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Proteins are polymers composed of amino acids linked together by peptide bonds. These amino acids contain a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a distinctive side chain. The sequence and arrangement of these amino acids determine each protein's unique structure and function.

Proteins are distinct macromolecules composed of amino acids, while other compounds essential to human function include carbohydrates, lipids, and nucleic acids. Each macromolecule type has different elemental composition and structural organization. Proteins specifically contain nitrogen in their amino groups, making them unique among major biological polymers.

Proteins are classified into fibrous proteins and globular proteins based on their three-dimensional shape. Fibrous proteins are elongated and typically provide structural support, while globular proteins are compact and spherical, often serving dynamic roles like catalysis and transport. Both types are essential for different physiological functions.

A protein's three-dimensional structure determines its ability to perform specific functions in cells and tissues. The folding of amino acid chains creates active sites, binding regions, and structural features necessary for the role of proteins in the human body. Disruptions to this structure can impair or eliminate protein function.

Proteins can undergo protein denaturation when exposed to extreme conditions such as high temperature, extreme pH, or certain chemical solvents. Denaturation disrupts the bonds maintaining protein structure, causing the molecule to unfold and lose its three-dimensional shape. This structural change typically results in loss of biological activity.

Amino acid side chains vary in chemical composition, ranging from nonpolar hydrophobic groups to polar and charged groups. These differences determine how amino acids interact with each other and their environment, influencing protein solubility, charge, and overall three-dimensional folding. Side chain properties are fundamental to protein diversity and function.

Peptide bonds are covalent linkages that connect amino acids together in a linear chain, forming the protein backbone. These bonds form between the carboxyl group of one amino acid and the amino group of the next through a dehydration reaction. The sequence of amino acids linked by peptide bonds determines the primary structure of every protein.