Biology Chapter 5 The Structure And Function Of Large Biomolecules

Front 1

Carbon

Hydrogen

Back 1

Organic molecules contain which two elements?

Front 2

Carbohydrates

Lipids

Proteins

Nucleic Acid

Back 2

Name 4 class of organic molecules in all living things

Front 3

Biomolecules

Macromolecules

Back 3

Organic molecules can also be called? (2 Terms)

Front 4

Organic Molecules

Back 4

- Always covalent bonding

- Often quite large, with many atoms

- Usually associated with living organisms

Front 5

Inorganic Molecules

Back 5

- Usually contain positive and negative ions

- Usually ionic bonding

- Always contain small number of atoms

- Often associated with nonliving matter

Front 6

Glycerol and Fatty Acids

- Does not form monomers

Fat

Back 6

What is a subunit of lipid?

Example of a polymer?

Front 7

Dehydration Reaction

Back 7

- Chemical reaction in which subunits are joined together by the formation of a covalent bond - water is produced during the reaction

Ex: Starch from glucose

Front 8

Hydrolysis reaction

Back 8

- Chemical reaction in which a water molecule is added to break a covalent bond

Ex: Glucose from starch

Front 9

Enzyme

Back 9

- Molecule that speeds up a chemical reaction

- Required for cells to carry out dehydration synthesis and hydrolysis reactions

- Not consumed, not changed in the reaction

Front 10

Carbohydrates

Back 10

- Energy source for living cells

- Provide structural building material

- Contain C, H, O in 1:2:1 ratio

Front 11

Monosaccharide

Back 11

- Also called simple sugars

- Backbone of 3 to 7 carbon atoms

- In aqueous solutions, form rings although drawn as linear skeletons

Front 12

Glucose (blood)

Fructose (fruit)

Galactose

Ribose

Deoxyribose (nucleotides)

Back 12

Give 3 examples of Hexose (6C) monosaccharides

2 Examples of Pentose (5C) monosaccharides

Front 13

Maltose (Glucose + Glucose)

Sucrose (Glucose + Fructose)

Lactose (Glucose + Galactose)

Back 13

Give 3 examples of disaccharides and their components

Front 14

Starch

Glycogen

Cellulose

Chitin

Peptidoglycan

Back 14

What provides energy storage in plants?

In animals?

Structurally, what are found in the cell walls of plants?

In the cell walls of fungi and exoskeleton of some animals?

In the cell walls of bacteria?

Front 15

Lipids

Back 15

- Vary in structure

- Do not form true polymers

- Large nonpolar molecules that are insoluble in water so called hydrophobic

Front 16

- Long-term energy storage

- Structural components of cells

- Cell communication/regulation

- Protection

- Fats, oils, waxes, phospholipids, steroids

Back 16

Give 4 Functions of Lipids and 5 Examples

Front 17

Fat

Back 17

- Long-term energy storage and insulation in animals

- Can be used as butter or lard

Front 18

Oils

Back 18

- Long-term energy storage in plants and their seeds

- Used for cooking

Front 19

Steroids

Back 19

- Component of plasma membrane as cholesterol, sex hormones

- Used as medicines

Front 20

Waxes

Back 20

- Protection, prevents water loss (cuticle of plant surfaces)

- Used as candles and polishes

Front 21

Triglycerides

- Glycerol molecule linked to 3 fatty acids

Back 21

- Long term energy storage and insulation

- Also called fats and oils (saturated or unsaturated)

- Name this compound and its structure

Front 22

Phospholipid

- Glycerol molecule linked to 2 fatty acid and phosphate group

- Phosphate head is hydrohilic, Fatty acid tail is hydrophobic

Back 22

- Component that form plasma membranes by forming lipid bilayer in water

- Name this component and its structure (Including which part is hydrophobic and hydrophilic)

Front 23

Steroids

- 4 Fused carbon rings

- Cholesterol, testosterone, estrogen

Back 23

- Various functional groups attached to a carbon skeleton

- Component of animal cell membranes and regulation

- Name this compound and its structure, then give 3 examples

Front 24

Cholesterol

Back 24

- Precursor molecule from which steroids are synthesized

Front 25

Waxes

- Long chain fatty acid bound to a long chain alcohol

Back 25

- Lipids solid at room temperature

- Impart waterproofing

- Resistant to degradation

- Provides protection such as in the plant cuticle

- Name this compound and its structure

Front 26

Peptide bond

Back 26

- Covalent bond between amino acids

Front 27

Protein

Back 27

Polypeptide that has folded into a particular shape and has a particular function

Front 28

Enzymatic Proteins

Back 28

- Type of protein that functions to provide selective acceleration of chemical reactions

Ex: Digestive ones catalyze the hydrolysis of bonds in food molecules

Front 29

Defensive Proteins

Back 29

- Type of protein that provides protection against disease

Ex: Antibodies inactivate and help destroy viruses and bacteria

Front 30

Storage Proteins

Back 30

- Type of protein that stores amino acids

Ex: Casein, protein of baby milk; ovalbumin, protein of egg white; plant seeds

Front 31

Transport Proteins

Back 31

- Type of protein that transports substances

Ex: Hemoglobin, proteins in cell membrane

Front 32

Hormonal Proteins

Back 32

- Proteins that function to coordinate organism's activities

Ex: Insulin - regulates blood sugar

Front 33

Receptor Proteins

Back 33

- Proteins that function to respond to chemical stimuli

Ex: Nerve cell membrane proteins detect signaling molecules released by other nerve cells

Front 34

Contractile/Motor Proteins

Back 34

- Proteins that are responsible for undulations of cilia and flagella

Ex: Actin and myosin

Front 35

Structural Proteins

Back 35

- Proteins that function as support

Ex: Keratin, collagen, elastin

Front 36

Amino Group

Side Chain Variable R Group

Carboxyl Group

Back 36

Structure of Amino Acid

Front 37

Denaturation

Back 37

- Proteins cannot function properly unless they fold into their proper shape - so when it loses its proper shape it is called?

- Can be caused by exposure to certain chemicals, change in pH, high temperature

Front 38

Primary: Sequence of amino acids

Secondary: Alpha helices or beta pleated sheets with hydrogen bonds

Tertiary: 3D shape of polypeptide, stabilized by hydrogen, ionic and covalent bonding

Quaternary: More than 1 polypeptide chain in association with one another

Back 38

Name then Describe 4 Levels of Structure of Proteins

Front 39

Chaperone Proteins

Back 39

- Help other proteins fold into their normal shape

- Defects in these can play role in Alzheimers and cystic fibrosis

Front 40

Prions

Back 40

- Misfoldded proteins that have been implicated in a group of fatal brain disease known as TSE's

Front 41

TSE

Back 41

- Group of fatal brain diseases

Ex: Mad Cow Disease

Front 42

Phosphate Group

Pentose Sugar

Nitrogen-containing base

Back 42

Structure of nucleotide

- They are joined together by a series of dehydration synthesis reactions to form a linear molecule called a strand

Front 43

Cytosine

Thymine

Uracil

Back 43

Pyrimidines

Front 44

Adenine

Guanine

Back 44

Purines

Front 45

Adenine

Ribose

3 Phosphates

Back 45

- High energy molecule due to the presence of the last two unstable phosphate bonds, which are easily broken

Name and describe the Structure of this compound

Front 46

Molecule ADP

Inorganic Phosphate

Energy

Back 46

3 Things that are yielded from the hydrolysis of ATP of its terminal phosphate bond