Protein Structure, Enzymes, Nucleic Acids, and Cell Biology

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Comprehensive vocabulary flashcards covering the structural hierarchy of proteins, enzyme kinetics, nucleic acids (DNA/RNA/ATP), cellular organelles, and plasma membrane dynamics from the lecture.

Last updated 5:38 AM on 10/14/26
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35 Terms

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Dehydration synthesis

A chemical reaction that combines two amino acids together to form a peptide bond while releasing a molecule of water.

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Dipeptide

A molecule formed by two amino acids connected together by a peptide bond.

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Polypeptide

A polymer chain consisting of over 5050 amino acids linked by peptide bonds.

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Hydrolysis reaction

A reaction that breaks a peptide bond by adding back a hydrogen atom from water to one amino acid and an oxygen and hydrogen atom to the other amino acid.

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Primary structure

The linear sequence or unfolded chain of amino acids linked together by peptide bonds.

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Secondary structure

The structural level formed by folding or winding an amino acid chain into corkscrew-shaped alpha helices or antiparallel beta pleated sheets, stabilized by hydrogen bonds.

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Tertiary structure

The third-order three-dimensional folding of a polypeptide into a functional globular protein.

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Quaternary structure

A fourth-order structural level that forms when two or more individual proteins or subunits combine, such as hemoglobin or transthyretin.

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Transthyretin

A functional transport protein made of four identical subunits that moves thyroid hormone (thyroxine) through blood and cerebrospinal fluid.

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Fibrous proteins

Stable, strand-like, water-insoluble structural proteins that provide mechanical support and tensile strength, such as collagen, keratin, and elastin.

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Globular proteins

Compact, spherical, water-soluble functional proteins possessing active sites that are sensitive to environmental shifts in temperature and pH.

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Denaturation

The process where a globular protein unfolds and loses its functional three-dimensional shape and active sites due to decreased pH or increased temperature.

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Enzyme

A globular protein that acts as a biological catalyst to increase reaction speed by lowering the required activation energy without being consumed.

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Apoenzyme

The large protein portion of a functional holoenzyme.

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Cofactor

A small helper component needed by an enzyme to function, which can be a metal ion like iron or an organic coenzyme such as a vitamin.

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Substrate

The specific chemical target that interacts temporarily with an enzyme's active site to undergo a reaction.

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Induced fit model

The model of enzyme action where the enzyme and substrate cause each other to bend upon binding to force a chemical reaction to occur.

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Nucleotide

The monomer building block of nucleic acids, consisting of a nitrogenous base, a five-carbon pentose sugar, and a phosphate group (PO4−2\text{PO}_4^{-2}).

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Purines

The larger class of nitrogenous bases composed of two linked rings of atoms, specifically adenine and guanine.

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Pyrimidines

The smaller class of nitrogenous bases composed of a single ring of atoms, including cytosine, thymine (in DNA), and uracil (in RNA).

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Complementary base pairing

The specific bonding rule in nucleic acids where adenine pairs with thymine via hydrogen bonds, and guanine pairs with cytosine.

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Adenosine triphosphate (ATP)

An adenine-containing RNA nucleotide bonded to three phosphate groups that provides usable energy when its high-energy terminal phosphate bond is broken.

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Phosphorylation

The process of transferring a phosphate group, typically from ATP, onto another chemical compound or protein to add energy or change its activity.

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Fluid mosaic model

A model of the plasma membrane describing it as a dynamic, semi-solid lipid bilayer containing floating proteins whose fluidity is regulated by cholesterol.

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Glycocalyx

A carbohydrate-rich sugar coating on the outer surface of the plasma membrane, made of glycolipids and glycoproteins, that serves as a biological marker for cell recognition.

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Integral proteins

Membrane proteins firmly inserted into the lipid bilayer, typically spanning both layers as transmembrane proteins with hydrophobic and hydrophilic regions.

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Peripheral proteins

Proteins that are not embedded in the lipid bilayer but are attached to the inner or outer surfaces, often hanging off integral proteins.

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Tight junctions

Impermeable cell junctions formed by fused integral proteins of adjacent cell membranes that prevent fluids and molecules from leaking between cells.

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Desmosomes

Anchoring junctions consisting of plaques, cadherin linker proteins, and keratin filaments that act like molecular Velcro to distribute tension and prevent tissues from tearing.

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Gap junctions

Communicating junctions formed by transmembrane protein tunnels called connexons that allow ions and small molecules to pass directly from cell to cell for electrical coordination.

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Rough endoplasmic reticulum (RER)

A network of intracellular chambers attached to the nucleus and studded with ribosomes that serves as a site for protein manufacturing.

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Golgi apparatus

A cellular organelle of membranous chambers that processes and packages proteins and other molecules into vesicles for transport or exocytosis.

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Mitochondria

Double-membraned organelles with folded inner membranes that utilize glucose and oxygen to synthesize ATP.

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Peroxisomes

Membranous cellular sacs containing chemicals that neutralize dangerous metabolic byproducts known as free radicals.

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Lysosomes

Membranous bubbles containing digestive chemicals that fuse with and destroy cellular debris or materials inside the cell.