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FREE AP Biology Unit 1 Study Guide

PRE-KNOWLEDGE

  • Atom: the smallest unit of matter

    • Contains:

      • protons (+ charge)

      • neutrons (0 charge)

      • electrons (- charge)

    • Note: electrons are of a much smaller size than protons or neutrons. Neutrons are slightly bigger than protons.

  • Element: a substance made up of only one type of atom

    • In a periodic table, it is expressed with:

      • Atomic number: expresses the number of protons that an element contains (remains the same ALL the time)

      • Chemical Symbol (abbreviation of the first two letters or Latin root name)

      • Element Name

      • Atomic weight

    • NOTE: Even when the number of neutrons or electrons changes, the number of protons is always consistent within the same element.

  • Isotope: a version of an element that contains a different number of neutrons

  • Ion: a group of atoms that has a charge

    • Anion: an ion with a negative net charge → more electrons than protons

    • Cation: an ion with a positive net charge → more protons than electrons

  • Chemical Bonds:

    • [Kaylyn's Analogy: BULLY IS TAKING UR FOOD] 

    • Ionic Bond: a bond between oppositely charged ions

      • One atom gives up its electron to give to another atom

      • Essentially, everyone wants to maintain their perfect octet structure, and the different elements are doing what is most CONVENIENT and EFFICIENT to them to

    • [Kaylyn's Analogy: SHARING IS CARING] 

    • Covalent Bond: a chemical bond formed when electrons are SHARED between two atoms

  • Molecule: a group of 2 or more atoms that are COVALENTLY bonded together

  • Chemical: a substance with a definite composition → able to determine all of its properties and characteristics

  • Compound: a substance of 2 or more different elements that have been chemically joined

  • Valence Electrons: electrons on the outer shell of the atom

  • Polar: molecule has unequal charge

  • Non-Polar: molecule has evenly spread charge


TOPIC 1.1 - All about water

  • Water’s Characteristics

    • 1 electronegative oxygen atom (it likes to hog electrons) and 2 hydrogen atoms that want to get rid of one valence electron to complete a set

    • The oxygen molecule and the hydrogen molecules are connected by COVALENT BONDS (bonds where multiple molecules share electrons)

    • The different water molecules are connected by HYDROGEN BONDS (bonds that form because of the slight polarity of water molecules)

      • There is a partial NEGATIVE charge at the oxygen, a partial POSITIVE charge at the hydrogens - this causes the negative ends to be attracted to the positive ends (and vice versa)

    • Hydrophillic molecules LOVE water, hydrophobic molecules DO NOT (oils and fats)

  • Water’s Properties

    1. Cohesion: all water molecules move with each other

      1. The reason for water having a high surface tension (the little bubble cover you see on top of the water’s surface)

    2. High Surface Tension: resistance of water’s surface to rupture when placed under tension (like a bug or a paper clip)

      • Reasoning: the water molecules on the surface of the water have no molecules pulling them from above, so ****they are more attracted to each other (COHESION) than the AIR.

      • The surface contracts to the smallest possible surface area as a result of this attraction

      • ex) water droplets, insects gliding on water

    3. High Heat Capacity

      • heat capacity: the amount of heat needed for 1 gram of water to increase by 1°C

      • If the heat capacity is high, it means that it needs lots of heat for water to increase → makes the overall temperature of an environment or organism very stable, won’t constantly change because of some extra heat → MINIMIZES TEMP VARIATIOn

    4. High heat of vaporization

      • heat of vaporization: the amount of energy needed to change 1 gram of liquid water to its gas form at a constant temp.

      • if the heat of vaporization is high, it means it needs a lot of energy to change from liquid to gas → to regulate temperature and avoid overheating

    5. Adhesion: water’s ability to stick to other surfaces

      • responsible for most of capillary action and transpiration

      • transpiration: the process by which evaporation + cohesion + adhesion pulls up water in plants

      • ex) water can travel up the xylem in trees

    6. UNIVERSAL SOLVENT: able to dissolve POLAR molecules quickly

      • Reasoning: a water molecule has a slight polarity, which is why it can form ionic bonds (bonds that take another’s electrons) with other polar molecules

      • ex) mix salt in water

    7. Density as a solid

      • GAS: water molecules are spread apart

      • LIQUID: water molecules are close together → hydrogen bonds are easily broken apart

      • SOLID: water molecules form a crystal structure → hydrogen bonds are stable

        • Because the density of ice is LESS than the density of liquid water, it allows aquatic life to survive during the winter because the lake will freeze from TOP-BOTTOM, instead of BOTTOM-UP.

        • This is also the reason why ice floats (a substance floats of it is less dense than other components in the mixture)

    8. CAPILLARY ACTION and MENISCUS

      1. Capillary action: Cohesion + Adhesion in action

        1. attraction between water molecules (cohesion) enables the water molecules to move as a group

        2. The surface tension allows the surface to be intact

        3. attraction between water and container (adhesion) enables the water to go up

      2. RESULT: a concave meniscus

      3. examples)

        • dip a paper towel in water and the water climbs up the towel

        • roots carry water from the soil to the plant

        • tear ducts carry tears to the eye

  • Difference between covalent vs. hydrogen bonds

    • Covalent bonds are WITHIN one water molecule (between the oxygen and 2 hydrogens)

    • Hydrogen bonds exist with different water molecules (as the partially positive ends connect with the partially negative ends)


TOPIC 1.2 - ELEMENTS OF LIFE

  • The only elements you need to know: CHONPS

    • Carbon - central element

    • Hydrogen - used in energy exchange (NAD+, NADH in cellular respiration), used to create energy gradients, standard for acidity/alkalinity (acids vs. bases)

    • Nitrogen - nitrogen cycle

    • Oxygen - photosynthesis + cellular respiration

    • Phosphorus - in ATP

    • Sulfur

  • 4 Macromolecules’ Elemental Composition

    • Nucleic Acids: Nitrogen, oxygen, carbon, phosphorus, hydrogen [CHONP]

    • Proteins: Nitrogen, oxygen, carbon, hydrogen, sulfur [CHONS]

    • Carbohydrates: Oxygen, carbon, hydrogen [CHO]

    • Lipids: Oxygen, carbon, hydrogen, phosphorus [CHO (P)]


TOPIC 1.3

  • Monomer: a building block for polymers

  • Polymer: a large molecule made of repeating subunits (monomers) → with specific 3D shapes and functions

    • Like a LEGO CASTLE!

  • Dehydration synthesis - ENZYMES combining monomers to create polymers

    • also called “condensation reaction”

    • Dehydration: because water is the waste product of the reaction

    • Synthesis: because we are combining two molecules into one

    • ENZYMES run this reaction

      • enzymes pull a hydroxyl group off of one monomer and pull a hydrogen out of the other monomer → AKA creates H20 and pulls it out

      • This creates a COVALENT BOND between the two molecules to SHARE ELECTRONS

  • Hydrolysis - ENZYMES breaking down polymers into monomers

    • Reactions that end with “lyse” have to do with breaking down something

    • Enzymes insert a water molecule between the two monomer components and this breaks the bond that held the two monomers together

  • Functional Group: a group of atoms that provide a particular function or characteristic when it is present in another molecule

    • Hydroxyl [OH]: Polar, hydrophilic

    • Carbonyl [C=O]: Polar, hydrophilic → increases solubility (ability to dissolve in a solvent) of water

    • Carboxyl [COOH]: Polar, hydrophilic

      • acidic → likes to donate their hydrogen ions (H+) → becomes COO-

      • essential in amino acids

    • Amine group [NH2]: Polar, hydrophilic

      • Basic → wants to gain another hydrogen ion

      • essential in amino acids

    • Phosphate group [PO43-]: polar, hydrophilic

      • acidic → wants to lose hydrogen ions

      • Key for energy exchange in ATP (adenosine triphosphate) → addition or removal of phosphate is used to store or release energy

        • phosphorylation/dphosphorylation

    • Sulfhydryl group [SH]: polar, hydrophilic

      • likes to form bonds with other sulfhydryl molecules → this forms a disulfide bridge, which is important in protein structure and folding

    • Methyl group [CH3]: nonpolar and hydrophobic

      • DNA methylation → methyl group is used to turn off genes

      • appears in phospholipid tails

    • Acetyl: used to activate DNA (opp of methyl)

NOTE: ALL macromolecules are composed of monomers that have already gone through dehydration synthesis to form those large, complex molecules.


TOPIC 1.4

  • Macromolecule: a large, organic molecule

  • 4 Different types of macromolecules/biomolecules: carbohydrates, lipids, proteins, nucleic acids

    • Lipid: hydrophobic → phospholipid bilyaer

    • Nucleic Acid: DNA and RNA

    • Carbohydrate: ends with “—ose”

    • Protein: peptide bonds

  • 4 Major Macromolecules’ Characteristics

  • Carbohydrates

    NOTE: all carbohydrates end with “—ose”

    • Name analysis

      • Carbo: 6 carbons

      • Hydrate: same ratio of oxygen: hydrogen as the ratio of oxygen: hydrogen in water (1 oxygen: 2 hydrogens)

      • Alternative name: Saccharide = Greek word for sweet 🍭 because glucose tastes sweet

    • What does it contain?

      • one carbon atom to one water molecule

    • [MONOMER OF CARBOHYDRATES] Monosaccharides: “one sugar”

      • Function) energy source and building blocks for more complex sugar structures

      • The most common form → exactly one carbon atom for each H20 molecule (with around 3-7 carbon atoms in total)

        • Most oxygen atoms are found in hydroxyl form (OH), one is part of a carbonyl (C=O) group

      • They can be in RING-shaped form or LINEAR chain → alpha (opposite sides) and beta form (same side)

      • Named based on # of carbons

        • Trioses (3 carbons)

        • Pentoses (5 carbons)

        • Hexoses (6 carbons)

      • ISOMER: having the same chemical formula, but different atom configuration

        • Glucose (6-carbon sugar)

        • Galactose: sugar found in milk - a stereoisomer of glucose (atoms are bonded in the same order, but different 3D organization)

        • Fructose: sugar found in fruit - a structural isomer of glucose and galactose (atoms are bonded in a different order)

    • Disaccharides: two monosaccharides join together through dehydration synthesis (release a water molecule and form a covalent bond known as GLYCOSIDIC LINKAGE)

      • Function) energy transfer

      • Examples:

        • Lactose (the sugar in milk) combination of glucose and galactose

          • Lactase: the enzyme that hydrolyzes lactose into monosaccharides → which mammals create when they are still drinking their mother’s milk because they need to be able to digest the milk. However, when you are an adult, most mammals don’t produce lactase because they don’t need to drink milk anymore.

          • Yet, because some human groups had access to milk products even when they were adults, this created groups that were able to have lactase persistence (continuing to produce lactase even through adulthood).

        • Maltose (malt sugar) - two glucose molecules

        • Sucrose (table sugar) - glucose and fructose

    • Polysaccharides: a long chain of monosaccharides linked by glycosidic bonds

      • Function) energy storage and structure

      • Examples of energy storage)

        • Starch - a stored form of sugar in plants

          • a combination of two polysaccharides - amylose and amylopectin

          • amylose: chains of glucose monomers

          • amylopectin: mostly glucose monomers

          • [DIGESTING CELLULOSE] Most animals cannot break down (hydrolyze) the bonds connecting the glucose monomers in cellulose (because we don’t have the enzymes that will actually use it for energy). A few animals (termites or ruminants) have symbiotic relationships with microorganisms that can convert cellulose into glucose.

          • On the other hand, starch has different bonds, which is why humans can digest it more easily.

        • Glycogen - storm form of sugars in HUMANS and other VERTEBRATES

          • A polymer of glucose monomers

          • Stored in liver and muscle cells

          • When blood glucose levels decrease, glycogen is broken down through hydrolysis

      • Examples of structure

        • Cellulose - the substance that cell walls are made up of

          • glucose monomers by 1-4 glycosidic bonds

          • Beta glycosidic linkages → cannot be digested by humans

          • [DIGESTING CELLULOSE] Most animals cannot break down (hydrolyze) the bonds connecting the glucose monomers in cellulose (because we don’t have the enzymes that will actually use it for energy). A few animals (termites or ruminants) have symbiotic relationships with microorganisms that can convert cellulose into glucose.

          • On the other hand, starch has different bonds, which is why humans can digest them more easily.

          • Hydrophilic → wants to go outside

          • Adenine and guanine are two-ringed → purine

          • Cytosine and thymine are single-ringed → primidine

          • partial - charge at nitrogen, partial + charge at hydrogen

          • partial - charge at oxygen, partial + charge at hydrogen

          • So, this forms a hydrogen bond

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

        • Chitin - the substance for the exoskeleton of insects

          • resembles cellulose, made up of glucose and nitrogen

  • Lipids

    • Need to be WHOLLY or PARTLY nonpolar (hydrophobic)

    • Note composed of REPEATING monomers → they have monomers though…

    • Functions

      • Fats/Oils: energy storage

      • Waxes: waterproofing

      • Phospholipid: membrane formation

      • Steroid: signaling hormones

    • Phospholipid

      • Hydrophobic/nonpolar tail

      • Hydrophillic/polar head

        • Head and tail connected by glycerol

      • When they are in water, the heads interact with water and the tails avoid water

    • Names: triglycerides (fats/oils), triacylglycerol

      • Fatty acid

        • Fatty: bc the carbon chain is hydrophobic

        • Acid: bc there is a carboxyl group (that is acidic)

      • Glycerol: 3 carbon chain, each with an OH group → sugar alcohol (because it has a hydroxyl group)

      • 3 Acyl groups: a carbonyl group that is bonded to another chain

      • Bond between these two through dehydration synthesis → forms covalent bonds together also releasing 3 water molecules

    • Saturated fats

      • no double bonds between carbons

      • “saturating the fat with as many hydrogens as possible”

      • solid at room temperature → relatively dense

      • ex) butter

    • Unsaturated fats

      • not as many hydrogens as possible

      • keeps the molecules from being dense → typically liquid at room temperature

      • Monounsaturated fat → only 1 double bond between carbons

      • Polyunsaturated fat → multiple double bonds between carbons

    • Trans fats: “unhealthy”

      • “cis configuration”

      • “trans configuration” → not found in nature, where you saturate the unsaturated fats with more hydrogen but not enough to be a saturated fat, trans bonds

TOPIC 1.5

  • CENTRAL DOGMA: the process of creating proteins goes from DNA to RNA to protein

  • DNA replication, transcription, translation

    DNA REPLICATION

    • Location:

      • Eukaryotic cell → nucleus

      • Prokaryotic cell → not in nucleus

    • When: before cell division (mitosis/meiosis) → interphase

    • Players: many enzymes that ends in “ase” → speed up reactions

      • Helicase: unzipping enzyme → breaks the hydrogen bonds that holds the bases together

      • DNA Polymerase: replicates the DNA molecules

      • Primase: tells the DNA polymerase where to start working by creating the primer (made up of RNA)

      • Ligase: glues the DNA fragments together

    • Process

      • Starts at the Origin → helicase unwinds the DNA

        • the SSB (single-stranded binding proteins) keep the two strands separated

        • the topoisomerase prevents the DNA from supercoiling

      • Primase creates the RNA primers on both strands

      • DNA polymerase builds the new strands in the 5’ to 3’ direction [leading strand]. Hence, the 3’ to 5’ direction has to constantly try and keep up with the unwinding. This strand is called the lagging strand, where primers have to keep being placed.

        • Fragments = “OKAZAKI fragments”

        • The ligase seals the gaps between the okazaki fragments

    • Semi-conservative: each copy contains one original strand and one new strand

    TRANSCRIPTION → change one form of something into another form

    • Location: nucleus

    • Process

      • DNA is unzipped by the RNA polymerase at the promoter (the marker that indicates where the RNA polymerase should attach to the DNA strand)

      • The RNA polymerase “reads” the DNA’s bases and creates complementary pairs. [This time, thymine is replaced with uracil. Everything else stays the same].

        • DNA - 3 prime to 5 prime

        • Messenger RNA - 5 prime to 3 prime direction

      • This forms an mRNA (messenger RNA) strand, which is then sent out of the nucleus and into the cytoplasm.

    TRANSLATION → translating RNA nucleotides into chain of amino acids

    • Location: cytoplasm/ribosome

    • Process

      • The tRNA strands reads the mRNA’s bases in threes. Certain tRNA strands bind to the mRNA if they are complementary.

        • Transfer RNA strands are just floating in the cytoplasm; they have an amino acid attached to them)

      • One comes and leaves an amino acid behind, another tRNA comes and leaves an amino acid behind, etc. → a long chain of amino acids

      • Continues until the stop codon indicates that the polypeptide (chain of long amino acids) is complete

    MORE BACKGROUND INFO

    • What is an acid vs. a base?

      • Essentially, solutions are classified as acid/base based on their hydrogen ion concentration relative to pure water

      • Acid: a cation

        • contains a high concentration of hydrogen ions (H+), greater than pure water → wants to increase the concentration of H+ in a solution by donating one of its hydrogen atoms

        • pH lower than 7 → acidic

      • Base: an anion

        • contains a low concentration of hydrogen ions, less than pure water → wants to decrease the concentration of H+ in a solution by providing a molecule that removes hydrogen ions

        • pH above 7 → basic (alkaline)

      • pH: the hydrogen ion concentration in a solution

        • 0-14 (nothing lower or higher)

      • Neutral pH: 7 (the pH of water)

    • What is deprotonation vs. protonation?

      • Deprotonation: removal of H+

      • Protonation: addition of H+

    • How do you number carbon?

      • Note: the numbering for the carbon always pertains to the SUGAR portion of the nucleotide

      • for DNA: either 5’ to 3’ OR 3’ to 5’

      • Sugar of DNA has carbons → the carbons on the sugar are numbered right AFTER the oxygen in a CLOCKWISE direction

      → 5’ to 3’

      → 3’ to 5’

  • Proteins: macromolecules made out of amino acids

    • Amino acids: monomers of proteins

      • Involved in the translation process to create proteins to serve different functions to survive

      • 20 common amino acids

      • Name Analysis

        • Amino: it contains an AMINE functional group

        • Acid: it contains a carboxyl functional group → carboxyl is acidic (wants to donate its protons)

      • ALL amino acids have an alpha carbon (central carbon) that has a covalent bond with:

        • 1) Amine group

        • 2) Carboxyl group

        • 3) 1 hydrogen atom

        • 4) R group - can be polar, non-polar, acidic, basic, etc.


      • The difference is in the 4th covalent bond with a side chain → AKA called R GROUPS

        • These side chains determine the behavior/shape of the proteins (how they fold, interact with the environment, etc.)

          • No polarity → Hydrophobic → want to enter inside of the protein

          • Polarity → Hydrophilic → want to be outside of the protein

      • How do the amino acids connect? → through peptide bonds

        • Dipeptide: the smallest chain, a molecule with 2 amino acids connected by 1 peptide bond

        • Polypeptide: chains of amino acids → can eventually become a protein or a part of a protein

    • Primary Str: a sequence of the polypeptide (chain of amino acids connected by peptide bonds, created by ribosomes during translation/protein synthesis)

      • Linear chain

    • Secondary Str: interactions involving the polypeptide’s backbone

      • in 3D form

      • interactions between carbonyl groups and amino groups → through dehydration synthesis, they form hydrogen bonds and they create a particular shape


      • Two common forms

        • alpha helix → corkscrew shape

        • beta-pleated sheets → if the parts of the polypeptide chain is parallel or antiparallel


    • Tertiary Str: interactions between amino acid side chains (R groups)

      • The overall shape is determined by the R group in the amino acids (aka the SIDE CHAINS)

        • The R group determines the characteristics of the amino acids, so this also determines the folding/shape of the protein

      • New ingredients)

        • Hydrogen bonds

        • Ionic bonds

        • Covalent bonds

        • Hydrophobic clustering

          • If the R group is hydrophobic, that amino acid will try to get away from water by going inside

          • Hydrophilic → wants to go outside

          • Adenine and guanine are two-ring → purine

          • Cytosine and thymine are single-ringed → primidine

          • partial - charge at nitrogen, partial + charge at hydrogen

          • partial - charge at oxygen, partial + charge at hydrogen

          • So, this forms a hydrogen bond

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

    • Quaternary Structure: interactions between multiple folded tertiary polypeptides


TOPIC 1.6

  • Nucleic acids: macromolecules made out of nucleotides

    • DNA: genetic material found in living organisms → MOLECULE OF HEREDITY

      • Location:

        • Eukaryotes → nucleus

        • Prokaryotes → nucleoid (special cell region)

      • NAME

        • Deoxyribonucleic acid → It is a nucleic acid because it is found in the nucleus of eukaryotes

        • Deoxyribose → comes from the deoxyribose sugar

          • Deoxyribose sugar is 5-carbon sugar that, typically, takes on a pentagonal/ring-like structure

      • Acid → considered an acid because each nucleotide contains a phosphate group

      • What is a nucleotide?

        • Basic building block of nucleic acid

        • Contains 1 sugar group, 1 phosphate group, 1 nitrogenous base

          • Nitrogenous base pairs (adenine, thymine, guanine, cytosine)

          • Adenine and guanine are two-ring → purines

          • Cytosine and thymine are single-ringed → primidine

          • partial - charge at nitrogen, partial + charge at hydrogen

          • partial - charge at oxygen, partial + charge at hydrogen

          • So, this forms a hydrogen bond

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

          • A phosphate group (makes it an acid)

          • A sugar group (deoxyribose sugar)

        • Connected to other nucleotides

        • Note: the nitrogenous bases are connected via HYDROGEN BONDS

          • Nitrogen wants to gather hydrogen protons because it is electron-negative.

          • Nitrogen is electronegative, so when nitrogen bonds with a hydrogen

          • partial - charge at nitrogen, partial + charge at hydrogen

          • partial - charge at oxygen, partial + charge at hydrogen

          • So, this forms a hydrogen bond

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

          • Oxygen is also electronegative

          • partial - charge at oxygen, partial + charge at hydrogen

          • So, this forms a hydrogen bond

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

        • Note: the phosphate and sugar groups are connected by phosphodiester linkages

      • What does DNA contain?

        • Chains of nucleotides

      • What is the DNA structure?

        • Double helix structure - like a twisted ladder with rungs consisting of the nucleotide/nitrogenous bases, the backbone consists of the sugar and phosphate

        • The two strands are considered complementary because they match perfectly with each other and form a helix together

      • Anti-parallel structure of DNA

        • The direction of the deoxyribose sugars is different for left and right ladders

        • Count the carbons after the oxygen in a clockwise direction

        • Left side: 5’ to 3’ direction

        • Right side: 3’ to 5’ direction

    • RNA

      • Properties

        • Single-stranded

        • Ribose, a nitrogenous base, and a phosphate group

      • Functions

        • Some viruses use RNA as their “genetic material”

        • Information transfer

        • It can act as an enzyme to catalyze reactions

      • ATP is RNA’s monomer

      • What is the RNA structure?

        • Just add a hydroxyl group to all of the deoxyribose sugars on the left-hand side only because RNA tends to be SINGLE-STRANDED

        • The nitrogenous bases are slightly different, but JUST LIKE DNA, they all have NUCLEOTIDES [nitrogen-containing ring (nitrogenous base), a five-carbon sugar, and at least one phosphate group)

          • Adenine, guanine, cytosine, and uracil (in place of thymine)

          • Get rid of the methyl group from thymine to make uracil

          • Why uracil? → evolution theory that it came before thymine (which is like an upgraded version LOL)

      • Different types of RNA

        • Messenger RNA (mRNA) - serves as a messenger between DNA and ribosomes by being a copy of a strand of DNA

          • Then, the ribosome reads the mRNA’s nucleotides in groups of three (called CODONS) to create a complementary strand.

        • Ribosomal RNA (rRNA) - helps mRNA bind in the right spot at the ribosome so that its nucleotides can be read, and also helps create bonds that link amino acids

        • Transfer RNA (tRNA) “CARRIERS” - involved in protein synthesis, for bringing the amino acids to the ribosome for protein synthesis

    • NUCLEOTIDES

      • Nitrogenous bases

        • Adenine and guanine - purines (structures contain two fused carbon-nitrogen rings)

        • Cytosine and thymine - pyrimidines (a single carbon-nitrogen ring)

      • Sugars (slightly different for DNA and RNA): both 5-carbon sugars

        • Deoxyribose: "deoxy" = lacking one oxygen

        • Ribose: has an oxygen atom

      • Phosphate

        • In DNA and RNA, each nucleotide has one phosphate group

    • POLYNUCLEOTIDE CHAINS

      • Has directionality → two ends go in different directions

      • DNA goes from 5’ to 3’

      • When a new nucleotide is attached through the sugar ends, the bond is called a phosphodiester linkage

EXTRA VOCAB

  • Amphiphatic molecules: having both polar and nonpolar regions

    • Amphi = both kinds on both sides

    • Able to interact with both hydrophilic and hydrophobic molecules

  • Adenine and thymine = purines, connected by 2 hydrogen bonds

  • Cytosine and guanine = pyrimidine, connected by 3 hydrogen bonds → more stable, harder to break

  • NOTE: Every unlabeled vertex implies that there is a CARBON ATOM

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"Human knowledge is never contained in one person. It grows from the relationships we create between each other and the world, and still it is never complete." 
- Paul Kalanithi (from When Breath Becomes Air)

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