BIOL 107 Chapter 4 Notes: Proteins & Glycoproteins

Flashcards covering key vocabulary related to proteins and glycoproteins from Chapter 4 of the BIOL 107 lecture notes.

Proteins

Macromolecules whose monomers are called amino acids.

Amino Acids

The monomers of proteins, consisting of an amino group, a carboxyl group, and an R group.

R Group

A variable group attached to an amino acid that determines its specific biochemical properties and contributes to protein diversity, structure, and function.

Peptide Bond

A bond formed between the carboxyl group of one amino acid and the amino group of another amino acid via a dehydration/condensation reaction.

N-terminus

The end of an amino acid chain (protein) that has a free amino group.

C-terminus

The end of an amino acid chain (protein) that has a free carboxyl group.

Primary Structure

The unique linear sequence of amino acids in a protein.

Secondary Structure

Local folding patterns in a protein, such as alpha-helices or beta-sheets, formed by hydrogen bonding between backbone atoms.

Tertiary Structure

The overall 3-dimensional shape of a single polypeptide chain, resulting from interactions between R groups (e.g., hydrogen bonds, Van der Waals interactions).

Quaternary Structure

The structure formed by the interactions between two or more fully folded protein subunits.

Enzymes

Proteins that catalyze (increase the speed of) biochemical reactions.

Transportation Proteins

Proteins that shuttle substances around, into, or out of the cell.

Support Proteins

Proteins responsible for maintaining cell structure, like the cytoskeleton.

Signaling Proteins

Proteins involved in communication between different parts of the cell or the entire body, such as peptide hormones.

Movement Proteins

Proteins involved in the movement of things within the cell or the movement of the cell itself (e.g., cilia or flagella).

Defense Proteins

Proteins active in the immune system, such as antibodies.

Protein Folding

The process by which a protein assumes a specific 3-dimensional shape, dictated by amino acid sequence and chemical interactions, essential for its function.

Chaperones

Proteins that assist other proteins in folding properly.

Denaturation

The process by which a protein loses its natural 3-dimensional shape and function, often caused by changes in pH, high temperatures, or certain chemicals, without altering its primary amino acid sequence.