Molecules Of Life

Front 1

Macromolecules

Back 1

Very large molecules that make up living things. We have lots of them. Made up of mostly Carbon, Hydrogen and Oxygen.

Are polymers made up of monomers.

Front 2

Polymers and Monomers

Back 2

Polymer- A large molecule consisting of many identical or similar building blocks linked by covalent bonds.

Monomers- The building blocks of a polymer.

Hint 2

Train

Front 3

Metabolism

Back 3

All enzyme reactions in the body. (build & break)

Front 4

Anabolism

Back 4

Chemical reaction (type of metabolism) that builds larger molecules from small ones through Dehydration Synthesis (condensation).

Front 5

Dehydration Synthesis Reaction

Back 5

Removes a water molecule, forming a new bond.

Front 6

Hydrolysis

Back 6

Adds a water molecule, breaking a bond.

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Carbohydrates

Back 7

Type of organic molecule mostly for energy. ( CH2O )x, carbón and water. In fruits, vegetables and grains.

Front 8

Catabolism

Back 8

Chemical reaction (type of metabolism) that breaks down large molecules into smaller ones through Hydrolysis. (occurs during digestion)

Front 9

Monosaccharides

Back 9

Single sugars with 3-7 carbons. Monomer. Hexose or Pentose (sided) rings. Used as a primary energy source. 3 types, all reducing sugars.

- glucose=blood sugar

- fructose=fruit sugar

- galactose=milk sugar

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Disaccharides

Back 10

Double sugars ( C12H22O11 ) of 2 monosaccharides. Used as energy source and building blocks for larger molecules.

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Polysaccharides

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Complex carbohydrates made up of several 100s/1000s of monosaccharides. Two types both made of entirely glucose.

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Types of Disaccharides

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Maltose- glucose + glucose

Lactose- glucose + galactose

( both reducing sugars)

Sucrose- glucose + fructose

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Storage polysaccharides

Back 13

For energy storage. Made of alpha glucose. Humans can digest.

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Alpha glucose

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Front 15

Glycogen

Back 15

Storage polysaccharides in animals. Found in liver and muscles, easily digested.

a1➡4 with a1➡6 branches

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Glycosidic linkages (alpha)

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a1➡4 straight line

a1➡6 branch

Front 17

Starch

Back 17

Storage polysaccharides in plants. Found in potatoes, legumes and grains.

Front 18

Types of starch

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Amylose- a1➡4

slower digestion, less space/soluble/common (20-30%)

Amylopectin- a1➡4 with a1➡6 branches

easily digested, more space/soluble/common (70-80%)

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Structural Polysaccharides

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Used as structural material. Made of beta glucose. Indigestible fibre.

Front 20

Beta Glucose

Back 20

Front 21

Chitin

Back 21

Structural polysaccharides in animals. B1➡4 often combined with calcium carbonate. Used by arthropods (insects, spiders and crustaceans) to build their exoskeleton.

Front 22

Cellulose

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Structural polysaccharides in plants. B1➡4, straight parallel chains held together by H-bond. Found in fruits, vegetables and grains. Makes cell wall.

Hint 22

Termites

Front 23

Glycosidic Linkages (beta)

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B1➡4

each upside down. H-bond. Straight parallel chains.

Front 24

Lipids

Back 24

Organic molecules with an oily, greasy or waxy consistency that are insoluble in water.

Found in meats, dairy, nuts and plant oil.

It's monomers are glycerol and fatty acid chains.

Front 25

Triglycerides

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Type of lipid with 3 fatty acids attached to a glycerol molecule.

Long term energy storage and physical and thermal insulation.

2.5 times more energy than carbs, but hard to transport in body.

Front 26

Fats

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Triglyceride of animal origin.

Solid at room temperature.

Saturated fatty acids, no double bonds.

Hint 26

Front 27

Oils

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Triglyceride of plant origin.

Liquid at room temperature.

Unsaturated fatty acids, aka double bonds.

Hint 27

Front 28

Double Bonds in Oil

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Cis- same side (healthier)

Trans- opposite side

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Hydrogenated

Back 29

Synthetically converted to saturated fats by adding Hydrogen.

( to be kept solid)

Hint 29

Margarine

Front 30

Phospholipids

Back 30

Type of lipid made up of a glycerol, 2 fatty acids and a phosphate.

Main component of cell membrane.

Hydrophilic head and Hydrophobic tails.

Front 31

Sterols (Steroids)

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Type of lipid with complex ring structure.

In hormones, for communication between cells.

Sex- testosterone, estrogen, progesterol

Stress- cortisol

Kidneys/blood pressure regulation- aldosterone

cholesterol

Front 32

Proteins

Back 32

Type of macromolecule with one or more polypeptides folded up or coiled together in a 3d shape (conformation).

Found in animal products and byproducts, nuts and legumes.

It's monomer are amino acids.

(20 different amino acids)

Structure: carbon with an amino group, a carboxyl group, a hydrogen and a variable R (functional) group.

Front 33

Polypeptides

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Polymers of many amino acids linked together by peptide bonds (covalent).

Each has an unique sequence of amino acids.

Sequence determines 3d shape,

3d shape determines function.

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Polarity of Amino Acids

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Determined by R groups, can be important to protein function.

Hydrophilic channels through membranes: polar amino acids allow polar substances through.

(non-polar embedded within the membrane, polar region portrudes)

Specifity of active sites: (&complementary shape) attract or repel substrate from active cite.

Hint 34

Straw

Front 35

Primary Structure of proteins

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The unique sequence of amino acids.

Determined by the DNA sequence.

A polypeptide.

Front 36

Secondary Structure of proteins.

Back 36

The coiling (alpha helix) and folding (beta pleated sheet) of sections of the amino acid.

Caused by Hydrogen Bonds.

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Tertiary Structure of proteins.

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The specific shape of the 3d folding of the entire polypeptide.

Interactions between the variable R groups.

A functional protein.

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Quartenary Structure of proteins.

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Two or more polypeptides grouped together into a functional protein.

Only for some.

Ex. hemoglobin

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Fibrous Proteins

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Long and narrow, with little or no tertiary structure.

Insoluble in water, have structural roles.

-collagen: strength in skin, tendons, cartilage and bone

-keratin: strength in hair and nails

-elastin: elasticity of arteries, lungs, skin and bladder

-myosin: contraction of muscle fibres

Front 40

Globular proteins

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Rounded shape with complex tertiary or quartenary structure.

Soluble in water with roles in metabolic reactions.

-enzymes

-immunoglobulins/antibiotics

-transport proteins

-hemoglobin: transport oxygen in red blood cells

Front 41

Functions of Proteins

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Chemical Reactions: enzymes

Structural Support: muscles, tendons, bones and ligaments

Movement: in muscles, actin and myosin

Defense: immune system

Transport: membrane transport

Cellular Communication: cell receptors and hormones, insulin

Front 42

Nucleic Acids (polynucleotides)

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Store and transmit hereditary information that controls cellular activity.

Monomer= Nucleotide containing a phosphate group, a sugar and a nitrogenous base.

Front 43

Nucleotide Sugars

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Front 44

Nucleotide Nitrogenous Bases

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Adenine

Thymine

Guanine

Cytytosine

And Uracil in RNA only

Front 45

DNA and RNA

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Deoxyribonucleic Acid: Stores genetic information in the nucleus. Double strand of polynucleotides in a double helix.

Sequence of nitrous bases in a section codes for sequence of amino acids in protein.

Ribonucleic Acid: "reading" the DNA code, protein synthesis. Makes a copy of the code, takes it to cytoplasm, makes a protein.

Single strand of polynucleotides.

Hint 45

Front 46

Micronutrients

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Required in very small amounts.

Vitamins: Organic molecules

-B & C water soluble.

Minerals: Inorganic molecules

Hint 46

V: scurvy

M: dancing frog legs, toothpaste

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Cohesión and Adhesion

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Cohesion: water's attraction to itself

Adhesion: water's attraction to other molecules

Hint 47

Plants