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Biology Videos

Videos that cover the same info as notes and incorporate practice questions.

Bio Bites

Short practice questions to reinforce learning as you progress through biology.

Bio Question Bank

A resource to practice what you've learned in biology.

DAT Bootcamp practice tests 1-10

Recommended practice tests to finish and review before taking the DAT.

Carbohydrates

Used as fuel and structural support, containing carbon, hydrogen, and oxygen atoms (CHO).

Monosaccharides

Carbohydrate monomers, examples include ribose, fructose, and glucose.

Ribose

A five carbon monosaccharide.

Fructose

A six carbon monosaccharide.

Glucose

A six carbon monosaccharide.

Disaccharides

Contain two monosaccharides joined by a glycosidic bond, resulting from a dehydration reaction.

Examples of Disaccharides

Common examples include sucrose, lactose, and maltose.

Polysaccharides

Contain multiple monosaccharides connected by glycosidic bonds to form long polymers.

Starch

Form of energy storage for plants.

Glycogen

Form of energy storage in animals.

Proteins

Contain carbon, hydrogen, oxygen, and nitrogen atoms (CHON) and are made of amino acids.

Amino acids

Monomers of proteins that link together to build polypeptides.

Matter

Anything that takes up space and has mass.

Element

A pure substance with specific physical/chemical properties that cannot be broken down.

Atom

The smallest unit of matter that retains the chemical properties of the element.

Molecule

Two or more atoms joined together.

Intramolecular forces

Attractive forces that act on atoms within a molecule.

Intermolecular forces

Forces that exist between molecules and affect physical properties of the substance.

Monomers

Single molecules that can polymerize, or bond with one another.

Polymers

Substances made up of many monomers joined together in chains.

Dehydration (condensation) reaction

Creates a covalent bond between monomers and releases water.

Hydrolysis

A reaction that breaks a covalent bond using water.

Primary structure

Sequence of amino acids connected through peptide bonds.

Secondary structure

Intermolecular forces between the polypeptide backbone (not R-groups) due to hydrogen bonding. Forms α-helices or β-pleated sheets.

Tertiary structure

Three-dimensional structure due to interactions between R-groups. Can create hydrophobic interactions based on the R-groups.

Quaternary structure

Multiple polypeptide chains come together to form one protein.

Protein denaturation

Describes the loss of protein function and higher order structures. Only the primary structure is unaffected.

Storage (Protein Function)

Reserve of amino acids.

Hormones (Protein Function)

Signaling molecules that regulate physiological processes.

Receptors (Protein Function)

Proteins in cell membranes which bind to signal molecules.

Structure (Protein Function)

Provide strength and support to tissues (hair, spider silk).

Immunity (Protein Function)

Antibodies that protect against foreign substances.

Enzymes (Protein Function)

Regulate rate of chemical reactions.

Catalysts

Increase reaction rates by lowering the activation energy of a reaction.

Transition state

The unstable conformation between the reactants and the products.

Phosphatase

Cleaves a phosphate group off of a substrate molecule.

Phosphorylase

Directly adds a phosphate group to a substrate molecule by breaking bonds within a substrate molecule.

Kinase

Indirectly adds a phosphate group to a substrate molecule by transferring a phosphate group from an ATP molecule.

Feedback regulation of enzymes

Occurs when the end product of an enzyme-catalyzed reaction inhibits the enzyme's activity by binding to an allosteric site.

Competitive inhibition

Occurs when a competitive inhibitor competes directly with the substrate for active site binding.

Induced fit theory

Describes how the active site molds itself and changes shape to fit the substrate when it binds.

Ribozyme

An RNA molecule that can act as an enzyme (a non-protein enzyme).

Cofactor

A non-protein molecule that helps enzymes perform reactions.

Coenzyme

An organic cofactor (i.e., vitamins).

Inorganic cofactors

Usually metal ions.

Denaturation

The process by which protein enzymes lose their functional shape.

Optimal temperatures and pH

Conditions required for protein enzymes to function effectively.

Noncompetitive inhibition

Occurs when the noncompetitive inhibitor binds to an allosteric site that modifies the active site.

Allosteric site

A location on an enzyme that is different from the active site.

Competitive inhibition

A type of enzyme inhibition where the inhibitor competes with the substrate for the active site.

Enzyme kinetics plot

A graph used to visualize how inhibitors affect enzymes.

Lipids

Organic molecules containing carbon, hydrogen, and oxygen atoms (CHO), characterized by long hydrocarbon tails that make them hydrophobic.

Triacylglycerol (triglyceride)

A lipid molecule with a glycerol backbone and three fatty acids connected by ester linkages.

Saturated fatty acids

Fatty acids with no double bonds that pack tightly and are solid at room temperature.

Vmax

The maximum reaction velocity of an enzyme.

Michaelis Constant (KM)

The substrate concentration at which the velocity is 50% of the maximum reaction velocity.

Saturation

Occurs when all active sites are occupied, causing the rate of reaction to plateau despite increasing substrate concentration.

Unsaturated fatty acids

Fatty acids that contain double bonds, preventing tight packing and increasing membrane fluidity.

Phospholipids

Lipid molecules with a glycerol backbone, one phosphate group, and two fatty acid tails, making them amphipathic.

Cholesterol

An amphipathic lipid molecule that is a component of cell membranes and a precursor to steroid hormones.

Lipoproteins

Molecules that allow the transport of lipid molecules in the bloodstream due to an outer coat of phospholipids, cholesterol, and proteins.

Waxes

Simple lipids with long fatty acid chains connected to alcohols.

Carotenoids

Lipid derivatives containing long carbon chains with double bonds that function mainly as pigments.

Sphingolipids

Lipids with a backbone of aliphatic amino alcohols, important for structural support, signal transduction, and cell recognition.

Glycolipids

Lipids found in the cell membrane with a carbohydrate group attached instead of a phosphate group.

Nucleic acid polymerization

The process that occurs as nucleoside triphosphates are added to the 3' end of the sugar-phosphate backbone.

Nucleic Acids

Nucleic acids contain nucleotide monomers that build into DNA (deoxyribonucleic acid) and RNA (ribonucleic acid) polymers.

DNA

DNA is an antiparallel double helix, in which two complementary strands with opposite directionalities (positioning of 5' ends and 3' ends) twist around each other.

Antiparallel Strands

DNA strands run parallel to each other, but in opposite directions.

Nucleosides

Nucleosides contain a five-carbon sugar and a nitrogenous base.

Nucleotides

Nucleotides contain a five-carbon sugar, a nitrogenous base, and a phosphate group.

mRNA

mRNA is single-stranded after being copied from DNA during transcription.

Deoxyribose sugars

Deoxyribose sugars (in DNA) have a hydrogen at the 2' carbon while ribose five-carbon sugars (in RNA) have a hydroxyl group at the 2' carbon.

miRNA

Small RNA molecules that can silence gene expression by base pairing to complementary sequences in mRNA.

Phosphodiester bonds

Phosphodiester bonds are formed through a condensation reaction where the phosphate group of one nucleotide (at the 5' carbon) connects to the hydroxyl group of another nucleotide (at the 3' carbon) and releases a water molecule as a by-product.

rRNA

rRNA (ribosomal RNA): It is formed in the nucleolus of the cell and helps ribosomes translate mRNA.

dsRNA

Some viruses carry their code as double stranded RNA.

Central Dogma of Genetics

The central dogma of genetics states that information is passed from DNA → RNA → proteins.

RNA world hypothesis

The RNA world hypothesis is the theory that early life forms relied on self-replicating RNA both to store genetic information and to catalyze chemical reactions before the evolution of DNA and proteins.

Endosymbiotic theory

The endosymbiotic theory states that eukaryotes developed when aerobic bacteria were internalized as mitochondria while the photosynthetic bacteria became chloroplasts.

Modern cell theory

Modern cell theory states that all lifeforms have one or more cells, the cell is the basic structural, functional, and organizational unit of life, all cells come from other cells (cell division), and genetic information is stored and passed down through DNA.

Phosphate group

A phosphate group is part of nucleotides and is involved in forming phosphodiester bonds.

tRNA

tRNA (transfer RNA): Small RNA molecule that participates in protein synthesis.

5' end

The 5' end of a nucleic acid strand has a free phosphate group.

3' end

The 3' end of a nucleic acid strand has a free hydroxyl group.

Five-carbon sugar

A five-carbon sugar is a component of nucleotides and nucleosides.

Nitrogenous base

A nitrogenous base is a component of nucleotides and nucleosides.

Protein

Proteins largely replaced RNA in catalyzing reactions (ribozymes being a notable exception).

Metabolism

The set of life-sustaining chemical reactions in organisms.

Biochemistry

The study of chemical processes within and relating to living organisms.

Eukaryotic Cells

Cells that possess a nucleus and other organelles enclosed within membranes.

Prokaryotic Cells

Cells that do not have a nucleus or other membrane-bound organelles.

Ribosomes

Molecular machines that synthesize proteins by translating messenger RNA.

Double Membrane

A structure consisting of two lipid bilayers that surrounds certain organelles.

Integral Proteins

Proteins that are embedded in the phospholipid bilayer and can function as receptors or channels.

Transmembrane Proteins

A type of integral protein that spans the entire phospholipid bilayer.