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21 Terms

1

Macromolecules

Large biological molecules essential for life, which include carbohydrates, proteins, nucleic acids, and lipids.

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2

Dehydration Synthesis

A chemical reaction where two monomers are joined together, releasing a water molecule in the process.

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3

Hydrolysis

A chemical process that breaks down polymers into monomers by adding water.

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4

Carbohydrates

Biological molecules that serve as a primary energy source and structural support, comprised of saccharides.

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5

Monosaccharide

The simplest form of carbohydrates, consisting of single sugar molecules like glucose.

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6

Disaccharide

Carbohydrates formed from two monosaccharides; examples include sucrose and lactose.

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7

Polysaccharide

Carbohydrates composed of long chains of monosaccharide units; examples include starch, glycogen, and cellulose.

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8

Amino Acids

Building blocks of proteins that link together through peptide bonds to form polypeptides.

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9

Peptide Bond

A covalent bond formed between the carboxyl group of one amino acid and the amino group of another.

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10

Nucleic Acids

Biological macromolecules that store and transmit genetic information; examples are DNA and RNA.

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11

Functional Groups

Specific groups of atoms within molecules that determine the characteristic chemical reactions of those molecules.

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12

Lipid

A diverse group of hydrophobic organic molecules including fats, oils, phospholipids, and steroids.

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13

Saturated Fatty Acid

A type of fatty acid that contains no double bonds between carbon atoms, resulting in a straight chain.

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14

Unsaturated Fatty Acid

A fatty acid that contains one or more double bonds, causing kinks in its structure.

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15

Phospholipid

A lipid comprising a phosphate group and two fatty acids, essential for forming cell membranes.

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16

Polypeptide

A chain of amino acids linked by peptide bonds that folds into a functional protein.

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17

Secondary Structure (of proteins)

The local folded structures that form within a polypeptide due to interactions between amino acids, including alpha helixes and beta sheets.

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18

Tertiary Structure (of proteins)

The overall three-dimensional structure of a polypeptide, determined by interactions among the R-groups of amino acids.

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19

Quaternary Structure (of proteins)

The structure formed when two or more polypeptide chains associate to form a single functional protein complex.

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20

Denaturation

The process by which a protein loses its native shape due to the disruption of non-covalent interactions, often caused by heat, pH, or salt.

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21

Hydrolysis Reaction

A reaction that breaks bonds through the addition of water, commonly used to revert polymers to monomers.

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