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Fatty acid
Hydrocarbon chains with a carboxyl group at one end.
Glycerol
A three-carbon alcohol that serves as the backbone for triglycerides and phospholipids.
Ester linkage
A covalent bond formed between a carboxyl group (-COOH) and a hydroxyl group (-OH), typically found in fats and phospholipids.
Triglycerol
A fat molecule composed of three fatty acids linked to one glycerol molecule.
Saturated fat
A type of fat characterized by fatty acid chains that have no double bonds between carbon atoms.
Unsaturated fat
A type of fat characterized by fatty acid chains that have one or more double bonds between carbon atoms.
Phospholipids
Lipids composed of a glycerol backbone, two fatty acid tails, and a phosphate group, forming the primary component of cell membranes.
Steroids
A class of lipids characterized by a four-ring structure, serving various functions in the body, including as hormones.
Enzymatic proteins
Proteins that act as biological catalysts, speeding up specific biochemical reactions.
Storage proteins
Proteins that store amino acids or other substances for later use.
Hormonal proteins
Proteins that act as chemical messengers, coordinating bodily activities.
Contractile and motor proteins
Proteins responsible for movement, such as actin and myosin in muscle contraction.
Defensin proteins
Proteins that play a role in the immune system, defending the body against pathogens.
Transport proteins
Proteins that facilitate the movement of substances across cell membranes.
Receptor proteins
Proteins that bind to specific signaling molecules, initiating cellular responses.
Structural proteins
Proteins that provide support and maintain the shape of cells, tissues, and organs.
Amino acids
There are 20 different amino acids; they can be combined in various sequences to form proteins.
Peptide bond
Covalent bonds that link amino acids together in a polypeptide chain.
N-terminus
The end of a polypeptide chain with a free amino group.
C-terminus
The end of a polypeptide chain with a free carboxyl group.
Primary structure
The unique linear sequence of amino acids in a polypeptide chain, determined by genetic information.
Secondary structure
The regular, local folding patterns of the polypeptide chain, mainly alpha helix and beta-pleated sheet.
Tertiary structure
The overall three-dimensional shape of a single polypeptide chain, resulting from interactions between R groups.
Quaternary structure
The arrangement of multiple polypeptide chains (subunits) to form a functional protein complex.
Denaturation of proteins
The process of unfolding a protein, disrupting its three-dimensional structure.
Nucleotide
The building block of nucleic acids, consisting of a nitrogen base, a pentose sugar, and a phosphate group.
Phosphodiester bond
A bond that joins the sugar of one nucleotide to the phosphate group of another, forming the backbone of nucleic acids.
ATP
Adenosine triphosphate, a nucleotide with additional phosphate groups that serves as an energy carrier.
DNA base pairing
In DNA, adenine pairs with thymine through 2 hydrogen bonds, and guanine pairs with cytosine through 3 hydrogen bonds.