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Anatomy & Physiology · Chapter 2

The Chemical Level of Organization

Every heartbeat, every thought, every drop of sweat begins as chemistry. Long before a cell can divide or a nerve can fire, atoms must bond, reactions must run, and water must do its quiet, essential work. This chapter takes you down to the chemical level — the foundation the whole rest of the book is built on. You will meet the atom and the handful of elements that make up almost all of you, learn the three bonds that hold molecules together, watch reactions rearrange matter and see how enzymes speed them up, discover why water is the perfect medium for life, learn to read pH and the buffers that guard your blood, and finish with the four great families of molecules that build your body. Get comfortable here — everything upstairs depends on this floor.

By the end of this chapter you can

  • Describe the structure of an atom — protons, neutrons, and electrons — and explain how the atomic number defines an element.
  • Name the major elements that make up most of the human body and distinguish them from trace elements and isotopes.
  • Compare ionic, covalent (polar and nonpolar), and hydrogen bonds, and explain the octet rule that drives bonding.
  • Classify chemical reactions as synthesis, decomposition, or exchange, and explain activation energy and how enzymes lower it.
  • Explain how water's polarity makes it the body's solvent, temperature buffer, and lubricant.
  • Interpret the pH scale, distinguish acids from bases, and describe how buffers hold blood near 7.4.
  • Identify the four organic macromolecule families — carbohydrates, lipids, proteins, nucleic acids — plus ATP, and give a job for each.
  • Contrast dehydration synthesis with hydrolysis as the way polymers are built and broken.

Section 1Atoms & the elements

Atomic structure reference figure
Reference. The structure of the atom — nucleus and electron shells — OpenStax, CC BY 3.0 (via Wikimedia Commons)

Matter, elements, and the atom

Anything that takes up space and has mass is matter — your bones, your blood, the air in your lungs. All matter is built from elements, pure substances that cannot be broken down into anything simpler by ordinary chemistry. There are 118 known elements, but life is surprisingly economical: only about two dozen appear in the body, and just six — oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus — account for roughly 99% of your mass. The smallest particle of an element that still behaves like that element is the atom. Split an atom apart and you no longer have the element; you have its raw ingredients.

ElementSymbol~% of body massA job it does
OxygenO65%Part of water; final electron acceptor in respiration
CarbonC18%The backbone of every organic molecule
HydrogenH10%Part of water; sets pH as the H⁺ ion
NitrogenN3%In every protein and nucleic acid
CalciumCa1.5%Bone mineral; muscle and nerve signaling
PhosphorusP1%Bone; the energy bonds of ATP and DNA

Inside the atom: three particles

An atom has a dense center, the nucleus, surrounded by a cloud of moving electrons. Only three subatomic particles matter for this course. Protons carry a positive charge and sit in the nucleus. Neutrons carry no charge and share the nucleus with the protons, adding mass but no charge. Electrons carry a negative charge and are almost weightless, whirling around the nucleus in layered shells (energy levels). Because protons and electrons carry equal and opposite charges, a neutral atom has exactly as many electrons as protons, and the whole thing balances out to no net charge.

ParticleChargeLocationRelative mass
Proton+1Nucleus1 (heavy)
Neutron0Nucleus1 (heavy)
Electron−1Shells around the nucleus~1/1800 (negligible)

Atomic number, isotopes, and the outer shell

One number is the atom's fingerprint: the atomic number, the count of protons in the nucleus. Change it and you change the element itself — 1 proton is always hydrogen, 6 is always carbon, 8 is always oxygen. The mass number adds protons and neutrons together. Atoms of the same element that carry different numbers of neutrons are called isotopes: carbon-12 and carbon-14 are both carbon (6 protons each), but carbon-14 has two extra neutrons and is radioactive, which is exactly why radioactive isotopes are so useful in medical imaging and dating. What drives an atom's chemistry, though, is not its nucleus but its outermost electrons — the valence shell. Atoms are “happiest” (most stable) when that outer shell is full, which for most biological atoms means eight electrons — the octet rule. An atom with a full outer shell is inert; an atom short a few electrons is reactive and ready to bond.

Isotopes at the bedside. Because isotopes behave chemically like their normal counterparts but announce themselves with radiation, clinicians use them to see the invisible: iodine-131 traces the thyroid, technetium-99m lights up bone scans, and fluorine-18, tagged onto a glucose analogue (FDG), drives PET imaging of metabolically active tissue. Same element, extra neutrons, enormous diagnostic power.

Pick an element and watch its atom assemble — nucleus in the center, electrons filling their shells — in the interactive below.

Interactive Pick an element and watch its atom build — nucleus in the center, electrons whirling in shells. Open full ↑
Key points
  • An atom has a nucleus of positive protons and neutral neutrons, orbited by negative electrons in shells.
  • The atomic number (proton count) defines the element; a neutral atom has equal protons and electrons.
  • Isotopes are the same element with different neutron counts; some are radioactive and medically useful.
  • The valence (outer) shell drives chemistry — atoms bond to reach a stable, full shell (the octet rule).

Section 2Chemical bonds

Chemical bonds reference figure
Reference. Ionic, covalent, and hydrogen bonds — OpenStax, CC BY 3.0 (via Wikimedia Commons)

Why atoms bond at all

Atoms bond for one reason: to reach a stable, full outer shell. An atom with a lonely, half-empty valence shell will do almost anything to fill it — give electrons away, take them, or share them — and each of those strategies produces a different kind of bond. The noble gases (helium, neon, argon) already have full shells, so they drift through the world refusing to react. Everything else is looking for a partner. Understanding the three main bonds — ionic, covalent, and hydrogen — lets you predict how nearly every molecule in the body behaves.

Ionic bonds: give and take

Sometimes the cleanest way to fill a shell is to hand an electron over completely. When one atom donates an electron and another accepts it, both walk away charged: the donor becomes a positive cation, the acceptor a negative anion. Opposite charges attract, and that electrostatic pull is the ionic bond. Table salt is the classic case: sodium hands its lone outer electron to chlorine, becoming Na⁺, while chlorine becomes Cl⁻, and the two cling together as NaCl. In water, ionic compounds pull apart into their separate ions — these dissolved, charged particles are your electrolytes (Na⁺, K⁺, Ca⁺⁺, Cl⁻), and they run nerve signals, muscle contraction, and fluid balance.

Covalent bonds: sharing — polar and nonpolar

More often, two atoms simply share a pair of electrons so that both count it toward a full shell — a covalent bond, the strongest and most common bond in the body. Carbon builds all of life on covalent bonds. But sharing is not always fair. When both atoms pull equally, the shared electrons sit in the middle and the bond is nonpolar (as in O₂ or the carbon–hydrogen bonds of fats). When one atom pulls harder, it hogs the electrons and the bond becomes polar, leaving one end slightly negative and the other slightly positive. Water is the great polar molecule: oxygen pulls the shared electrons away from its two hydrogens, so oxygen carries a partial negative charge and the hydrogens a partial positive — a lopsidedness that, as you will see, makes life possible.

Hydrogen bonds: weak but mighty

A hydrogen bond is not a bond within a molecule but a gentle attraction between molecules (or between distant parts of one big molecule). It forms when the slightly positive hydrogen of one polar molecule is drawn to the slightly negative oxygen or nitrogen of another. Any single hydrogen bond is feeble — a fraction of the strength of a covalent bond — but in the millions they become mighty. Hydrogen bonds hold liquid water together, zip the two strands of DNA into a double helix, and fold proteins into their working shapes. They are strong enough to give structure yet weak enough to break and re-form, which is exactly what living molecules need.

BondHow it formsStrengthExample
IonicOne atom donates an electron to another; opposite charges attractStrong (weak once dissolved in water)Na⁺Cl⁻ (table salt)
Covalent (nonpolar)Electrons shared equallyStrong (covalent bonds are the strongest in the body)O₂; C–H bonds in fats
Covalent (polar)Electrons shared unequally — partial chargesStrong (covalent bonds are the strongest in the body)Water (H₂O)
HydrogenAttraction between partial + and partial − on polar moleculesWeak (strong in numbers)Between water molecules; DNA strands
Ionic bonds dissolve; covalent bonds don't. Drop salt in water and it splits into Na⁺ and Cl⁻ — the ionic bond gives way. Drop sugar in water and it dissolves but stays a whole molecule, because its atoms are held by covalent bonds that water cannot break. This one difference explains why blood is full of free electrolytes yet its glucose stays intact.

Flip between ionic, covalent, and hydrogen bonds and watch how each one forms in the interactive.

Interactive Give electrons away, share them, or feel a gentle attraction — flip between the three bonds. Open full ↑
Key points
  • Atoms bond to fill their valence shell; a full shell is stable and unreactive.
  • Ionic bonds transfer electrons, making charged ions (electrolytes) that separate in water.
  • Covalent bonds share electrons — equally (nonpolar) or unequally (polar); they are the body's strongest bonds.
  • Hydrogen bonds are weak individual attractions between polar molecules that add up to hold water, DNA, and proteins together.

Section 3Chemical reactions & enzymes

Chemical reactions and activation energy reference figure
Reference. Reactions, activation energy, and how enzymes lower the hill — OpenStax, CC BY 4.0 (via Wikimedia Commons)

Reactants, products, and three ways to rearrange atoms

A chemical reaction is simply the making or breaking of bonds — atoms let go of old partners and grab new ones. The starting materials are the reactants; what you end up with are the products. No atoms are created or destroyed; they are only rearranged. Almost every reaction in the body fits one of three patterns. Synthesis reactions join smaller parts into a larger molecule (A + B → AB) — the building, or anabolic, reactions. Decomposition reactions break a large molecule into smaller pieces (AB → A + B) — the demolishing, or catabolic, reactions, like digesting a meal. Exchange reactions do both at once, swapping partners (AB + CD → AC + BD). Many reactions are also reversible, running either direction depending on conditions.

TypePatternWhat it doesBody example
Synthesis (anabolic)A + B → ABBuilds larger moleculesAmino acids joined into a protein
Decomposition (catabolic)AB → A + BBreaks molecules apartDigesting starch into glucose
ExchangeAB + CD → AC + BDSwaps partnersBuffers trading H⁺ in the blood

Energy: the hill every reaction must climb

Chemical bonds are little reservoirs of energy, so rearranging them always involves an energy change. Reactions that release energy (usually as heat) are exergonic — these power the body, like breaking down glucose. Reactions that absorb energy are endergonic — building big molecules costs energy. But here is the catch: even a reaction that releases energy overall must first be nudged over an initial hump called the activation energy — the energy needed to get the reactants unstable enough to react at all. Think of a boulder resting in a small dip near the top of a hill: it will roll down and release a lot of energy, but only after something lifts it over the lip first. That lip is activation energy, and at body temperature most reactions would sit stuck behind it for hours or years.

Enzymes: shrinking the hill

The body cannot wait hours, and it cannot simply crank up the heat — so it uses enzymes. An enzyme is a biological catalyst (nearly always a protein) that lowers the activation energy of a reaction, letting it run thousands or millions of times faster at a safe 37 °C. Crucially, an enzyme is not consumed — it does its job and is freed to do it again. Each enzyme is exquisitely specific, with an active site shaped to fit one particular substrate like a key in a lock (or, more accurately, a glove that molds around the hand). Because enzymes are proteins, anything that unfolds a protein — a high fever, the wrong pH — can cripple them, which is one reason your body guards its temperature and pH so fiercely.

The “-ase” giveaway. Most enzymes are named for their substrate plus the suffix -ase: lactase digests lactose, lipase digests lipids, protease digests protein, and sucrase digests sucrose. See a molecule's name with “-ase” on the end and you are almost certainly looking at the enzyme that takes it apart.

Watch a reaction run over its energy hill, then switch on an enzyme and see the hill shrink in the interactive below.

Interactive Watch a reaction climb its energy hill, then add an enzyme and see the hill shrink. Open full ↑
Key points
  • Reactions rearrange atoms from reactants into products as synthesis, decomposition, or exchange.
  • Exergonic reactions release energy; endergonic reactions absorb it; every reaction must first clear its activation energy.
  • Enzymes are protein catalysts that lower activation energy, are reused, and are highly specific to their substrate.
  • Enzymes depend on their shape, so heat and pH extremes can disable them.

Section 4Water, the solvent of life

Water as a polar solvent reference figure
Reference. Water's polarity and its role as a solvent — OpenStax, CC BY 3.0 (via Wikimedia Commons)

Polarity: the source of all water's tricks

You are roughly 60% water, and that is no accident — nearly every remarkable thing water does traces back to a single feature: it is polar. Recall from Section 2 that oxygen hogs the shared electrons in each O–H bond, so a water molecule (H₂O) carries a slightly negative pole at the oxygen and slightly positive poles at the two hydrogens. Because opposite partial charges attract, every water molecule clings by hydrogen bonds to the water molecules around it. That constant, shifting web of hydrogen bonds is the hidden machinery behind water's role as a solvent, a temperature buffer, and a lubricant.

The universal solvent

Water is called the universal solvent because its charged poles surround and pull apart other charged or polar substances, scattering them evenly into solution. The dissolving liquid is the solvent, the dissolved substance the solute. Molecules that mix into water — salts, sugars, amino acids — are hydrophilic (“water-loving”), while nonpolar molecules like fats are hydrophobic (“water-fearing”) and refuse to dissolve. This split does real anatomical work: it is exactly why cell membranes, made of hydrophobic lipids, form watertight barriers in your watery body. And because so much of the body's chemistry happens in solution, water is the medium in which nutrients travel, wastes dissolve, and reactions occur — blood plasma is, at heart, water carrying dissolved cargo.

Heat, cushioning, and chemistry

Water's hydrogen bonds also give it a very high heat capacity: it takes a lot of energy to raise water's temperature, so your water-rich body resists sudden swings in temperature and stays near 37 °C. Better still, evaporating water carries away enormous heat, which is why sweating cools you so effectively on a hot day. The same cohesive stickiness lets water form protective, cushioning films — the slippery fluid in serous membranes, the synovial fluid in joints, the mucus lining your airways all rely on it. Finally, water is not just a bystander to chemistry; it is a participant. The body builds big molecules by removing water (dehydration synthesis) and breaks them down by adding water (hydrolysis) — the two reactions you will meet again in Section 6.

PropertyWhy (from polarity)What it does for you
SolventCharged poles pull solutes apartTransports nutrients, wastes, and ions in blood
High heat capacityHydrogen bonds absorb heatBuffers body temperature near 37 °C
Evaporative coolingBreaking H-bonds carries off heatSweating cools the body
Cohesion / lubricationMolecules stick to one anotherSlippery films in joints, membranes, airways
ReactantCan be added or removed in reactionsBuilds and breaks macromolecules
“Like dissolves like.” Polar and ionic substances dissolve in polar water; nonpolar substances dissolve in nonpolar fats. This simple rule predicts a lot of physiology — why oil and water separate, why fat-soluble vitamins (A, D, E, K) need fat to be absorbed, and why the hydrophobic core of a cell membrane keeps the watery inside and outside apart.

Explore what water's lopsided charge buys you — dissolving, sticking, and buffering heat — in the interactive.

Interactive Water is polar — lopsided in charge. Explore what that one fact buys you. Open full ↑
Key points
  • Water is polar, so its molecules hydrogen-bond to one another — the source of all its special properties.
  • As the universal solvent, water dissolves hydrophilic solutes but not hydrophobic ones, a split that shapes membranes.
  • High heat capacity and evaporative cooling let water stabilize body temperature and enable sweating.
  • Water is a reactant — removed in dehydration synthesis, added in hydrolysis.

Section 5pH, acids, bases & buffers

The pH scale reference figure
Reference. The pH scale from acidic to basic — OpenStax, CC BY 3.0 (via Wikimedia Commons)

What pH actually measures

pH is a measure of how many free hydrogen ions (H⁺) are floating loose in a fluid. The more H⁺, the more acidic the fluid; the fewer, the more basic (alkaline). The scale runs from 0 to 14, with 7 as neutral (pure water). Below 7 is acidic, above 7 is basic. The one twist students must respect is that the scale is logarithmic: each whole step is a tenfold change in H⁺. A fluid at pH 4 is not slightly more acidic than pH 5 — it holds ten times more hydrogen ions. That is why a drift of even a few tenths of a pH unit in the blood is a genuine emergency.

Acids, bases, and the number that matters most

An acid is a substance that releases H⁺ into solution, driving pH down — stomach acid sits near pH 2. A base accepts H⁺ (or releases OH⁻), driving pH up — household bleach and pancreatic secretions are basic. The number that matters most in all of physiology is the pH of blood, which must stay locked in the razor-thin range of 7.35 to 7.45 (about 7.4). Slip below 7.35 and you are in acidosis; rise above 7.45 and you are in alkalosis. Push past roughly 6.8 or 7.8 and proteins denature, enzymes fail, and the situation becomes life-threatening. Compared with the wild pH swings of the world outside, the body keeps its blood almost eerily steady.

FluidApprox. pHAcidic / basic
Stomach acid~2Strongly acidic
Urine~6Slightly acidic
Pure water7Neutral
Blood7.35–7.45Slightly basic
Pancreatic juice~8Basic

Buffers: holding the line at 7.4

How does blood hold its pH so steady while acids pour in from every meal and every muscle? The answer is buffers — chemical partnerships that soak up excess H⁺ when a fluid turns too acidic and release H⁺ when it turns too basic. The body's front-line buffer is the bicarbonate system: carbonic acid (H₂CO₃) and bicarbonate ion (HCO₃⁻) sit in equilibrium, trading hydrogen ions back and forth to blunt any swing. Buffers do not make acid disappear; they cushion the blow long enough for the lungs (which blow off CO₂) and kidneys (which excrete H⁺) to restore true balance. It is homeostasis at the molecular level — and a preview of the acid–base chapters ahead.

A little number, a big deal. Because pH is logarithmic, blood at 7.1 holds roughly twice the H⁺ of blood at 7.4 — a change that sounds tiny on paper but can slow the heart, cloud consciousness, and threaten life. When a clinician frets over a pH of 7.2, remember it is not a rounding error; it is a tenfold-scale alarm.

Push the pH up and down and watch buffers fight to pull it back toward neutral in the interactive.

Interactive pH measures free H⁺; blood must stay near 7.4. Push the pH around and watch buffers respond. Open full ↑
Key points
  • pH measures free H⁺: below 7 is acidic, above 7 is basic, and the scale is logarithmic (each unit = 10×).
  • Acids release H⁺; bases accept it; blood must stay in the narrow range 7.35–7.45.
  • Straying gives acidosis (too low) or alkalosis (too high), both dangerous.
  • Buffers — chiefly the bicarbonate system — absorb or release H⁺ to hold pH steady.

Section 6The molecules of life

Note. The four families of organic macromolecules

Organic molecules and the carbon backbone

Turn from the small inorganic molecules — water, salts, gases — to the big organic ones, and you meet the true building blocks of the body. Organic molecules are, by definition, built on a skeleton of carbon. Carbon is the perfect construction atom because it can form four covalent bonds at once, letting it chain into long backbones, branch, and close into rings. The largest of these — macromolecules — are usually polymers: long chains snapped together from small repeating units called monomers. The body assembles a polymer by dehydration synthesis (removing a water molecule to bond two monomers) and takes it apart by hydrolysis (adding water to split the bond). Nearly everything you are made of belongs to just four families — plus one special molecule that powers the whole enterprise.

The four families

Carbohydrates are sugars and their chains — monomers called monosaccharides (glucose) link into polysaccharides (glycogen, starch). They are the body's quick, preferred fuel. Lipids are the oily, water-fearing molecules: triglycerides store energy and insulate, phospholipids build every cell membrane, and steroids like cholesterol become hormones. Their hydrophobic nature is exactly what makes membranes work. Proteins are the body's workhorses, built from twenty kinds of amino acids strung together and then folded into precise three-dimensional shapes — and because shape determines function, a protein that unfolds (denatures) from heat or wrong pH stops working, like an egg white turning solid in a hot pan. Proteins serve as enzymes, structural fibers, transporters, and messengers. Nucleic acids — DNA and RNA — are chains of nucleotides that store and carry the genetic instructions for building every protein you own.

FamilyMonomer / unitExampleMain job
CarbohydrateMonosaccharide (glucose)Glycogen, starchQuick energy; short-term fuel storage
LipidFatty acids + glycerolTriglyceride, phospholipid, cholesterolEnergy storage, insulation, membranes, hormones
ProteinAmino acid (20 kinds)Enzymes, keratin, hemoglobinStructure, catalysis, transport, signaling
Nucleic acidNucleotideDNA, RNAStore and express genetic information

ATP: the cell's energy currency

One small molecule deserves its own spotlight: adenosine triphosphate, or ATP. It is the universal energy currency every cell spends. ATP holds three phosphate groups on a tail, and the bond to the last phosphate is a coiled spring of energy. When the cell needs power — to contract a muscle, pump an ion, or build a molecule — it snaps off that last phosphate (ATP → ADP + phosphate) and the released energy drives the work. The cell then recharges ADP back into ATP using energy from food. You are, in a very real sense, rebuilding your body weight in ATP every day, spending and remaking it billions of times a second.

Shape is everything for a protein. A protein's job is written in its folded shape, so anything that unfolds it — a high fever, an acid or base, some poisons — can destroy its function even though the amino acids are all still there. That is denaturation, and it is why a fever above about 41 °C is dangerous: the body's own enzymes begin to lose their shape.

Pick a macromolecule family and watch it snap together from its monomers in the interactive below.

Interactive Four families of organic molecules, each built from small monomers — pick one and watch it build. Open full ↑
Key points
  • Organic molecules are built on carbon, which forms four bonds; big ones are polymers of repeating monomers.
  • Polymers form by dehydration synthesis (removing water) and break by hydrolysis (adding water).
  • The four families: carbohydrates (fuel), lipids (membranes, storage, hormones), proteins (workhorses whose shape is their function), and nucleic acids (genetic information).
  • ATP is the cell's energy currency, releasing energy when its last phosphate is removed.

The chapter in one breath

  • All matter is built from elements, and the smallest unit of an element is the atom — a nucleus of protons and neutrons orbited by electrons; the atomic number (protons) defines the element.
  • Six elements — O, C, H, N, Ca, P — make up about 99% of the body; atoms bond to fill their outer shell (the octet rule).
  • Three bonds hold molecules together: ionic (transfer electrons → ions), covalent (share electrons, polar or nonpolar), and weak hydrogen bonds.
  • Reactions rearrange atoms by synthesis, decomposition, or exchange; each must clear an activation energy hill that enzymes lower.
  • Water is polar, making it the body's solvent, temperature buffer, and lubricant, and a reactant in building and breaking molecules.
  • pH tracks free H⁺ on a logarithmic scale; blood is held at 7.35–7.45 by buffers such as bicarbonate.
  • Life is built from four organic families — carbohydrates, lipids, proteins, nucleic acids — plus ATP, assembled by dehydration synthesis and broken by hydrolysis.

ReferenceWords worth knowing

A quick reference for the terms in this chapter — skim it now, or circle back whenever a word trips you up.

Acid
A substance that releases hydrogen ions (H⁺) into solution, lowering pH below 7.
Activation energy
The initial energy hump that reactants must overcome before a reaction can proceed; enzymes lower it.
Atom
The smallest unit of an element that retains the element's properties; a nucleus of protons and neutrons orbited by electrons.
Atomic number
The number of protons in an atom's nucleus, which defines the element.
ATP (adenosine triphosphate)
The cell's energy currency; it releases usable energy when its terminal phosphate is removed to form ADP.
Base
A substance that accepts hydrogen ions (or releases OH⁻), raising pH above 7.
Buffer
A chemical system that resists changes in pH by absorbing or releasing H⁺, such as the bicarbonate buffer of blood.
Carbohydrate
An organic family of sugars and their polymers (glucose, glycogen) used mainly for quick energy.
Covalent bond
A bond in which atoms share electrons; equal sharing is nonpolar, unequal sharing is polar.
Dehydration synthesis
Building a polymer by removing a water molecule to link two monomers.
Electron
A negatively charged, nearly massless particle that orbits the nucleus in shells and drives chemical bonding.
Element
A pure substance that cannot be broken down chemically; the body is built mostly from six of them.
Enzyme
A biological catalyst (usually a protein) that lowers a reaction's activation energy without being consumed.
Hydrogen bond
A weak attraction between the partial-positive hydrogen of one polar molecule and a partial-negative atom of another.
Hydrolysis
Breaking a polymer apart by adding a water molecule across the bond.
Ionic bond
A bond formed when one atom donates an electron to another, creating oppositely charged ions that attract.
Isotope
An atom of an element with the usual number of protons but a different number of neutrons.
Lipid
A hydrophobic organic family including triglycerides, phospholipids, and steroids; used for storage, membranes, and hormones.
Nucleic acid
A polymer of nucleotides (DNA or RNA) that stores and expresses genetic information.
pH
A logarithmic measure of free hydrogen-ion concentration; 7 is neutral, lower is acidic, higher is basic.
Polar molecule
A molecule with an uneven charge distribution, such as water, where one end is slightly negative and the other slightly positive.
Protein
A polymer of amino acids folded into a specific shape; its shape determines its function as an enzyme, structure, transporter, or messenger.

Check yourself

1. An atom has 8 protons, 8 neutrons, and 8 electrons. What element is it, what is its net charge, and what is its mass number?
Oxygen; net charge zero; mass number 16. The atomic number (8 protons) makes it oxygen; equal protons and electrons make it neutral; protons plus neutrons (8 + 8) give a mass number of 16.
2. Two atoms of the same element have different numbers of neutrons. What are they called, and does their chemical behavior change?
They are isotopes, and their chemistry is essentially the same. Chemical behavior is set by electrons (and thus proton count), not neutrons, so isotopes react alike — but the extra neutrons can make one radioactive and useful for imaging.
3. Why do atoms form chemical bonds at all, and why are the noble gases like neon inert?
Atoms bond to fill their outer (valence) shell and become stable — the octet rule. Noble gases already have full outer shells, so they have no reason to gain, lose, or share electrons and stay unreactive.
4. Classify each bond: (a) sodium gives an electron to chlorine; (b) two oxygen atoms share electrons equally; (c) a partial-positive H is drawn to a partial-negative O on a neighboring molecule.
(a) Ionic; (b) nonpolar covalent; (c) hydrogen bond. Ionic bonds transfer electrons to make ions, covalent bonds share them (equally here, so nonpolar), and hydrogen bonds are weak attractions between polar molecules.
5. Salt (NaCl) and sugar both dissolve in water, but only one splits into charged particles. Which one, what are those particles called, and why does the other stay whole?
Salt splits into ions (electrolytes: Na⁺ and Cl⁻); sugar stays a whole molecule. Salt's ionic bond gives way in water, freeing charged ions, while sugar's atoms are held by covalent bonds that water cannot break.
6. Name the three types of chemical reaction and match each to an example: digesting starch into glucose; joining amino acids into a protein; buffers trading H⁺.
Decomposition = digesting starch; synthesis = joining amino acids; exchange = buffers trading H⁺. Decomposition breaks molecules apart (catabolic), synthesis builds them up (anabolic), and exchange swaps partners.
7. What is activation energy, and how does an enzyme let a reaction run faster at body temperature without being used up?
Activation energy is the initial energy hump a reaction must clear; an enzyme lowers that hump. By lowering activation energy the enzyme speeds the reaction dramatically at 37 °C, and because it is a catalyst it emerges unchanged and can act again.
8. Water's most important feature is that it is polar. Explain what “polar” means for a water molecule and name two properties that result.
Polar means uneven charge: oxygen is slightly negative, the hydrogens slightly positive. This lets water hydrogen-bond to itself and to solutes, giving it its solvent power, high heat capacity, cohesion, and role in reactions — any two of these count.
9. Why do fat-soluble vitamins need fat to be absorbed, phrased using the rule “like dissolves like”?
Because they are nonpolar (hydrophobic), they dissolve in nonpolar fats, not in polar water. “Like dissolves like” means polar substances dissolve in water and nonpolar ones dissolve in fat, so fat-soluble vitamins ride along with dietary fat.
10. The pH scale is logarithmic. How much more acidic is a fluid at pH 4 than one at pH 6, and why is a blood pH of 7.1 a serious concern?
pH 4 has 100 times more H⁺ than pH 6 (two units = 10 × 10). Because each unit is a tenfold change, even the small drop from 7.4 to 7.1 roughly doubles blood H⁺ — enough to disrupt enzymes and threaten life (acidosis).
11. Blood is constantly flooded with acids yet holds its pH near 7.4. What chemical system prevents wild swings, and does it remove the acid permanently?
Buffers — chiefly the bicarbonate system (H₂CO₃ / HCO₃⁻) — and no, they only cushion the change. Buffers absorb or release H⁺ to blunt swings, buying time for the lungs (exhaling CO₂) and kidneys (excreting H⁺) to restore true balance.
12. Name the four organic macromolecule families and give the monomer of each. Then explain why a high fever endangers proteins.
Carbohydrates (monosaccharides), lipids (fatty acids + glycerol), proteins (amino acids), nucleic acids (nucleotides). A protein's function depends on its folded shape; a high fever denatures proteins — unfolds them — so enzymes lose their shape and stop working even though the amino acids remain.