Macromolecules and Biochemical Principles in General Biology

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Carbon is a fundamental element in biological molecules due to its versatile bonding properties and role in organic chemistry.

Carbon Bonding: Carbon atoms can form up to four covalent bonds with other atoms, allowing for a variety of stable structures such as chains, rings, and branched molecules.
Hydrolysis and Dehydration Reactions:
- Dehydration (Condensation) Reaction: A chemical reaction in which two molecules are joined by removing a molecule of water. This process is essential for forming polymers from monomers.
- Hydrolysis Reaction: The reverse process, where a water molecule is added to break a bond, splitting polymers into monomers.
Example: The formation of a peptide bond between two amino acids involves a dehydration reaction.

Living organisms are composed of four major classes of macromolecules, each with distinct structures and functions.

Carbohydrates: Serve as energy sources and structural components. Monomers are monosaccharides (e.g., glucose).
Lipids: Include fats, oils, and phospholipids. They are hydrophobic and function in energy storage, insulation, and membrane structure.
Proteins: Polymers of amino acids that perform a wide range of functions, including catalysis (enzymes), structure, transport, and signaling.
Nucleic Acids: DNA and RNA, which store and transmit genetic information. Monomers are nucleotides.

Additional info: Each macromolecule has unique monomers and bonds that link them together.

Fats are a type of lipid, and their structure determines their physical properties and health implications.

Saturated Fats: Have no double bonds between carbon atoms; all carbons are saturated with hydrogen. Typically solid at room temperature (e.g., butter).
Unsaturated Fats: Contain one or more double bonds, causing kinks in the fatty acid chains. Usually liquid at room temperature (e.g., olive oil).
Example: Animal fats are generally saturated, while plant oils are often unsaturated.

Hydrocarbons are organic molecules consisting entirely of carbon and hydrogen. They are nonpolar and hydrophobic.

The central dogma describes the flow of genetic information within a biological system.

Proteins have four levels of structure, each contributing to their function.

Primary Structure: The linear sequence of amino acids in a polypeptide chain.
Secondary Structure: Local folding into structures such as alpha-helices and beta-pleated sheets, stabilized by hydrogen bonds.
Tertiary Structure: The overall three-dimensional shape of a single polypeptide, determined by interactions among R groups.
Quaternary Structure: The association of multiple polypeptide chains to form a functional protein complex.
Example: Hemoglobin has quaternary structure, consisting of four polypeptide subunits.

Different types of bonds link monomers to form biological polymers.