Bio Chapter 1-5 Test

Front 1

Functions common to all life

Back 1

-Nutrition

-Transport/Distribution

-Respiration

-Excretion

-Response to environment

-Reproduction

Front 2

Themes of biology

Back 2

1. Organization

2. Information

3. Energy and matter

4. Interactions

5. Evolution

Front 3

Domain Bacteria

Back 3

Bacteria

Front 4

Domain Archaea

Back 4

prokaryotes know as archaea

Front 5

Domain Eukarya

Back 5

-Kingdom Plantae

-Kingdom Fungi

-Kingdom Protists

-Kingdom Animalia

Front 6

Proton

Back 6

- +1 charge

- 1 dalton

- Location nucleus

Front 7

Neutron

Back 7

-Neutral charge

- 1 dalton

- Location nucleus

Front 8

Electron

Back 8

- Charge -1

- negligable

- Location Outside

Front 9

Maximum number of electrons in each energy shell

Back 9

- 1st shell- 2 electrons

- 2nd shell- 8 electrons

- 3rd shell- 8 electrons

Front 10

What is 1H2 1H3

Back 10

deuterium

tritium

Front 11

Atomic weight

Back 11

measured in units called daltons

- 1 dalton= 1 proton

Front 12

What is a mole?

Molarity?

Back 12

6.02 x 10^23

Molarity is the number of moles of solute per liter of solution

Front 13

Isotopes

Back 13

- Stable isotopes

- Unstable isotopes- Raidoactive

-helpful

- harmful

Front 14

Half-life

Back 14

- A fixed amount of time for half the quanity of a particular isotope to decay to a stable element.

- U238 - 4.5 billion years

- C14 - 5,730 years

Front 15

Enegry

Back 15

the capacity to do work

Front 16

Potential energy

Back 16

the energy that matter has because of its location or structure

Front 17

Ionic bonds

Back 17

lose or gain electrons

Front 18

Covalent bonds

Back 18

-share electrons

-strong bonds

-polar

-nonpolar

Front 19

Electronegativity scale

Back 19

- O=3.5

- N=3.0

- C=2.5

- H=2.1

Front 20

Non polar covalent bonds

Back 20

- Atoms have similar electronegativity

- Electrons are shared equally

Front 21

Polar covalent bonds

Back 21

- Unequal sharing of electrons

- Atoms become slightly charged

- i.e. H2O

Front 22

Ionic bonds

Back 22

-Formed by the movement of electrons from one atom to another.

- Attraction between a cation and anion

Front 23

1. Cation

2. Anion

Back 23

1. positively charged ion

2. negatively charged ion

Front 24

Hydrogen bonds

Back 24

- Weak

- Forced attraction between polar covalent or charged regions of molecules

Front 25

Van der Waals Interactions

Back 25

- Asymmetric arrangement of ions resulting in "hot spots" of positive or negative charge.

- Causes attractions between molecules that are close together as a result of these charges.

- i.e. interactions between molecules of a gecko's toe hairs and a wall surface.

Front 26

Water's Properties

Back 26

1. Cohesive behavior

2. Ability to moderate temperature

3. Expansion upon freezing

4. Versatility as a solvent

Front 27

Cohesion and Adhesion

Back 27

-Cohesion: when the molecules want to be together (they stick)

- i.e. surface tension

-Adhesion: water bondng to the glass being held together by hydrogen bonds. The glass is charged as well

Front 28

Temperature vs. Heat

Back 28

-Temperature: measures of the average kinetic energy of the molecules

-Heat: total kinetic energy of the molecules

Front 29

Calorie

Back 29

amount of heat required to raise the temperature of 1g of water by 1 degree C

Front 30

What causes water's high specific heat?

Back 30

Hydrogen bonds

Front 31

Water expands when it freezes

Back 31

- Maximum density a 4 degree C.

- Below freezing hydrogen bonds resist breaking and lock water molecules in an expanded lattice-like bonding pattern

-Ice is less dense than water so it floats

Front 32

1. Solution

2. Solvent

3. Solute

4. Aqueous solution

Back 32

1. a liquid that is completely homogeneous mixture of substances.

2. the dissolving agent of the solution

3. the substance that is dissolved

4. one in which water is the solvent

Front 33

Hydrophilic

Hydrophobic

Back 33

- Ions and polar covalent molecules easily dissolve in water

- Nonpolar substances will not dissolve in water

-Hydrocarbons

- Fats and Oils

Front 34

Hydrogen ion (H+)

Back 34

- The hydrogen atom leaves its electron behind and is transferred as a proton

Front 35

Hydroxide ion (OH-)

Back 35

Molecule that has lost the proton

Front 36

Hydroniumion (H3O+)

Back 36

Molecule with the extra proton.

Often represented as (H+)

Front 37

Acid

Back 37

a substance that gives off hydrogen ions in a solution.

increases the [H+] concentration

Front 38

Base

Back 38

a substance which removes hydrogen ions from a solution thereby reducing the [H+] concentration

Front 39

Buffers

Back 39

substances that minimize changes in concentration of H+ and OH- in a solution

Front 40

Wohler (1828)

Back 40

Synthesis of urea

Front 41

A.I. Oparin (1924)and John Haldane (1929)

Back 41

Hypothesizes that the primitive atmosphere was a reducing atmosphere

H2 NH3 CH4 H2O

Organic compounds were synthesized in the primitive oceans

Front 42

Harold Urey (1893-1981)

Back 42

University of Chicago

won Nobel prize in chemistry for the discovery of deuterium

Front 43

Stanley Miller (1953)

Back 43

Miller-Urey experiment to test the Oparin-Haldane hypothesis

Front 44

What makes molecules different

Back 44

- Length and configuration of carbon chain

- Types of covalent bonds

- Presence of other elements

- Isomers

- Functional groups

Front 45

1. Methane

2. Ethane

3. Propane

4. Octane

5 Ethene

6. Ethyne

Back 45

1. CH4

2. C2H6

3. C3H8

4. C8H18

5. C2H4

6. C2H2

Front 46

Isomer

Back 46

Same molecular formula but different structures and properties

Front 47

Seven most important functional groups

Back 47

1. Methyl group

2. Hydroxyl group

3. Carbonyl group

4. Carboxyl group

5. Amino group

6. Sulfhydryl group

7. Phosphate group

Front 48

Adenosine triphosphate (ATP)

Back 48

important source of energy for cellular processes

Adenosine attached to three phosphate groups

Front 49

Classes of large biological molecules

Back 49

1. Carbohydrates

2. Lipids

3. Proteins

4. Nucleic acids

Front 50

Polymer

Monomer

Back 50

Polymer: Carbohydrate

Protein

Nucleic Acid

Monomer: Simple sugar

Amino acid

Nucleotides

Front 51

Dehydration synthesis

Back 51

Bonding of two monomers through the loss of a water molecule

Front 52

Hydrolysis

Back 52

The revers of dehydration synthesis

Front 53

Monosaccharides

Back 53

CH2O

Can be anywhere from C3 to C7

triose sugars, pentose sugars, hexose sugars

Front 54

Disaccharides

Back 54

formed when a dehydration reaction joins two monosaccharides

bond called glycosidic linkage

Front 55

Polysaccharides

Back 55

storage of glucose

structural roles (determined by its sugar monomers and the position of glycosidic linkages)

siginals in the cell

Front 56

Starch and Glycogen

Back 56

Starch: a storage polysaccharide of plants (consists of entirely glucose monomers)

Glycogen: a storage polysacchride in animals (consists entirely of glucose monomers)

Front 57

Lipids

Back 57

-Not polymers

- Composed of CHO

CHO not 2:1 ratio of H:O

- Hydrophobic

-Fats, Phosopholipids, Steroids

Front 58

Fats

Back 58

-Nutrient storage

-Insulation

-Cushion

-Composed of:

-3 fatty acids and 1 glycerol

- fatty acids are joined to glycerol by an ester linkage

-Triglyceride

Front 59

Protein

Back 59

-Control of chemical reactions

-Structural support

-Storage

-Transport

-Cellular communications

-Movement

-Defense against foreign substances

-is a biologically functional molecule that consists of one ore more polypeptides

Front 60

Amino Acid

Back 60

organic molecules with carboxyl and amino groups

differ on their R group

there are 20

Front 61

Nonpolar side chains; hydrophobic

Back 61

1. Glycine

2. Alanine

3. Valine

4. Leucine

5. Isoleucine

6. Methionine

7. Phenyalanine

8. Tryptophan

9. Proline

Front 62

Polar side chains; hydrophilic

Back 62

1. Serine

2. Threonine

3. Cysteine

4. Tyrosine

5. Asparagine

6. Glutamine

Front 63

Electrically charged side chains; hydrophilic

Back 63

Acidic (negatively charged)

1. Aspartic acid

2. Glutamic acid

Basic (positively charged)

1. Lysine

2. Arginine

3. Histidine

Front 64

Protein structure

Back 64

functional protein consist of one or more polypeptids precisely twisted, folded, and coiled into a unique shape

sequence of amino acids determine the 3D structure

Front 65

Four levels of Protein structure

Back 65

1. Primary: unique sequence of amino acids

2. Secondary: coils and folds the popypeptide chain. Determined by hydrogen bonds

3. Tertiary: Globular structure. Formed from interactions among various side chains

4. Quaternary: consists of multiple polypeptide chains. Interfolding of multiple polypeptides

Front 66

Denaturation

Back 66

the loss of a protein's native structure, becomes biologically inactive

Front 67

Nucleic acids

Back 67

store, transmit, and help express hereditary information.

the amino acid sequence of a polypeptide is programmed by a gene

Genes are made of DNA

DNA is a nucleic acid made of monomers called nucleotides

Two types: DNA and RNA

Front 68

DNA and RNA

Back 68

DNA: provides directions for its own replication. Directs synthesis of messenger RNA which controls protein synthesis (mRNA)