Water, Macromolecules, Biological Membranes, Energetics, and Transport

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Comprehensive vocabulary review flashcards covering water properties, amino acid and protein structures, biological membrane fluidity and architecture, thermodynamics, ATP energetics, and cellular transport mechanisms.

38 Terms

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Polar Molecule

A molecule with an uneven charge distribution, featuring partial positive and negative regions due to differences in electronegativity, such as between hydrogen and oxygen in water.

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Hydrogen Bond

A weak bond formed between a partially positive hydrogen atom and a partially negative atom (such as oxygen or nitrogen) in another molecule; each water molecule can form up to four of these bonds.

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Hydrophilic

"Water-loving" substances that interact favorably with water, typically composed of polar or charged molecules that dissolve readily in aqueous solutions.

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Hydrophobic

"Water-fearing" substances that lack charges or partial charges; these nonpolar molecules, such as lipids and oils, fail to dissolve and aggregate in aqueous environments.

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pH

A scale ranging from 00 to 1414 measuring the concentration of hydrogen ions (H+\text{H}^+) in a solution, where 77 is neutral, below 77 is acidic, and above 77 is basic (alkaline).

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Physiological pH Range

The tightly regulated normal pH range of human blood (7.35 to 7.457.35\text{ to }7.45) that is essential for cellular homeostasis, enzyme function, and metabolism.

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<p>Amino Acids</p>

Amino Acids

The monomer building blocks of proteins, each composed of a central alpha (α\alpha) carbon bonded to an amino group (−NH2-\text{NH}_2), a carboxyl group (−COOH-\text{COOH}), a hydrogen atom, and a variable R-group (side chain).

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Peptide Bond

A covalent linkage formed through a condensation reaction connecting the carboxyl group of one amino acid to the amino group of another.

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Primary Structure

The linear sequence of amino acids in a polypeptide chain, strictly determined by the genetic information encoding the protein.

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Secondary Structure

Regular, repeating local folding patterns in a polypeptide backbone, primarily including coiled α\alpha-helices and pleated β\beta-sheets stabilized by hydrogen bonds.

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Tertiary Structure

The overall three-dimensional shape of a single polypeptide, stabilized by interactions among amino acid R-groups including hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges.

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Quaternary Structure

The arrangement and functional association of multiple individual polypeptide subunits into a single multi-subunit protein complex, such as hemoglobin.

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Disulfide Bridge

A strong covalent bond formed between the sulfhydryl (−SH-\text{SH}) groups of two cysteine residues that reinforces protein tertiary and quaternary structures.

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Sickle Cell Mutation

A specific genetic mutation in the β\beta-globin gene that substitutes valine for glutamic acid at position 66, producing abnormal hemoglobin S (HbS) that aggregates under low oxygen and deforms red blood cells into rigid sickles.

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Hydrophobic Effect

The physical phenomenon whereby nonpolar molecules or fatty acid tails aggregate together in an aqueous medium to minimize water exposure, driving membrane bilayer assembly and protein folding.

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Plasma Membrane

The selectively permeable external lipid bilayer of a cell, measuring approximately 5 to 7 nm5\text{ to }7\,\text{nm} thick, composed predominantly of phospholipids, proteins, and cholesterol (in animal cells).

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<p>Open System</p>

Open System

A thermodynamic system that exchanges both matter and energy with its surroundings, exemplified by living cells exchanging nutrients, wastes, and heat.

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<p>Phospholipid</p>

Phospholipid

An amphipathic membrane lipid consisting of a hydrophilic head (composed of glycerol, a phosphate group, and a polar group) and two nonpolar hydrophobic fatty acid tails.

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<p>Fluid Mosaic Model</p>

Fluid Mosaic Model

The model proposed in 19721972 by Singer and Nicolson characterizing the plasma membrane as a dynamic, fluid phospholipid bilayer embedded with a mosaic of mobile proteins.

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<p>Unsaturated Fatty-Acid Tails</p>

Unsaturated Fatty-Acid Tails

Hydrocarbon chains containing one or more carbon-carbon double bonds that introduce bends or "kinks," preventing tight packing and thereby increasing membrane fluidity while lowering the melting point.

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<p>Cholesterol (Membrane Buffer)</p>

Cholesterol (Membrane Buffer)

A steroid lipid constituting up to 25%25\% of animal cell membranes that buffers fluidity by restraining phospholipid motion at higher temperatures and preventing rigid packing at colder temperatures.

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<p>Integral Membrane Protein</p>

Integral Membrane Protein

A membrane protein containing both hydrophobic and hydrophilic domains that penetrates or completely spans the hydrophobic core of the lipid bilayer.

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Peripheral Membrane Protein

A membrane protein lacking exposed hydrophobic groups that does not enter the bilayer core, attaching loosely to the exterior or interior membrane surface.

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First Law of Thermodynamics

The principle of energy conservation stating that energy cannot be created or destroyed, only transferred or transformed from one form to another.

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Second Law of Thermodynamics

The principle stating that natural processes always increase the entropy (disorder or randomness) of a system and its surroundings over time.

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<p>Adenosine Triphosphate (ATP)</p>

Adenosine Triphosphate (ATP)

The primary energy currency of the cell, composed of the nitrogenous base adenine, a ribose sugar, and three negatively charged phosphate groups whose terminal high-energy bond powers cellular work.

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Phosphorylation

The enzymatic transfer of a high-energy phosphate group from ATP to another molecule, which induces conformational activation to drive mechanical, transport, or chemical work.

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<p>Cell Transport</p>

Cell Transport

The organized systems of cellular movement categorized into passive transport (simple diffusion, osmosis, facilitated diffusion) and active transport (carrier pumps and bulk vesicle transport).

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Selective Permeability

The property of the plasma membrane allowing nonpolar substances (O2\text{O}_2, CO2\text{CO}_2) to diffuse easily while restricting large polar compounds (glucose) and charged ions (Na+\text{Na}^+, Cl−\text{Cl}^-).

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Simple Diffusion

The passive transport of solute particles directly through the lipid bilayer down their concentration gradient (from high to low concentration) until dynamic equilibrium is reached.

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Osmosis

The passive net movement of water molecules across a selectively permeable membrane from an area of lower solute concentration (higher free water) to an area of higher solute concentration (lower free water).

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Facilitated Diffusion

Passive transport down a concentration gradient aided by transmembrane channel or carrier proteins that shield polar or charged solutes from the membrane's hydrophobic core without consuming ATP.

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Primary Active Transport

Transport that directly consumes ATP to phosphorylate a carrier protein, driving molecules across the membrane against their established concentration gradient.

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Sodium-Potassium Pump (Na+/K+\text{Na}^+/\text{K}^+ Pump)

An electrogenic primary active transport pump that uses ATP to export 3 Na+3\,\text{Na}^+ ions and import 2 K+2\,\text{K}^+ ions against their concentration gradients in animal cells.

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Secondary Active Transport

A transport process in which the movement of a substance against its gradient is powered by the potential energy stored in an electrochemical ion gradient created by primary active transport.

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Endocytosis

The active, vesicle-mediated bulk transport process by which cells invaginate their plasma membrane to engulf external fluids, solutes, or particles into the cytoplasm.

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Exocytosis

The active bulk transport mechanism where membrane-bound secretory vesicles fuse with the plasma membrane to release hormones, neurotransmitters, or cellular waste into the extracellular fluid.

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Familial Hypercholesterolemia

A genetic disorder resulting from defective cell surface LDL receptors that impairs receptor-mediated endocytosis of cholesterol, producing elevated low-density lipoprotein levels in the blood.