Macromolecules: Carbohydrates, Lipids, Proteins, and Nucleic Acids

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Vocabulary practice flashcards covering macromolecule types, chemical reactions, lipid structures, and protein structural levels from Lecture 6.

Last updated 3:25 PM on 9/11/26
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26 Terms

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Dehydration Synthesis

A chemical reaction that combines monomers into polymers by removing a water molecule (H2OH_2O).

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Hydrolysis

A chemical reaction that breaks polymers down into monomers by adding a water molecule (H2OH_2O).

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Monosaccharide

The simple sugar monomer subunit that links together to form carbohydrate polymers.

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Starch and Glycogen

Branched complex carbohydrates used for energy storage that can be digested by humans.

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Cellulose and Chitin

Straight-chain complex carbohydrates used for structural support that cannot be digested by humans.

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Nucleic Acids

Biological macromolecules (DNADNA and RNARNA) composed of nucleotide monomers that store genetic information and code for proteins.

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<p>Nucleotide</p>

Nucleotide

The monomer building block of nucleic acids, consisting of a phosphate group, a sugar, and a nitrogenous base.

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Glycerol

A three-carbon lipid monomer skeleton with a hydroxyl group (-OH\text{-OH}) attached to each carbon.

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Fatty Acid

A lipid monomer consisting of a carboxyl group (-COOH\text{-COOH}) attached to a long hydrocarbon chain, often 1616 to 1818 carbons long.

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Triglyceride

A lipid polymer formed by binding three fatty acid chains to a glycerol molecule via dehydration synthesis, removing 33 water molecules (3H2O3H_2O).

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Saturated Fatty Acid

A fatty acid filled with hydrogens containing only single carbon-carbon bonds, resulting in a straight structure that is solid at room temperature.

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Unsaturated Fatty Acid

A fatty acid containing one or more double carbon-carbon bonds, creating a bent structure that is liquid at room temperature.

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Hydrogenation

The process of adding hydrogens to unsaturated fatty acids to remove double bonds and convert them into saturated fats.

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Cis-fatty Acid

An unsaturated fatty acid with hydrogens on the same side of the double bond, causing the molecule to fold back into a U-like formation.

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<p>Trans-fatty Acid</p>

Trans-fatty Acid

An unsaturated fatty acid with hydrogens on opposite sides of the double bond, resulting in a linear molecule typically produced in partially hydrogenated foods.

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High-Density Lipoproteins (HDL)

Known as good cholesterol; particles that pick up excess cholesterol in the body and transport it back to the liver for processing.

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Low-Density Lipoproteins (LDL)

Known as bad cholesterol; particles that transport cholesterol throughout the body, where excess buildup in artery walls narrows blood flow.

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<p>Phospholipid</p>

Phospholipid

An amphipathic lipid consisting of a polar, hydrophilic phosphate head and two non-polar, hydrophobic fatty acid tails.

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Amphipathic

Describing a dual-nature molecule that contains both hydrophobic (water-fearing) and hydrophilic (water-loving) regions.

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<p>Amino Acid</p>

Amino Acid

The monomer building block of proteins, consisting of a central carbon bonded to an amino group (-NH2\text{-NH}_2), a carboxylic acid group (-COOH\text{-COOH}), a hydrogen, and a variable side chain (R group).

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Primary Protein Structure

The linear sequence of amino acids in a polypeptide chain linked together by strong covalent peptide bonds.

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<p>Secondary Protein Structure</p>

Secondary Protein Structure

Local folding patterns in a polypeptide backbone, such as alpha helices and beta pleated sheets, stabilized by hydrogen bonding.

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<p>Tertiary Protein Structure</p>

Tertiary Protein Structure

The overall functional 3D shape of a single polypeptide chain, stabilized by hydrogen bonds, hydrophobic interactions, disulfide bridges, and ionic bonds.

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<p>Quaternary Protein Structure</p>

Quaternary Protein Structure

The structural level formed by the aggregation of two or more individual polypeptide chains (tertiary protein subunits), such as collagen or hemoglobin.

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<p>Myoglobin</p>

Myoglobin

A single-chain tertiary protein found primarily in muscle tissue that serves as an intracellular storage site for oxygen.

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<p>Denaturation</p>

Denaturation

The process in which extreme environmental conditions (such as temperature or pH changes) disrupt a protein's 3D shape and function without altering its primary amino acid sequence.