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Vocabulary flashcards covering key terms and definitions from water properties, macromolecules, and nucleic acids from the notes.
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Polar covalent bond
A covalent bond where electrons are shared unequally, creating partial charges within a molecule (as in the O–H bonds of water).
Water polarity
A property of water due to unequal electron sharing, giving partial positive charges on H and partial negative on O, enabling hydrogen bonding.
Hydrogen bond
A weak attraction between a hydrogen atom on one molecule and a highly electronegative atom (like O or N) on another or within a molecule.
Cohesion
Attraction between like molecules, such as water–water, due to hydrogen bonding.
Adhesion
Attraction between water and nonwater substances, aiding movement of water along surfaces.
Surface tension
The cohesive force at a liquid’s surface that makes it behave as if covered with a stretched film.
Specific heat capacity
The amount of heat required to raise the temperature of a substance; water has a high value, helping stable body temperatures.
Heat of vaporization
The energy required to convert a liquid to vapor; water’s high value enables evaporative cooling.
Evaporative cooling
Cooling that occurs when liquid water evaporates, removing heat as it changes to gas.
Capillary action
The upward or lateral movement of water in narrow spaces due to cohesion and adhesion.
Homeostasis
Maintenance of stable internal conditions in living organisms.
Macromolecule
A large biological polymer (carbohydrates, proteins, lipids, nucleic acids) built from monomers.
Carbohydrate
Macromolecule made of C, H, O; monomers are monosaccharides; functions include energy storage and structure.
Protein
Macromolecule composed of amino acids; functions include enzymes, structure, signaling.
Lipid
Nonpolar, hydrophobic macromolecule; includes fats, steroids, phospholipids; diverse roles in storage, membranes, and signaling.
Nucleic acid
Macromolecule (DNA or RNA) that stores and transmits genetic information; monomers are nucleotides.
Monomer
A single subunit that can join with others to form a polymer.
Polymer
A large molecule composed of many repeating monomers linked together.
Monosaccharide
Simple sugar; monomer of carbohydrates (e.g., glucose, fructose).
Disaccharide
Two monosaccharides joined by a glycosidic bond (e.g., sucrose, maltose).
Polysaccharide
Polymers made of many monosaccharides; includes starch and cellulose.
Glycosidic bond
Covalent bond linking carbohydrate monomers.
Starch
Plant storage polysaccharide with primarily alpha-1,4 glycosidic bonds; digestible by humans.
Cellulose
Plant structural polysaccharide with beta-1,4 glycosidic bonds; not digestible by humans.
Sulfur-containing amino acids
Amino acids that include sulfur (e.g., cysteine, methionine) in proteins.
Phosphorus-containing macromolecules
Molecules that include phosphorus, such as phospholipids and nucleic acids.
Nitrogen-containing macromolecules
Molecules that include nitrogen, notably nucleic acids and proteins.
Phosphodiester bond
Covalent bond connecting nucleotides in nucleic acids’ backbone.
Ester bond
Bond between glycerol and fatty acids in lipids.
Glycerol
Three-carbon backbone in triglycerides that bonds to fatty acids via ester bonds.
Amino acid
Amino acids are the monomers of proteins; they contain an amino group, carboxyl group, a central carbon, and an R group.
Peptide bond
Covalent bond formed between amino acids during dehydration synthesis.
N-terminus
End of a protein that contains the amino group.
C-terminus
End of a protein that contains the carboxyl group.
Monomer vs polymer terminology
Monomer is a single unit; polymer is a long chain of many monomers linked together.
Primary structure
Linear sequence of amino acids in a protein.
Secondary structure
Local folding patterns (alpha-helix and beta-pleated sheet) stabilized by hydrogen bonds.
Alpha-helix
Right-handed coiled structure common in proteins’ secondary structure.
Beta-pleated sheet
Sheet-like secondary structure formed by hydrogen bonds between segments of the polypeptide.
Tertiary structure
Three-dimensional shape of a single polypeptide, stabilized by various bonds and interactions.
Disulfide bridge
Covalent bond between cysteine residues that helps stabilize a protein’s structure.
Quaternary structure
Assembly of multiple polypeptides into a functional protein.
N-terminus and C-terminus function
Terminate ends of polypeptide chains with amino and carboxyl groups, respectively, affecting directionality.
DNA
Deoxyribonucleic acid; stores genetic information; typically double-stranded; uses A-T and C-G base pairing.
RNA
Ribonucleic acid; information carrier and functional molecule; typically single-stranded; uses A-U and C-G base pairing.
Nucleotide
Monomer of nucleic acids; consists of a sugar, phosphate, and a nitrogenous base.
Purine
Double-ring nitrogenous bases (A and G) in DNA/RNA.
Pyrimidine
Single-ring nitrogenous bases (C, T, and U) in DNA/RNA.
Adenine
Purine base that pairs with thymine in DNA and with uracil in RNA.
Thymine
Pyrimidine base in DNA that pairs with adenine; replaced by uracil in RNA.
Cytosine
Pyrimidine base that pairs with guanine.
Guanine
Purine base that pairs with cytosine.
Uracil
Pyrimidine base in RNA that pairs with adenine; replaces thymine.
Deoxyribose
Five-carbon sugar in DNA lacking an oxygen atom at the 2' position.
Ribose
Five-carbon sugar in RNA with a hydroxyl group at the 2' position.
5' end
End of a nucleic acid with the phosphate attached to the 5' carbon of the sugar.
3' end
End of a nucleic acid with a free hydroxyl group on the 3' carbon.
Antiparallel
Two strands run in opposite 5' to 3' directions in DNA.
Complementary base pairing
Specific pairing: A with T (or U in RNA), and C with G.
Double helix
The spiral, two-stranded structure of DNA formed by antiparallel strands with base pairing.