Biological Molecules: Water, Carbohydrates, Lipids, Proteins, and Nucleic Acids

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Vocabulary practice flashcards covering water characteristics, carbohydrates, lipids, protein structure, types of proteins, and nucleic acid biochemistry.

Last updated 9:46 AM on 10/18/26
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57 Terms

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Polar molecule

A molecule with regions of negativity and regions of positivity resulting from the unequal sharing of electrons across covalent bonds.

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Hydrogen bond

A relatively weak chemical interaction formed when the slightly positive region of one polar molecule attracts the slightly negative region of another polar molecule.

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Cohesion

The property of water molecules sticking together and moving as one mass due to mutual attraction between polar molecules.

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Adhesion

The attraction of water molecules to other materials and polar surfaces.

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Capillary action

The process by which water rises up a narrow tube against the force of gravity, resulting from the combined effects of cohesion and adhesion.

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Carbohydrate

A biological molecule containing only carbon, hydrogen, and oxygen, usually occurring in the ratio Cx(H2O)yC_x(H_2O)_y.

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Monosaccharide

A single sugar unit that serves as a monomer for larger carbohydrates (e.g., glucose, fructose, and ribose).

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Disaccharide

A sugar formed when two monosaccharides join together by a glycosidic bond via a condensation reaction (e.g., maltose, lactose, and sucrose).

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Polysaccharide

A large carbohydrate polymer formed from many monosaccharide subunits linked together (e.g., glycogen, cellulose, and starch).

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Hexose monosaccharide

A monosaccharide sugar composed of six carbon atoms, having the molecular formula C6H12O6C_6H_{12}O_6, such as glucose, fructose, or galactose.

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Alpha (α\alpha) and Beta (β\beta) glucose

Two structural isomers of hexose glucose that differ in the orientation of the hydroxyl (−OH-OH) group attached to carbon 1.

<p>Two structural isomers of hexose glucose that differ in the orientation of the hydroxyl ($$-OH$$) group attached to carbon 1.</p>
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Condensation reaction

A chemical reaction in which two molecules join together through covalent bond formation with the elimination of a water molecule.

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Glycosidic bond

A covalent bond formed between two monosaccharides in a condensation reaction.

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Amylose

An unbranched starch polysaccharide composed of α\alpha-glucose monomers joined solely by 1,41,4-glycosidic bonds that twists into a compact helix stabilised by hydrogen bonds.

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Amylopectin

A branched starch polysaccharide composed of α\alpha-glucose molecules joined by 1,41,4-glycosidic bonds with 1,61,6-glycosidic branching points occurring approximately once every 2525 glucose subunits.

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Glycogen

A highly branched, compact energy storage polysaccharide in animals and fungi composed of α\alpha-glucose subunits with extensive 1,61,6-glycosidic branching points.

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Hydrolysis reaction

A chemical reaction that breaks bonds between monomers by the addition of a water molecule, catalysed by enzymes.

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Cellulose

A straight, unbranched polysaccharide made of β\beta-glucose molecules, in which alternate glucose units are rotated 180∘180^\circ upside down.

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Microfibrils

Strong structural bundles formed by parallel cellulose chains held together by hydrogen bonds, which aggregate into macrofibrils to form cell wall fibres.

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Reducing sugar

A sugar capable of donating electrons to (reducing) another chemical substance, such as all monosaccharides and some disaccharides including maltose and lactose.

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Benedict's reagent

An alkaline solution of copper(II) sulfate used to detect reducing sugars; upon reduction, blue Cu2+Cu^{2+} ions gain electrons to form a brick-red Cu+Cu^{+} precipitate.

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Colorimeter

An instrument that quantitatively measures the light absorbance or light transmission of a coloured solution to determine solute concentration.

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Biosensor

A device that combines a biological component (such as an enzyme, antibody, or ssDNA) with a transducer to produce an electrical or visual signal determining analyte concentration.

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Triglyceride

A lipid macromolecule composed of one molecule of glycerol combined with three fatty acid molecules via three ester bonds.

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Ester bond

The covalent bond formed between the hydroxyl group of glycerol and the carboxyl group of a fatty acid in a condensation reaction (esterification).

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Saturated fatty acid

A fatty acid chain that contains no carbon-to-carbon double bonds, holding the maximum possible number of hydrogen atoms bonded to carbon.

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Unsaturated fatty acid

A fatty acid containing one or more double bonds between carbon atoms, which creates kinks in the hydrocarbon chain preventing close packing.

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Phospholipid

A modified triglyceride in which one fatty acid chain is replaced by a negatively charged inorganic phosphate group (PO43−PO_4^{3-}), creating a hydrophilic head and two hydrophobic tails.

<p>A modified triglyceride in which one fatty acid chain is replaced by a negatively charged inorganic phosphate group ($$PO_4^{3-}$$), creating a hydrophilic head and two hydrophobic tails.</p>
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Surfactant

A surface active agent, such as a phospholipid, that forms a monolayer on water with hydrophilic heads in water and hydrophobic tails sticking out.

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Sterol

A lipid alcohol based on a four-carbon ring structure with a polar hydroxyl group, such as cholesterol.

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Emulsion test

A laboratory test for lipids in which a sample is dissolved in ethanol, mixed with water, and shaken; a milky-white emulsion layer indicates a positive result.

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Trans fat

An unsaturated lipid produced during industrial oil hardening where the natural kinks of the double bonds in fatty acid chains have been reversed.

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Amino acid

The monomer unit of proteins consisting of a central carbon bonded to an amine group (−NH2-NH_2), a carboxyl group (−COOH-COOH), a hydrogen atom, and a variable R-group.

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Peptide bond

A covalent bond formed between the carboxyl group of one amino acid and the amine group of another amino acid through a condensation reaction.

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Peptidyl transferase

The enzyme located within ribosomes that catalyses the formation of peptide bonds between amino acids during protein synthesis.

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Primary structure

The specific sequence of amino acids joined together by peptide bonds in a polypeptide chain.

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Secondary structure

The repeating coil (alpha helix) or pleated sheet (beta pleated sheet) conformation assumed by a polypeptide, stabilised by hydrogen bonds along the repeating backbone.

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Tertiary structure

The overall three-dimensional folding of a protein into its final functional shape, held together by hydrogen bonds, ionic bonds, hydrophobic/hydrophilic interactions, and disulfide bridges between R-groups.

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Quaternary structure

The functional three-dimensional protein macromolecule resulting from the association of two or more individual polypeptide subunits.

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Biuret test

A chemical test for proteins that uses sodium hydroxide and copper sulfate (or biuret reagent) to produce a violet-coloured complex in the presence of peptide bonds.

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Thin layer chromatography (TLC)

An analytical technique used to separate non-volatile mixtures, such as amino acids, based on differential movement between a stationary phase (e.g., silica gel) and an organic mobile phase.

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Retention value (RfR_f)

The ratio calculated in chromatography by dividing the distance travelled by an individual component by the distance travelled by the solvent front.

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Globular protein

A compact, roughly spherical, water-soluble protein whose tertiary structure places hydrophobic R-groups internally and hydrophilic R-groups on the exterior.

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Conjugated protein

A globular protein that contains a non-protein prosthetic group essential for its biological activity.

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Prosthetic group

A permanent non-protein component incorporated into a conjugated protein, such as a haem group containing an iron(II) ion (Fe2+Fe^{2+}).

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Haemoglobin

A conjugated quaternary globular protein consisting of four polypeptide subunits (two α\alpha and two β\beta), each containing a prosthetic haem group with an Fe2+Fe^{2+} ion to reversibly bind oxygen.

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Catalase

A quaternary enzyme containing four haem prosthetic groups that catalyses the breakdown of harmful metabolic hydrogen peroxide into water and oxygen.

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Fibrous protein

An insoluble, structurally repetitive protein consisting of long, uncoiled polypeptide chains with a high proportion of hydrophobic amino acids.

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Keratin

A fibrous protein found in hair, skin, and nails, characterised by a large proportion of the sulfur-containing amino acid cysteine forming strong, rigid disulfide bridges.

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Elastin

A fibrous protein found in elastic fibres in blood vessel walls and alveoli, formed by cross-linked tropoelastin molecules that stretch and recoil.

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Collagen

A tough, flexible fibrous structural protein consisting of three polypeptide chains wound in a triple helix, with every third amino acid being glycine.

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Nucleotide

The monomer of nucleic acids composed of a pentose sugar, a negatively charged phosphate group, and a nitrogenous base.

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Phosphodiester bond

A strong covalent bond linking the 5′5' phosphate group of one nucleotide to the 3′3' hydroxyl group of an adjacent nucleotide in a polynucleotide backbone.

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Pyrimidines

The smaller, single-carbon-ring nitrogenous bases found in nucleic acids: thymine (T), cytosine (C), and uracil (U).

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Purines

The larger, double-carbon-ring nitrogenous bases found in nucleic acids: adenine (A) and guanine (G).

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Antiparallel

The structural arrangement of DNA where the two parallel polynucleotide strands run in opposite directions (5′5' to 3′3' and 3′3' to 5′5').

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Complementary base pairing

The specific pairing rule in nucleic acids where a purine always pairs with a pyrimidine: adenine pairs with thymine via two hydrogen bonds, and cytosine pairs with guanine via three hydrogen bonds.

<p>The specific pairing rule in nucleic acids where a purine always pairs with a pyrimidine: adenine pairs with thymine via two hydrogen bonds, and cytosine pairs with guanine via three hydrogen bonds.</p>