benedict’s reagent.

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Lipid

Non-polar biological molecule used for energy storage

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Triglyceride

A lipid made from one glycerol and three fatty acids joined by ester bonds.

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Fatty Acid

Long hydrocarbon chain with a carboxyl group; can be saturated (no double bonds) or unsaturated (has double bonds).

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Glycerol

A three-carbon alcohol that forms the backbone of triglycerides and phospholipids.

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Ester Bond

Bond formed between glycerol and a fatty acid during condensation.

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Phospholipid

Lipid with two fatty acids and a phosphate group; forms bilayers in cell membranes.

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Hydrophobic

Repelled by water; non-polar molecules or parts of molecules.

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Hydrophilic

Attracted to water; polar molecules or groups.

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Emulsion Test

Test for lipids; positive result is a cloudy white emulsion after mixing with ethanol and water.

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Amino Acid

Monomer of proteins; contains an amine group

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Peptide Bond

Covalent bond between amino acids formed by condensation.

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Polypeptide

Chain of amino acids joined by peptide bonds.

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Primary Structure (Protein)

The specific sequence of amino acids in a polypeptide chain.

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Secondary Structure (Protein)

Folding of polypeptide into α-helices and β-pleated sheets via hydrogen bonding.

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Tertiary Structure (Protein)

3D shape of a polypeptide due to interactions between R groups

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Quaternary Structure (Protein)

Structure formed when two or more polypeptides join

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Globular Protein

Compact, circular and carry out functions

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Fibrous Protein

Long, string like and provide structural support. Not soluble in water

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Hydrogen Bond (Protein)

Weak bond between polar groups that stabilises protein structure.

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Ionic Bond (Protein)

Attraction between oppositely charged R groups in protein structure.

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Disulfide Bridge

Strong covalent bond between sulfur atoms in cysteine amino acids.

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Biuret Test

Test for proteins; turns purple in presence of peptide bonds.

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Enzyme

Biological catalyst that speeds up reactions by lowering activation energy.

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Active Site

Region on an enzyme where the substrate binds and the reaction occurs.

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Substrate

Molecule that fits into an enzyme’s active site to be transformed.

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Enzyme-Substrate Complex

Temporary combination of enzyme and substrate during catalysis.

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Induced Fit Model

Model where the enzyme changes shape slightly to better fit the substrate.

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Lock and Key Model

Model where enzyme active site fits substrate exactly.

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Activation Energy

Minimum energy needed for a chemical reaction to occur; lowered by enzymes.

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Denaturation

Loss of enzyme structure and function due to changes in temperature or pH.

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Optimum Temperature / pH

The temperature or pH at which an enzyme’s activity is highest.

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Competitive Inhibitor

Molecule that competes with the substrate for the active site.

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Non-Competitive Inhibitor

Molecule that binds elsewhere on the enzyme