Carbon Compounds, Chemical Reactions, And Enzymes

Monomer

A small, single molecular unit that acts as a building block for larger molecules.

Polymer

A large molecule made up of many repeating monomer units joined together.

Carbohydrate

An organic macromolecule composed of C, H, and O (1:2:1 ratio) used primarily for fast energy and structure.

Monosaccharide

Single sugar molecule monomer (e.g., glucose, fructose, galactose).

Disaccharide

Two monosaccharides joined covalently (e.g., sucrose, lactose, maltose).

Polysaccharide

Long chain of monosaccharides (e.g., starch, glycogen, cellulose, chitin).

Saturated Fat / Lipid

A fatty acid chain containing only single carbon-carbon bonds (C-C). Solid at room temperature (e.g., butter).

Unsaturated Fat / Lipid

A fatty acid chain containing one or more double bonds (C=C). Liquid at room temperature (e.g., olive oil).

Lipid

Nonpolar, hydrophobic macromolecule composed mostly of C, H, and O (e.g., fats, oils, waxes, steroids, phospholipids).

Nucleotide

Monomer of nucleic acids made of three components: a 5-carbon sugar, a phosphate group, and a nitrogenous base.

Nucleic Acid

Polymer stored in cell nuclei that transmits and stores genetic information (DNA and RNA). Made of C, H, O, N, P.

DNA (Deoxyribonucleic Acid)

Double-stranded nucleic acid containing deoxyribose sugar; stores genetic code.

RNA (Ribonucleic Acid)

Single-stranded nucleic acid containing ribose sugar; involved in protein synthesis.

Amino Acid

Monomer of proteins consisting of a central carbon, an amino group (_NH2), a carboxyl group (-COOH), a hydrogen atom, and a variable R-group.

Protein

Macromolecule made of amino acid chains joined by peptide bonds. Function depends on shape.

Chemical Reaction

Process that transforms one set of chemical compounds into another by breaking and forming chemical bonds.

Reactant

Starting substances in a chemical reaction (left side of the equation).

Product

Final substances produced by a chemical reaction (right side of the equation).

Activation Energy

Minimum energy needed to start a chemical reaction.

Catalyst

A substance that speeds up the rate of a chemical reaction without being consumed by lowering activation energy.

Enzyme

Biological protein catalyst that speeds up biochemical processes.

Substrate

Specific reactant that binds to an enzyme's active site.

Competitive Inhibitor

Molecules that closely resemble the substrate and compete for binding directly to the active site.

Noncompetitive Inhibitor (Allosteric Inhibitor)

Molecules that bind to an allosteric site, changing the overall shape of the enzyme.

Dehydration Synthesis

Combines monomers into polymers by removing a water molecule.

Hydrolysis

Breaks polymers apart into monomers by adding a water molecule.

Primary Structure

Linear sequence of amino acids linked together by peptide bonds.

Secondary Structure

Coiling or folding of the polypeptide chain into alpha-helices or beta-pleated sheets maintained by hydrogen bonds.

Tertiary Structure

3D folding pattern driven by R-group interactions.

Quaternary Structure

Structural combination of two or more polypeptide chains.

HONC Rule

The HONC 1234 rule helps remember how many covalent bonds each element typically forms: H=1, O=2, N=3, C=4.

Covalent Bonds

Bonds formed when atoms share electrons.

Enzyme Action

Substrate binds to the enzyme's active site, forming an Enzyme-Substrate Complex.

Temperature Impact on Enzymes

Low temp slows reactions; optimal temp peaks reaction rate; high temp denatures enzymes.

pH Impact on Enzymes

Enzymes have an optimal pH range for activity; deviation can cause denaturation.

Substrate Concentration Impact

Increasing concentration speeds up reaction until saturation is reached.

Denatured Protein

A protein that has lost its normal 3D shape and active function.

Peptide Bond

Covalent bond linking the carbonyl carbon of one amino acid to the amino nitrogen of the adjacent amino acid.

Triglycerides

Provide long-term energy storage, insulation, and cell membrane structure.

Essential Amino Acids

Amino acids that must be obtained from the diet for protein synthesis.

Hydrophobic Interactions

Forces that drive nonpolar (hydrophobic) amino acids to cluster together in proteins.

Hydrogen Bonds

Weak bonds that can help maintain the secondary structure of proteins.