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Vocabulary-style flashcards covering core biomolecules and related chemistry concepts from the notes (carbohydrates, lipids, proteins, nucleic acids, and foundational biochemistry).
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Carbohydrate
Biomolecule class with formula Cx(H2O)x; includes sugars and polysaccharides; primary role is energy storage and, in some organisms, structural support.
Monosaccharide
Simple sugar; basic unit of carbohydrates (e.g., glucose, fructose).
Disaccharide
Two monosaccharides linked by a glycosidic bond (e.g., sucrose, lactose, maltose).
Polysaccharide
Polymer of many monosaccharides; can be storage (starch, glycogen) or structural (cellulose, chitin).
Glycosidic linkage
Covalent bond between two monosaccharides formed by dehydration synthesis; can be alpha or beta depending on orientation.
Alpha glycosidic linkage
Glycosidic bond where the linked OH group is below the ring plane; common in starches.
Beta glycosidic linkage
Glycosidic bond where the linked OH group is above the ring plane; common in cellulose.
Starch
Plant storage polymer of glucose; consists of amylose (unbranched) and amylopectin (branched); has alpha linkages.
Amylose
Unbranched component of starch.
Amylopectin
Branched component of starch.
Glycogen
Animal storage polymer of glucose; highly branched; stored mainly in liver and muscles.
Cellulose
Structural polysaccharide in plant cell walls; beta-1,4 glycosidic linkages; humans cannot digest it.
Chitin
Structural polysaccharide in fungal cell walls and arthropod exoskeletons; amino sugar monomers with beta linkages.
Lipid
Large, nonpolar biomolecules that do not mix well with water; include fats, phospholipids, and steroids.
Fat (triglyceride)
Glycerol bound to three fatty acids via ester bonds; major energy-storage molecule and insulator.
Fatty acid
Carboxylic acid with a long hydrocarbon chain; can be saturated or unsaturated.
Saturated fatty acid
Fatty acid with only single bonds between carbons; typically solid at room temperature.
Unsaturated fatty acid
Fatty acid with one or more carbon–carbon double bonds; typically liquid at room temperature.
Trans fat
Unsaturated fat with one or more trans double bonds; often produced by hydrogenation; associated with health risks.
Phospholipid
Lipid with glycerol, two fatty acids, and a phosphate group; amphipathic; major component of cell membranes.
Steroid
Lipid with four fused carbon rings; includes cholesterol and many hormones.
Cholesterol
Steroid important for animal cell membranes; precursor to other steroids.
Protein
Polymers of amino acids folded into a functional three-dimensional structure; perform many cellular roles.
Amino acid
Monomer of proteins; contains an amino group, a carboxyl group, and a variable R group.
Peptide bond
Covalent bond linking amino acids via dehydration synthesis.
Primary structure
Linear sequence of amino acids in a protein.
Secondary structure
Local folding patterns (alpha-helix, beta-pleated sheet) stabilized by backbone hydrogen bonds.
Alpha-helix
Right-handed coiled secondary structure common in proteins.
Beta-pleated sheet
Secondary structure with sheet-like arrangement stabilized by backbone hydrogen bonds.
Tertiary structure
Overall three-dimensional shape of a protein caused by R-group interactions (hydrophobic, ionic, hydrogen bonds, disulfide bridges).
Quaternary structure
Association of two or more polypeptide chains into a functional protein.
Denaturation
Loss of a protein’s native shape due to disruption of weak chemical bonds (e.g., by pH, salt, or heat).
Sickle-cell anemia
Genetic disease caused by a single amino acid substitution (Val for Glu) in beta-globin; deforms red blood cells and impairs oxygen transport.
Enzyme
Protein that acts as a catalyst to speed up chemical reactions without being consumed.
Active site
Region of an enzyme where substrate binds and catalysis occurs.
Substrate
Reactant that binds to an enzyme.
Induced fit
Model in which an enzyme changes shape to better embrace its substrate.
Cofactor
Nonprotein component required for enzyme activity (can be inorganic ion or organic molecule).
Coenzyme
Organic cofactor that assists enzyme activity.
Competitive inhibitor
Substance that competes with the substrate for access to the active site; effect can be overcome by increasing substrate concentration.
Noncompetitive inhibitor
Inhibitor that binds to a site other than the active site, altering enzyme shape and reducing activity.
Allosteric regulation
Regulation of an enzyme by binding a molecule at a site other than the active site, affecting activity at another site.
Cooperativity
Substrate binding to one subunit increases catalytic activity of other subunits (e.g., hemoglobin).
ATP
Adenosine triphosphate; energy currency of the cell; three phosphate groups; drives energy-requiring reactions.
Nucleic acid
Polymers (DNA and RNA) composed of nucleotides; store and transmit genetic information.
Nucleotide
Nucleic acid monomer: sugar + nitrogenous base + phosphate.
Nucleoside
Sugar + nitrogenous base; lacks phosphate group.
Purine
Broad, two-ring nitrogenous bases (adenine and guanine).
Pyrimidine
Single-ring nitrogenous bases (cytosine, thymine, uracil).
DNA
Deoxyribonucleic acid; double helix with two antiparallel strands; sugar is deoxyribose; bases A–T and C–G pair via hydrogen bonds.
RNA
Ribonucleic acid; typically single-stranded; sugar is ribose; bases A–U, C–G.
Base pairing
A pairs with T (or U in RNA) via two hydrogen bonds; C pairs with G via three hydrogen bonds.
Double helix
Three-dimensional structure of native DNA with two antiparallel polynucleotide strands coiled around an axis.
Human Genome Project
Large-scale project (1990–2003) to sequence the entire human genome.
Genomics
Study of whole genomes and their structure, function, and evolution.
Proteomics
Study of the full set of proteins (and their sequences) produced by an organism.
Bioinformatics
Use of computer software and computational tools to analyze large biological data sets.