Introduction to Cell Biology & Biochemistry

These flashcards cover key concepts in protein structure from the lecture on Cell Biology & Biochemistry.

Protein Structure

The arrangement of amino acids in a protein which determines its shape and function.

Tertiary Structure

The overall three-dimensional shape of a protein made by a single polypeptide chain.

Fibrous Proteins

Proteins that are long strands or sheets, typically providing structural support and shape.

Globular Proteins

Proteins that are folded into spherical shapes, often involved in enzyme activity and regulation.

α-Helix

A type of secondary protein structure characterized by a right-handed spiral.

β-Sheets

A type of secondary protein structure formed by hydrogen bonds between chains, creating a sheet-like formation.

Quaternary Structure

The structure formed when two or more polypeptide chains associate to create a functional protein.

Hydrophilic

A property of molecules or regions that are attracted to water.

Hydrophobic

A property of molecules or regions that repel water and prefer to associate with other nonpolar substances.

Collagen

A fibrous protein consisting of repeating sequences mainly composed of glycine, providing structural support.

Silk Fibroin

A protein produced by spiders and silkworms, known for its strength and flexibility.

Prosthetic Group

A non-polypeptide unit that is tightly and permanently attached to a protein and is necessary for that protein's function.

Myoglobin

A globular protein in muscle cells that stores oxygen, containing a single iron-containing heme group.

Haemoglobin

The oxygen-carrying protein in red blood cells composed of four polypeptide chains, each containing a heme group.

Hydrogen Bonds

Weak bonds that can form between the electronegative atom of one molecule and a hydrogen atom bonded to another electronegative atom.

Van der Waals Interactions

Weak attractions between molecules or parts of molecules that result from transient local partial charges.