Chapter 5.3-5.3 Flashcards
fat
A lipid consisting of three fatty acids linked to one glycerol molecule; also called a triacylglycerol or triglyceride.
triaglycerol
Three fatty acids linked to one glycerol molecule; also called a fat or a triglyceride.
unsaturated fatty acid
A fatty acid possessing one or more double bonds between the carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton.
saturated fatty acid
A fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton.
trans fat
An unsaturated fat containing one or more trans double bonds.
phospholipid
A lipid made up of glycerol joined to two fatty acids and a phosphate group. The hydrocarbon chains of the fatty acids act as nonpolar, hydrophobic tails, while the rest of the molecule acts as a polar, hydrophilic head. Phospholipids form bilayers that function as biological membranes.
steroid
A type of lipid characterized by a carbon skeleton consisting of four rings with various chemical groups attached.
cholesterol
A steroid that forms an essential component of animal cell membranes and acts as a precursor molecule for the synthesis of other biologically important steroids, such as hormones.
catalyst
A chemical agent that increases the rate of a reaction without being consumed by the reaction.
polypeptide
A polymer (chain) of many amino acids linked together by peptide bonds.
protein
A functional biological molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure.
amino acid
An organic molecule possessing both carboxyl and amino groups. Amino acids serve as the monomers of polypeptides.
polypeptide
The covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction.
primary structure
The level of protein structure referring to the specific sequence of amino acids.
secondary structure
The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between constituents of the backbone.
a helix
A spiral shape constituting one form of the secondary structure of proteins, arising from a specific pattern of hydrogen bonding.
B pleated sheet
One form of the secondary structure of proteins in which the polypeptide chain folds back and forth. Two regions of the chain lie parallel to each other and are held together by hydrogen bonds.
tertiary structure
Irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges.
disulphide bridges
A strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer.
quaternary structure
The particular shape of a complex, aggregate protein, defined by the characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide.
denaturation
In proteins, a process in which a protein unravels and loses its native shape, thereby becoming biologically inactive; in DNA, the separation of the two strands of the double helix. Denaturation occurs under extreme (noncellular) conditions of pH, salt concentration, and temperature.
chaperonin
A protein molecule that assists in the proper folding of other proteins.
X-ray crystallography
A technique that depends on the diffraction of an X-ray beam by the individual atoms of a crystallized molecule to study the three-dimensional structure of the molecule.
