Introductory Biology: Macromolecules, Chemistry of Life, and Cell Structure

0.0(0)
Studied by 0 people
call kaiCall Kai
Locked
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/31

flashcard set

Earn XP

Description and Tags

Vocabulary practice flashcards covering chemical bonding, characteristics of life, water properties, macromolecule classes, and cell membrane structures from BIOL 1124 lectures.

Last updated 2:31 AM on 9/2/26
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai
Chat

No analytics yet

Send a link to your students to track their progress

32 Terms

1
New cards

Atom

The smallest chemical unit of a type of pure substance (element).

2
New cards

Molecule

A chemical structure consisting of two or more atoms held together by chemical bonds.

3
New cards

Cell

The fundamental unit of life.

4
New cards

Homeostasis

The process of maintaining a state of internal biological equilibrium, such as temperature, water, pH, and sugar levels.

5
New cards

Covalent Bond

An intra-molecular chemical bond formed when atoms share electrons.

6
New cards

Nonpolar Covalent Bond

A covalent bond in which bonding electrons are shared equally between two atoms, resulting in no charges on the atoms.

7
New cards

Polar Covalent Bond

A covalent bond in which bonding electrons are shared unequally between two atoms, resulting in partial positive (δ+\delta+) and partial negative (δ\delta-) charges.

8
New cards

Ionic Bond

A chemical bond formed by the complete transfer of one or more valence electrons, creating ions of opposite charges that attract each other.

9
New cards

Hydrogen Bond

A weak inter-molecular attraction formed between the partial charges of polar molecules.

10
New cards

Oxidation

The loss of an electron by an atom or molecule during a chemical reaction.

11
New cards

Reduction

The gain of an electron by an atom or molecule during a chemical reaction.

12
New cards
<p>Types of Chemical Bonds Diagram</p>

Types of Chemical Bonds Diagram

A diagram comparing a nonpolar covalent bond (equal sharing), a polar covalent bond (unequal sharing), and an ionic bond (complete electron transfer).

13
New cards
<p>Redox Reaction Diagram</p>

Redox Reaction Diagram

An illustration showing oxidation as the loss of an electron and reduction as the gain of an electron.

14
New cards

Hydrophilic

Water-loving; descriptive of polar molecules and charged ions that dissolve easily in water.

15
New cards

Hydrophobic

Water-fearing; descriptive of nonpolar, uncharged molecules (such as fats and waxes) that do not dissolve in water.

16
New cards

Monomer

A small, single molecular subunit that can bind to other subunits to form a polymer.

17
New cards

Polymer

A large molecule consisting of linked, repeating monomer subunits.

18
New cards

Dehydration Synthesis

A condensation reaction that joins monomers together by releasing a molecule of water (H2OH_2O).

19
New cards

Hydrolysis Reaction

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

<p>A chemical reaction that cleaves polymers into monomers by adding a molecule of water ($$H_2O$$).</p>
20
New cards

Monosaccharide

The monomer of carbohydrates, containing a carbon backbone (usually a ring), which functions as the most common metabolic fuel for life.

21
New cards

Polysaccharide

A carbohydrate polymer formed by connecting multiple monosaccharides together end-to-end.

22
New cards

Polypeptide

A linear chain of amino acids linked together by peptide bonds.

23
New cards

Protein

A functional macromolecule consisting of one or more polypeptides folded and shaped in a specific 3D structure.

24
New cards

Amino Acid

The monomer of proteins, consisting of a core structure and a unique R group that determines its chemical behavior.

25
New cards

Protein Structure Levels

The four structural levels of a protein: primary (amino acid sequence), secondary, tertiary, and quaternary structure.

<p>The four structural levels of a protein: primary (amino acid sequence), secondary, tertiary, and quaternary structure.</p>
26
New cards

Hydrophobic Exclusion

The process by which a polypeptide folds in water to minimize exposure of nonpolar R-groups, hiding them inside the protein structure.

27
New cards

Denaturation

The disruption of weak hydrogen bonds in a protein caused by factors like heat, protons (H+H^+), or hydroxides (OHOH^-), altering its structure and eliminating its function.

28
New cards

Lipid

A diverse class of organic molecules (including fats, oils, waxes, and steroids) that are at least partially hydrophobic and composed of sub-units such as heads and fatty acid tails.

29
New cards

Nucleic Acid

A class of organic macromolecules (such as DNA and RNA) made of nucleotide monomers that store genetic information.

30
New cards

Phospholipid Bilayer

A membrane structure composed of two layers of phospholipids, with polar hydrophilic heads contacting water and nonpolar hydrophobic tails oriented inward.

<p>A membrane structure composed of two layers of phospholipids, with polar hydrophilic heads contacting water and nonpolar hydrophobic tails oriented inward.</p>
31
New cards

Amphipathic Molecule

A molecule (such as a phospholipid) containing both hydrophilic (polar) and hydrophobic (nonpolar) regions.

32
New cards

Transmembrane Protein

An integral membrane protein that spans the lipid bilayer, featuring hydrophobic regions contacting fatty acid tails and hydrophilic regions contacting aqueous surroundings.