LeClaire Institute

Module 1 · Protein

Protein from the atoms up: the four kinds of atom in an amino acid, the shared backbone and changing side chain, the peptide bond, all 20 amino acids drawn at one scale, how chains fold into working shapes, how you digest and use protein, and which foods give you all 9 essential amino acids. The figure is on the left and the lesson script on the right; the quiz is at the end.

Previous lesson: Module 1 · Other Lipids

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Figure 1

The Protein Family Tree

Amino acids build up into peptides and proteins; food supplies the amino acids.

Protein on a food label
Protein (grams)Every gram gives about 4 kcal, the same as carbohydrate. The grams are total protein, whatever the source.
%DV is often missingIn the US the % Daily Value for protein is optional unless the package makes a protein claim or the food is for young children; then it is adjusted for protein quality.
Not listed: which amino acidsThe label doesn’t say whether a protein is complete. Figure 7 shows how to tell from the food itself.
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Figure 2

From Atoms to an Amino Acid

Four kinds of atom, one shared backbone, one side chain that changes.

The atoms

Four atoms, four ways to bond

Carbon makes 4 bondsmethane, CH4

Nitrogen makes 3ammonia, NH3

Oxygen makes 2water, H2O

Sulfur makes 2hydrogen sulfide, H2S

Hydrogen makes just 1 bond. Every amino acid is built from these few atoms: carbon, hydrogen, oxygen and nitrogen, plus sulfur in two of them. Nitrogen is the atom that fats and carbohydrates don’t have.

The amino acid

Glycine, C2H5NO2 the simplest amino acid

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  1. 1Amine group (NH2): a nitrogen with two hydrogens. This is the “amino” in amino acid.
  2. 2Alpha carbon: the centre that everything hangs on.
  3. 3Carboxyl group (COOH): the “acid”. Its OH can give up a hydrogen.

Alanine, C3H7NO2

1234
  1. 1Amine group, same as glycine.
  2. 2Alpha carbon, same as glycine.
  3. 3Carboxyl group, same as glycine.
  4. 4Side chain (R group): here a CH3. Glycine’s side chain is just one hydrogen. The side chain is the only part that differs between the 20 amino acids.

carbon hydrogen oxygen nitrogen sulfur · every molecule on this page is drawn at the same scale with every hydrogen shown · tap one to enlarge it

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Figure 3

The Peptide Bond

Amino acids join head to tail and release water.

Two amino acids join

Glycine

1
+

Alanine

2
→

Glycyl-alanine, C5H10N2O3

3
+

Water

  1. 1The OH of glycine’s carboxyl group…
  2. 2…and one H of alanine’s amine group leave together as a water molecule.
  3. 3Peptide bond: the carbon of one amino acid now bonds straight to the nitrogen of the next (C–N), next to its C=O. This bond is strong and flat.
A chain grows

A tripeptide: Gly-Ala-Ser, C8H15N3O5

N12C
  1. 1First peptide bond.
  2. 2Second peptide bond. Each new amino acid adds one more and releases one more water.
  3. NN-terminus: a free amine group starts every chain.
  4. CC-terminus: a free carboxyl group ends it.

The repeating N–C–C, N–C–C pattern is the backbone. A chain of up to about 50 amino acids is usually called a peptide; longer ones are proteins. Most proteins are a few hundred amino acids long.

carbon hydrogen oxygen nitrogen · every molecule on this page is drawn at the same scale with every hydrogen shown · tap one to enlarge it

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Figure 4

The 20 Amino Acids

Same backbone, 20 side chains; 9 you must eat.

The 9 essential amino acids

Histidine essentialHis · ring with nitrogens

Isoleucine essentialIle · branched

Leucine essentialLeu · branched

Lysine essentialLys · ends in NH₂

Methionine essentialMet · has sulfur

Phenylalanine essentialPhe · benzene ring

Threonine essentialThr · has OH

Tryptophan essentialTrp · double ring

Valine essentialVal · branched

The 6 conditionally essential

ArginineArg · conditional

CysteineCys · conditional

GlutamineGln · conditional

GlycineGly · conditional

ProlinePro · conditional

TyrosineTyr · conditional

The 5 non-essential

AlanineAla

AsparagineAsn

Aspartic acidAsp

Glutamic acidGlu

SerineSer

carbon hydrogen oxygen nitrogen sulfur · every molecule on this page is drawn at the same scale with every hydrogen shown · tap one to enlarge it

What the essential ones do
EssentialWhat its side chain doesIn your body
Leucine, isoleucine, valineBranched carbon chains (the BCAAs); oily, so they sit inside proteinsPlentiful in muscle protein; leucine also signals muscle to build protein
LysineLong chain ending in NH2, chargedCollagen cross-links, carnitine; often the lowest essential amino acid in grains
MethionineContains sulfurStarts nearly every new protein chain; the body makes cysteine from it; often lowest in beans
PhenylalanineBenzene ringThe body makes tyrosine from it. People with PKU can’t, which is why aspartame labels warn about it
TryptophanLargest: a double ring with nitrogenRaw material for serotonin and melatonin, and some niacin (vitamin B3)
ThreonineHas an OH groupPart of mucus proteins that line the gut; collagen
HistidineRing with two nitrogensRaw material for histamine; part of hemoglobin’s iron pocket
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Figure 5

From Chain to Shape

Four levels of structure, and why cooking changes protein.

Four levels of structure

1 · Primary: the order of amino acids

Set by your genes. Change one amino acid and the whole protein can change: sickle-cell hemoglobin differs from normal hemoglobin by a single swap.

2 · Secondary: local coils and sheets

Alpha helix: each C=O bonds to the N–H four amino acids along

C=Oamino acid 1N–Hamino acid 5N-terminusC-terminus
carbonnitrogenoxygenhydrogenhydrogen bond

Backbone only (side chains left off), real helix geometry: 3.6 amino acids per turn. The bonds all run along the spiral's length, which holds it like a spring.

Beta sheet: strands side by side, C=O on one bonded to N–H on the next

C=ON–HNCNCNC
carbonnitrogenoxygenhydrogenhydrogen bond

Antiparallel: neighbouring strands run in opposite directions, N to C (the arrows). In a parallel sheet they all run the same way. Here the bonds run across, between strands, not along them. Backbone only, seen from above.

Held by hydrogen bonds between the C=O of one peptide bond and the N–H of another.

3 · Tertiary: the whole chain folds

Tertiary: one chain folds into its final shape

oily corewaterwaterS–SS–SNC
oily (hydrophobic) side chain, insidewater-loving (polar or charged) side chain, outsidesulfur: S–S cross-link between two cysteineswater (H₂O) all around

Cartoon, not to scale: the blue line is the chain, each ball a side chain. Water pushes the oily ones together in the middle; the charged and polar ones stay out in the water.

Shape decides the job: an enzyme’s pocket

enzymepocketright shape:
fits
wrong shape:
doesn’t fit

Only the molecule that matches the pocket’s shape fits and gets worked on. If the chain unfolds, the pocket is lost.

Oily side chains tuck inside, water-loving ones face out, and sulfur cross-links between cysteines can hold the fold. The shape decides the job.

4 · Quaternary: chains team up

Hemoglobin: four chains, each with a heme

α chainβ chainβ chainα chainheme (see close-up)FeO₂
α chainα chainβ chainβ chainheme ringiron (Fe)oxygen (O₂)nitrogen

Cartoon, not to scale. Each heme’s iron holds one O₂, so one hemoglobin carries four. The close-up below shows one heme atom by atom.

Close-up: one heme in its pocket, atom by atom

The iron (Fe) sits in the middle of the flat ring. O₂ binds on top and His E7 hydrogen-bonds it (dashed line); His F8 holds the iron from below.

One heme in its pocket in hemoglobin, ball-and-stick with every hydrogen: a flat ring of four pyrroles joined by CH bridges, its four nitrogens (blue) holding an orange iron atom at the centre. Above the iron an oxygen molecule (two red atoms) is bound end-on and bent; the distal histidine E7 above it hydrogen-bonds the far oxygen (dashed line). Below, the proximal histidine F8 is bonded to the iron. Valine, phenylalanine and leucine side chains (sticks) line the pocket, and pale blue tubes trace the E and F helices of the protein chain.O₂His E7His F8Fe12345678E helixF helix

Side view: the same heme edge-on. The ring is flat; the iron sits in it, with O₂ and His E7 straight above and His F8 straight below.

The same heme seen edge-on: the ring is a flat line with the iron in it; the O2 sits straight above the iron, bent, with histidine E7 above it, and histidine F8 sits straight below.O₂H-bondHis E7His F8Feflat ring
  1. 1pyrrole: a five-atom ring with one N; four of them make the heme ring
  2. 2methine bridge (=CH–) joining two pyrroles
  3. 3methyl, CH₃ (four on the ring)
  4. 4vinyl, CH=CH₂ (two)
  5. 5propionate, CH₂CH₂COO⁻ (two, charged, they face the water)
  6. 6valine E11
  7. 7phenylalanine CD1
  8. 8leucine FG3: 6 to 8 are oily side chains (sticks) that keep water away from the iron

carbon hydrogen oxygen nitrogen iron (Fe²⁺) hydrogen bond protein backbone (helix) · same scale as every molecule on this page, every hydrogen shown

Real atom positions from the X-ray structure of oxygen-carrying human hemoglobin (Protein Data Bank 2DN1, 1.25 Å), one α chain; hydrogens added, since X-rays barely see them. In this structure the iron is bonded to the four ring nitrogens (2.0 Å) and sits almost exactly in the ring; the O₂ binds end-on (Fe–O 1.8 Å) and bends at 124°. In the side view the iron is drawn in front of the ring edge so you can see it.

Collagen: three chains wound into a rope

chain 1chain 2chain 3glycine

A triple helix. The white dots mark glycine: every third amino acid is glycine, the smallest one, the only one small enough to fit in the middle of the tight rope.

Hemoglobin is 4 chains (2 alpha, 2 beta), each holding one heme with an iron atom (orange) that carries oxygen. Collagen is 3 chains wound into a rope.

Cartoons, not to scale: each bead is a whole amino acid, and each ribbon is a stretch of chain. The helix and sheet are drawn ball-and-stick, backbone only. Tap any white panel to enlarge it.

Cooking unfolds proteins

Heat, acid, salt or whipping break the weak bonds that hold the folds, so the chain unravels: this is denaturing. Egg white turns from clear to white, milk curdles with lemon juice, meat firms up. The peptide bonds stay, so the amino acids are all still there; your stomach does the same thing with acid.

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Figure 6

Digestion and Use

Back to amino acids, into the pool, and out as urea.

From plate to amino acids
  1. Mouthchewing only; no protein digestion
  2. Stomachacid unfolds proteins; pepsin cuts them into shorter pieces
  3. Small intestinetrypsin and chymotrypsin from the pancreas, then enzymes on the gut wall, cut down to single amino acids and pairs or threes
  4. Into the bloodabsorbed and carried to the liver first
  5. The amino acid poolyour body’s supply, used to build proteins all day

The small intestine also absorbs some pairs and threes of amino acids, which are split inside the gut-wall cells.

What the pool is used for
BuildingMuscle, skin, hair, bone matrix (collagen) and the lining of the gut, all constantly broken down and rebuilt.
Working proteinsEnzymes that run chemical reactions, antibodies, hemoglobin and other carriers, and hormones such as insulin.
Fuel, lastAmino acids not needed for building are burned for energy (4 kcal per gram) or turned into glucose or fat. The body doesn’t store spare protein.
Getting rid of the nitrogen

Urea, CH4N2O how the nitrogen leaves

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  1. 1Two nitrogens: when an amino acid is burned, its amine group comes off as ammonia, which is toxic. The liver packs it into urea, and the kidneys send it out in urine.

In your body: Protein builds and repairs every tissue and makes enzymes, antibodies and many hormones.

Too little: Too little over time causes muscle loss, slow healing, weaker immunity, thin hair and, in severe shortage, swelling from fluid (kwashiorkor) and poor growth in children.

Too much: Extra protein is burned or stored as fat, and makes more urea to clear, so you need a little more water. Very high intakes are a concern mainly for people with kidney disease.

Following one amino acid: alanine

Alanine, C3H7NO2its amine group (NH₂) holds the nitrogen; the rest is the carbon skeleton

The nitrogen → urea

1 · The amine group comes off. Alanine hands it to another molecule (transamination), and the liver then pulls it off as ammonia (deamination).

Ammonia, NH₃toxic, even in small amounts

2 · The urea cycle, in the liver. Two nitrogens, one from ammonia and one passed in by another amino acid (aspartate), are joined to one carbon and one oxygen, which come from CO₂.

Urea, CH4N2Oharmless and dissolves in water

3 · Out of the body: blood → kidneys → urine

The carbon skeleton → fuel, glucose or fat

What’s left once the amine group is gone is pyruvate: the same three carbons, with a C=O where the amine group was.

Pyruvate, C3H4O3drawn as pyruvic acid, like the amino acids

Then one of three fates:

Burned for energypyruvate → acetyl-CoA → citric acid cycle → CO₂ + water + energy (ATP)

Made into glucosein the liver, when blood sugar runs low

Made into fatwhen there’s more than you need: through acetyl-CoA into fatty acids

Every amino acid splits the same way: its nitrogen leaves as urea, and its carbon skeleton is burned or rebuilt. Same scale as every molecule on this page; tap one to enlarge it.

carbon hydrogen oxygen nitrogen · every molecule on this page is drawn at the same scale with every hydrogen shown · tap one to enlarge it

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Figure 7

Complete and Incomplete Protein

Which foods have all 9 essentials, and how to combine the rest.

Complete and incomplete foods
FoodProtein typeLowest essential amino acid
Meat, poultry, fishCompletenone
Eggs, milk, yogurt, cheeseCompletenone
Soybeans (tofu, tempeh, edamame)Completenone really (methionine a little low)
Quinoa, buckwheatComplete, or closenone really
Beans, lentils, peas, chickpeasIncompletemethionine (and cysteine)
Wheat, rice, oats, cornIncompletelysine
Nuts and seedsIncompletelysine (most)
Putting plant proteins together
Limiting amino acidA protein is only as useful as its scarcest essential amino acid. Your body can’t build a protein when one is missing.
Beans + grainsBeans are low in methionine but rich in lysine; grains are the opposite. Together they cover each other: rice and beans, hummus and pita, peanut butter on whole-wheat bread.
Over the day is fineThe amino acid pool lasts for hours, so the foods don’t have to be eaten in the same meal, just over the course of the day.
How much you need
Adults: 0.8 g per kgThe US RDA is 0.8 grams of protein per kilogram of body weight per day: about 56 g for a 70 kg (154 lb) adult.
More at some stagesPregnancy and breastfeeding need more; growing children need more per kilogram; some research suggests older adults benefit from a little more.
Found inMeat, poultry, fish, eggs, dairy, beans, lentils, peas, soy, nuts, seeds and whole grains.
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Figure 8

Where protein is used in the body

Tap a number on the cell to see what that part does; the list below it gives every other place in the body.

Digested to amino acids, then built back into the proteins that do almost every job in the body.

Inside a cell

A typical animal cell, not to scale. Real cells hold thousands of ribosomes and hundreds of mitochondria.

Every cell builds its own proteins from amino acids. Here is where each step happens, in a typical cell.

  1. DNA holds the gene for every protein. It is wound on spools of histone proteins, and a gene is copied into messenger RNA (mRNA) to send out.
  2. Read the mRNA and join amino acids one by one with peptide bonds. Free ribosomes make the proteins that stay in the cytosol.
  3. Ribosomes on it make proteins for export or for membranes. Inside, the chain folds and S–S links form.
  4. Adds sugar tags, sorts the finished proteins and ships them in little sacs to the membrane or out of the cell, like albumin from liver cells.
  5. The fluid inside the cell, crowded with enzyme proteins that run its reactions, such as breaking glucose down for energy.
  6. Their enzymes burn fuel and their protein machines make ATP. The carbon from spare amino acids is burned here too.
  7. Protein fibers that give the cell its shape and move things around inside it. In muscle cells, actin and myosin slide past each other to contract.
  8. Channel and carrier proteins let amino acids, glucose and salts in and out; receptor proteins catch signals such as insulin.
  9. Small sacs of enzymes that break worn-out proteins and cell parts back down to amino acids for reuse.

Everywhere else in the body

Each item, the places outside the cell where it is found or used, and what it does there.

Digesting protein

  • Stomach. Acid unfolds proteins and pepsin starts cutting them.
  • Pancreas. Sends trypsin, chymotrypsin and other enzymes into the small intestine.
  • Small intestine. Its lining finishes the job and absorbs amino acids and small peptides into the blood.

Proteins that move you

  • Skeletal muscle. Holds about 40% of body protein; actin and myosin slide past each other to contract.
  • Heart. Its muscle uses the same proteins for every beat.
  • Gut and blood vessel walls. Smooth muscle squeezes food along and sets vessel width.

Proteins that hold you together

  • Skin. Collagen gives it strength and elastin lets it stretch back.
  • Bones and teeth. A collagen framework holds the minerals.
  • Tendons, ligaments and cartilage. Mostly collagen.
  • Arteries and lungs. Elastin lets them stretch and recoil.
  • Hair, nails and outer skin. Made of keratin.
  • Eyes. Collagen keeps the cornea clear; crystallin proteins make the lens.

Proteins in the blood

  • Liver. Makes albumin, which holds water in the blood and carries things, and the clotting factors such as fibrinogen.
  • Red blood cells. Hemoglobin carries oxygen.
  • Blood. Carrier proteins move iron, fats and hormones.

Defense

  • Bone marrow, lymph nodes, spleen and gut lining. Plasma cells there make antibodies that tag germs.
  • Skin and mucus. Protein barriers and germ-killing enzymes such as lysozyme in tears and saliva.

Protein hormones

  • Pancreas. Insulin and glucagon.
  • Pituitary gland. Growth hormone, ADH and oxytocin.
  • Parathyroid glands. PTH, which raises blood calcium.
  • Kidneys. EPO, which tells the marrow to make red blood cells.
  • Fat tissue. Leptin, which signals how much fat is stored.
  • Gut. Gastrin, CCK and other digestion signals.

Amino acids made into other things

  • Brain. Serotonin from tryptophan, dopamine from tyrosine, and GABA and glutamate.
  • Adrenal glands. Adrenaline from tyrosine.
  • Thyroid. Thyroid hormones are built on tyrosine.
  • Skin and hair. Melanin, the pigment, from tyrosine.
  • Bone marrow. Heme is built from glycine.
  • Liver, kidneys and muscle. Creatine is made in the kidneys and liver and stored in muscle for quick energy.
  • Breast milk. Casein and whey proteins feed the baby.

Spare amino acids

  • Liver. Removes their nitrogen as urea and turns the rest into glucose, fat or energy.
  • Kidneys. Send urea out in urine and use glutamine to balance acid.
  • Muscle. In a fast, breaks some protein down to supply amino acids.
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Figure 9

Putting It All Together

The whole lesson in one table, plus a few extras.

The whole lesson in one table
IdeaIn one lineSee
AtomsC, H, O and N (plus S): nitrogen is what sets protein apart from fat and carbohydrateFigure 2
Amino acidAmine + alpha carbon + carboxyl + one side chainFigure 2
Peptide bondCarboxyl of one joins the amine of the next; one water releasedFigure 3
20 amino acids9 essential, 6 conditionally essential, 5 non-essentialFigure 4
ShapePrimary, secondary, tertiary, quaternary; cooking unfolds itFigure 5
DigestionBack to amino acids; nitrogen leaves as ureaFigure 6
FoodAnimal foods and soy are complete; combine beans and grainsFigure 7
Worth knowing

Protein powders are just protein

Whey and casein come from milk, and pea and soy powders from those plants. They give the same amino acids as the whole foods, without the fibre, vitamins and minerals that come along in the food.

Collagen is incomplete

Collagen, the most common protein in your body, is rich in glycine and proline but has almost no tryptophan, so on its own it’s an incomplete protein.

Gelatin is cooked collagen

Simmering bones and skin unfolds collagen into gelatin, which sets into a gel as it cools.

Protein quality scores

PDCAAS and DIAAS score proteins by their essential amino acids and how well they are digested. Milk, eggs and soy score near the top.

General education, not medical advice. Facts follow mainstream sources (US Dietary Guidelines, NIH Office of Dietary Supplements, standard biochemistry and food-science texts).

Quiz

Tap a question to see the answer

1. How many kcal does a gram of protein give?

About 4, the same as carbohydrate (Figure 1).

2. Which atom do proteins have that fats and carbohydrates don’t?

Nitrogen, in the amine group of every amino acid (Figure 2).

3. What three parts do all amino acids share, and what part differs?

An amine group, an alpha carbon and a carboxyl group are shared; the side chain (R group) differs (Figure 2).

4. What is released when a peptide bond forms?

One water molecule: an OH from one amino acid’s carboxyl and an H from the next one’s amine (Figure 3).

5. How many amino acids are essential? Name three.

Nine: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine (Figure 4).

6. Which essential amino acid contains sulfur?

Methionine (cysteine, a conditionally essential one, has sulfur too) (Figure 4).

7. What does cooking an egg do to its proteins?

It denatures them: the folds unravel, but the peptide bonds and amino acids stay (Figure 5).

8. Where does protein digestion start, and which enzyme begins it?

In the stomach, where acid unfolds proteins and pepsin starts cutting them (Figure 6).

9. What happens to the nitrogen when amino acids are burned for energy?

It comes off as ammonia, the liver turns it into urea, and the kidneys remove it in urine (Figure 6).

10. Why do rice and beans go well together?

Grains are low in lysine and beans in methionine; each supplies what the other lacks (Figure 7).

11. What is the US RDA for protein for adults?

0.8 grams per kilogram of body weight per day, about 56 g for a 70 kg adult (Figure 7).

12. Is collagen a complete protein?

No; it has almost no tryptophan (Figure 9).

Next lesson: Module 1 · Carbohydrates →