1/55
Vocabulary flashcards covering organic chemistry principles, functional groups, isomers, polymerization reactions, carbohydrates, lipids, proteins, enzymes, and nucleic acids based on the lecture transcript.
Name | Mastery | Learn | Test | Matching | Spaced | Call with Kai | Chat |
|---|
No analytics yet
Send a link to your students to track their progress
Organic Chemistry
The branch of chemistry devoted to carbon compounds.
Carbon
The chemical element whose properties are fundamental to forming biologically important organic molecules, capable of forming up to four covalent bonds.
Functional Groups
Groups of atoms with characteristic chemical structures and properties that bond to carbon in organic molecules.
Amino Group
A weakly basic functional group (-NH2) that can accept H+, is polar, and forms part of peptide bonds in amino acids and proteins.
Carbonyl Group
A polar, highly chemically reactive functional group (-CO) found in ketones, aldehydes, steroids, waxes, and proteins that forms hydrogen bonds.
Carboxyl Group
An acidic functional group (-COOH) that gives up H+ in water and forms part of peptide bonds in amino acids and fatty acids.
Hydroxyl Group
A polar functional group (-OH) that forms hydrogen bonds with water; found in steroids, alcohol, carbohydrates, and some amino acids.
Methyl Group
A nonpolar functional group (-CH3) that may be attached to DNA, proteins, and carbohydrates.
Phosphate Group
A polar, weakly acidic functional group (-PO42−) that is negatively charged at typical pH of living organisms; found in nucleic acids, ATP, and phospholipids.
Sulfhydryl Group
A polar functional group (-SH) found in proteins containing cysteine that forms disulfide bridges.
Isomers
Organic molecules that have identical molecular formulas but a different arrangement of atoms.
Structural Isomers
Isomers that differ in the order in which their constituent atoms are attached.
Stereoisomers
Isomers with identical bonding relationships whose atoms differ in their spatial positioning.
Geometric Isomers
Stereoisomers (cis/trans isomers) that differ in spatial positioning of atoms around a double bond.
Enantiomers
Stereoisomers that exist as non-superimposable mirror images of each other (chiral molecules).
Polymers
Large biological molecules constructed by linking together many identical or similar subunits called monomers.
Monomers
Small, repeating organic subunits that polymerize to form polymers.
Dehydration Synthesis Reaction
A chemical reaction that synthesizes polymers from monomers by removing a molecule of water (H2O).
Hydrolysis Reaction
A chemical reaction that depolymerizes or breaks down polymers into monomers by adding a molecule of water (H2O).
Monosaccharides
Single sugar molecules consisting of linked carbons and hydrogens that serve as the monomers of carbohydrates.
Glycosidic Bond
The covalent bond formed between two monosaccharides joined by a dehydration reaction.
Starch
A plant storage polysaccharide composed of α-glucose monomers, existing as unbranched amylose and branched amylopectin.
Glycogen
A highly branched animal storage polysaccharide composed of α-glucose monomers linked by α-1-4 and α-1-6 linkages.
Cellulose
An unbranched structural polysaccharide in plant cell walls composed of long chains of β-glucose molecules joined by β-1-4 linkages.
Chitin
A structural polysaccharide found in animal exoskeletons and fungal cell walls composed of N-acetylglucosamine monomers.
Fatty Acids
Hydrocarbon chains of varying length terminating in a carboxyl group that serve as basic subunits of lipids.
Saturated Fatty Acid
A fatty acid with no double bonds between carbon atoms, resulting in a linear structure that packs tightly and is solid at room temperature.
Unsaturated Fatty Acid
A fatty acid containing one or more double bonds that introduce kinks in the hydrocarbon chain, preventing tight packing and causing it to be liquid at room temperature.
Cis-Fats
Naturally occurring unsaturated fats where the hydrocarbon chain is in the cis conformation across double bonds.
Trans-Fats
Artificially manufactured unsaturated fats where the hydrocarbon chain is in the trans conformation across double bonds.
Triglycerides
Pseudo-polymers formed by joining three fatty acid molecules to a single glycerol backbone via ester bonds in dehydration reactions.
Ester Bond
The covalent bond formed between the hydroxyl group of glycerol and the carboxyl group of a fatty acid.
Phospholipids
Amphipathic lipid molecules consisting of a polar hydrophilic head and two nonpolar hydrophobic fatty acid tails, forming cell membrane bilayers.
Steroids
Lipids defined by a structure of four fused carbon rings, including cholesterol, estradiol, and testosterone.
Waxes
Lipids composed of fatty acids bonded to long hydrocarbon chains, used by organisms for waterproofing and protection.
Amino Acids
The building blocks of proteins, consisting of a central α-carbon bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R group).
Peptide Bond
The covalent bond formed between the carboxyl carbon of one amino acid and the amino nitrogen of another during protein synthesis.
Polypeptide
A linear sequence of amino acids linked together by peptide bonds, serving as the structural unit of a protein.
Primary Structure
The linear sequence of amino acids in a polypeptide chain.
Secondary Structure
Conformations within a polypeptide, such as α-helices and β-pleated sheets, held together by hydrogen bonds between backbone atoms.
Tertiary Structure
The overall three-dimensional shape of a single polypeptide chain formed by folding secondary structures and connecting coil regions.
Quaternary Structure
The functional protein complex formed when two or more polypeptide subunits bind to each other.
Disulfide Bridge
A covalent bond formed between the sulfhydryl (-SH) groups of two cysteine residues within a protein.
Denaturation
A process in which a protein loses its specific three-dimensional shape and biological activity due to heat, pH changes, or chemicals.
Chaperone Proteins
Proteins that assist misfolded proteins in correctly refolding into their functional three-dimensional structures using ATP.
Enzyme
A protein that acts as an organic catalyst to accelerate a chemical reaction without being consumed, by lowering its activation energy (Ea).
Ribozyme
An RNA molecule that exhibits enzymatic activity.
Induced Fit Model
The model describing how an enzyme undergoes a conformational change upon substrate binding at the active site to form the enzyme-substrate complex.
Competitive Inhibitor
A reversible inhibitor that binds directly to the active site of an enzyme, competing with the substrate.
Noncompetitive Inhibitor
A reversible inhibitor that binds to an allosteric site on an enzyme, altering its shape so that it cannot bind substrate effectively.
Nucleotides
The monomeric units of nucleic acids, each composed of a pentose sugar, a phosphate group, and a nitrogenous base.
Phosphodiester Bond
The covalent bond linking nucleotides, formed between the 3′ hydroxyl group of one pentose sugar and the 5′ phosphate group of the adjacent sugar.
Purines
Double-ring nitrogenous bases found in nucleic acids, consisting of Adenine and Guanine.
Pyrimidines
Single-ring nitrogenous bases found in nucleic acids, consisting of Cytosine, Thymine (DNA only), and Uracil (RNA only).
Deoxyribonucleic Acid (DNA)
A double-stranded, antiparallel nucleic acid containing deoxyribose sugar and thymine that stores genetic information in units called genes.
Ribonucleic Acid (RNA)
A typically single-stranded nucleic acid containing ribose sugar and uracil that provides access to genetic information for protein expression.