Ap Biology Chapter 3

Front 1

Lactase

Back 1

Secreted by the digestive cells in the small intestine to absorb sugars from milk.

Front 2

Enzyme

Back 2

A protein which speeds up a specific chemical reaction.

Front 3

Organic compounds

Back 3

Carbon-based molecules

Front 4

Hydrocarbons

Back 4

Composed of only carbon and hydrogen

Front 5

Isomer

Back 5

Compound with the same molecular formula as another compound, but a different structure. Ex: butane and isobutane

Front 6

Functional groups

Back 6

The groups of atoms that usually participate in chemical reactions in organic chemistry

Front 7

Characteristic of functional groups

Back 7

All are polar, which tends to make compounds containing them hydrophilic (water-loving)and souble in water.

Front 8

Hydroxyl

Back 8

-OH in alcohols

Front 9

Carbonyl

Back 9

>C=O
Called a ketone in the middle of a carbon chain, and an aldehyde at the end.

Front 10

Carboxyl

Back 10

-COOH
Acts as an acid by donating H+ to make carboxylic acids

Front 11

Amino

Back 11

N<
Make amines. Picks up H+ from solution: base.

Front 12

Phosphate

Back 12

-OPO3 with a -2 charge. Make organic phosphates. Involved in energy transfers

Front 13

Macromolecules

Back 13

Large biological molecules, include carbs, lipids, proteins, nucleic acids. Can have 1000+ atoms.

Front 14

Monomer

Back 14

Building blocks of polymers

Front 15

Polymer

Back 15

Large molecule with many identical or similar molecular units strung together

Front 16

Dehydration reaction

Back 16

Removes a molecule of H2O and joins two polymers (or monomer and polymer) one donating OH- and one donating H+ to the reaction.

Front 17

Hydrolysis

Back 17

Opposite of dehydration reaction. Breaks apart polymers by adding H2O to them.

Front 18

Monosaccharides

Back 18

Carbohydrate monomers. Molecular formulas are a multiple of CH2O.

Front 19

Sugar

Back 19

A number of hydroxyl groups and a carbonyl group.

Front 20

Disaccharides

Back 20

Formed by linking two monosaccharides with a dehydration reaction

Front 21

Sucrose

Back 21

Glucose + fructose

Front 22

Maltose

Back 22

Glucose and glucose

Front 23

Lactose

Back 23

Glucose + galactose

Front 24

Polysaccharides

Back 24

Long chains of sugar units

Front 25

Starch

Back 25

In roots an dother tissues of plants (only glucose monomers). Serve as sugar stockpiles. Humans use starch by hydrolyzing it in digestive systems.

Front 26

Glycogen

Back 26

Where animals store excess sugar. More highly branched than starch. Most stores in liver and muscle cells, which hydrolyze the glycogen to use glucose when needed.

Front 27

Cellulose

Back 27

Most abundant organic compound on Earth. Polymer of glucose. Monomers form an unbranched rod, not coil. Joined by H- bonds.

Front 28

Insoluble Fiber

Back 28

Cows and termites have cellulose-hydrolyzing microorganisms inside them.

Front 29

Lipids

Back 29

C and H atoms linked by NONPOLAR covalent bonds. Hydrophobic.

Front 30

Fat

Back 30

Large lipid mde from glycerol and fatty acids

Front 31

Glycerol

Back 31

Fatty acid. Main function of fat is energy storage.

Front 32

Triglyceride

Back 32

3 fatty acids and 1 glycerol linked by a dehydration reaction.

Front 33

Unsaturated

Back 33

Less than max hydrogens.

Front 34

Saturated

Back 34

Only single bonds. Max number of hydrogens.

Front 35

Phospholipids

Back 35

Like fats, but contain phosphorus and 2 fatty acids.

Front 36

Wax

Back 36

One fatty acid and an alchohol. More hydrophobic than fats.

Front 37

Steroids

Back 37

Lipids wth a carbon skeleton bent to form four fused rings. Always 3 six-sided rings and one five sided ring

Front 38

Anabolic steroids

Back 38

Synthetic variant of testosterone. Use can alter mood, liver function, high blood pressure, infertility, cardiovascular probs.

Front 39

Anabolism

Back 39

Building of substances by the body

Front 40

Proteins

Back 40

Polymers consisting of amino acid monomers

Front 41

Proteins in the body

Back 41

Muscles contain contractile proteins, antibodies, hemoglobin (transport protein for O2), ovalbumin (storage source of amino acids for embryos)

Front 42

How are proteins made?

Back 42

Proteins are made from amino acids linked by peptide bonds

Front 43

Shape of enzymes

Back 43

Globular. like lysozyme in tears and white blood cells

Front 44

Shape of structural proteins

Back 44

in hair and tendons. Long and thing (fibrous)

Front 45

High temperatures and proteins

Back 45

Can denature proteins (change shape). This is why high fevers can be dangerous.

Front 46

Primary protein structure

Back 46

Unique sequence of amino acids. Slight change can affect its ability to function

Front 47

Secondary protein structure

Back 47

Parts of the polypeptide folded or coiled, alpha helix, or pleated sheet.

Front 48

Tertiary protein structure

Back 48

3D shape of polypeptide. Globular or fibrous. Restults from interactions among the R groups of the amino acids. May be reinforced further by covalent bonds (disulfide bridges)

Front 49

Quaternary protein structure

Back 49

Results from the polypeptide chains (subunits). Collagen has 3 pp. chains in a triple helix.

Front 50

Linus Pauling

Back 50

Found out how hemoglobin carries O2 and how abnormal hemoglobin causes sickle-cell disease. Alpha helix & pleated sheet, also.

Front 51

Nucleic acids

Back 51

Polymers which are blueprint for proteins

Front 52

DNA

Back 52

Deoxyribonucleic acid. Double helix shape. A pairs with T, and G with C.

Front 53

Interaction btwn. DNA and RNA

Back 53

Dna's info is transcribes into RNA, which is translated into primary structure of proteins.

Front 54

Genes

Back 54

Specific parts of DNA molecule that program amino acid sequences (primary structure)

Front 55

Nucleotides

Back 55

Monomers in nucleic acids (p.47). 5 carbon sugar (ribose or deoxyribose) + phosphate group + nitrogenous base.

Front 56

List the nitrogenous bases found in DNA

Back 56

A- adenine pairs with T- Thymine.
C- Cytosine pairs with G-Guanine.

Front 57

List the nitrogenous bases found in RNA

Back 57

Adenine, Cytosine, Guanine, Uracil (uracil pairs with adenine when it bonds with DNA).

Front 58

RNA's shape

Back 58

single polynucleotide strand.