Exam 1 Study Guide Review

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78 Terms

1

strength order of bonds (strongest to weakest)

ionic, covalent, hydrogen, Van der Waals

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2

ionic bond

transfer of valence electrons between atoms; forms a salt

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3

covalent bond

sharing of valence electrons by two atoms

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4

molecule

consist of two or more atoms held together by covalent bonds (single, double or triple); smallest units of compounds that retains the characteristics of the said compound

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5

nonpolar covalent bond

equal sharing of valence electrons; usually between atoms of the same element or two elements with similar electronegativities

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6

polar covalent bond

unequal sharing of valence electrons

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7

electronegativity

an atom’s strength of attraction/pull on the valence electrons

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8

hydrogen bond

the non-covalent attraction between a hydrogen and an electronegative atom when the hydrogen atom has a partial positive charge

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9

hydrogen bond example

the hydrogen (partial positive) of one H2O molecule will be attracted to the oxygen (partial negative) of another molecule

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10

Van der Waals interaction

ever-changing regions of positive and negative charge that enable all atoms and molecules to stick to one another

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11

the 4 properties of water

cohesive behavior, ability to moderate temperature, expansion upon freezing, universal solvent

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12

cohesive behavior

the linking of like (water) molecules; results in surface tension

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13

surface tension

measure of how difficult it is to stretch or break the surface of a liquida

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14

adhesion

the clinging of one substance (water) to another; helps to counter gravity

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15

ability to moderate temperature

water has a high specific heat capacity (it takes a lot of energy to change the temperature of one gram of water molecules by 1 degree C

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16

example of water’s ability to moderate temperature

an elephant sprays water on itself to cool itself through vaporization

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17

expansion upon freezing

water is less dense as a solid than as a liquid

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18

universal solvent

water eventually dissolves all ions by forming a hydration shell around its atoms

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19

hydration shell

a sphere of water molecules around a dissolve ion

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20

functional groups

components of organic molecules that are most involved in chemical reactions

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21

kinetic energy

energy of motionth

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22

thermal energy

kinetic energy created by the random motion of atoms and molecules

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23

temperature

a measure, in degrees, of the average kinetic energy (thermal energy) of the atoms and molecules in a substance

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24

carbon structure properties

length, branching, double bond position, presence of rings

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25

isomers

compounds with the same molecular formula but different structures and properties

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26

structural isomers

different covalent arrangements of atoms

<p>different covalent arrangements of atoms</p>
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27

cis-trans (geometric) isomers

same covalent bonds that differ in their spatial arrangements

<p>same covalent bonds that differ in their spatial arrangements</p>
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28

enantiomers

isomers that are mirror images of each other

<p>isomers that are mirror images of each other</p>
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29

essential elements in humans

carbon, hydrogen, oxygen, nitrogen (CHON)

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30

trace essential elements

iron and iodine

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31

pH=-log[H+]

more H+ atoms = lower pH

<p>more H+ atoms = lower pH</p>
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32

Which structures are affected by sickle cell anemia?

primary and quaternary

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33

Which structures are affected by denaturation?

secondary, tertiary and quaternary

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34

prokaryotic cells

smaller, have a nucleoid region, are unicellular, have circular DNA, have no membrane-bound organelles, have all seven characteristics of life

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35

eukaryotic cells

larger, have a nucleus, have membrane-bound organelles, have linear DNA, can be unicellular or multicellular, have all seven characteristics of life

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36

What are the similarities between prokaryotic and eukaryotic cells?

both are cells, and both have the seven characteristics of life

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37

Thiomargarita magnifica

prokaryote with prokaryotic ribosomes and circular DNA, but contains an enclosed nucleus and vacuole (membrane-bound organelles); exclusion of the differences between prokaryotic and eukaryotic cells

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38

advantages to compartmentalization

higher metabolism, more metabolic reactions, can undergo catabolic/anabolic reactions with many molecules, each compartment can have its own chemical/physical environment, allows division of labor amongst organelles

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39

nucleic acids

polymers made of monomers called nucleotides; have a phosphate group, sugar (ribose), and a base group; held together by a phosphodieter bond

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40

phosphodieter bond

between the phosphate group of one nucleic acid to the hydroxyl group of another nucleic acid

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41

lipids

any of a large group of large biological molecules that mix poorly with water; have hydroxyl, carboxyl, and phosphate groups; held together by Ester linkages

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42

Ester linkage/bond

between the hydroxyl of a glycerol and the carboxyl group of a fatty acid (lipids)

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43

trans fats

unsaturated fatty acids that try to mimic the linear shape of a saturated fatty acid

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44

amino acids

have an amino and carboxyl functional group; form peptide bonds

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45

proteins

a biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific 3-dimensional structure

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46

8 proteins necessary for life

  1. enzymatic

  2. defensive

  3. storage

  4. transport

  5. hormonal

  6. receptor

  7. contractile

  8. structural

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47

carbohydrates

have a carbonyl and hydroxyl group; normally ring-shaped; utilize a glycosidic linkage

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48

glycosidic linkage

bond between hydroxyl groups (carbohydrates)

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49

What is the difference between carbohydrates and lipids?

Carbohydrates store short-term energy and are more concentrated in plants whose seeds germinate quickly. Lipids store long-term energy because of their higher energy content, and are more concentrated in plants whose seeds undergo large stages of dormancy.

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50

main functions of compartmentalization

  • environmental interactions

  • hereditary information transmission

  • genetic information storage

  • energy and matter transformation

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51

example of enzymatic proteins

digestive enzymes

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52

example of defensive proteins

antibodies

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53

example of storage proteins

ovalbumin in eggs

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54

example of transport proteins

hemoglobin in blood

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55

example of hormonal proteins

insuline

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56

example of receptor proteins

receptor-mediated endocytosis

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57

examples of contractile proteins

actin and myosin

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58

examples of structural proteins

keratin or collagen

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59

examples of environmental interactions between compartments

plasma membranes and differing chemistries

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60

examples of hereditary information transmission

turning genes into proteins

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61

example of genetic information storage

storage of DNA in the nucleus

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62

examples of energy and matter transformation

anabolism/catabolism, photosynthesis

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63

What is the difference between starch and cellulose?

Starch has an alpha glycosidic linkage, which is digestible by humans. Cellulose has a beta glycosidic linkage, which is not digestible by humans.

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64

smooth endoplasmic reticulum function

produces lipids and stores ions

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65

rough endoplasmic reticulum function

studded with ribosomes; produces proteins

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66

lysosome function

hydrolysis

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67

hydrolysis

the chemical breakdown of a compound with water

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68

golgi body function

folds proteins and makes vesicles for transport

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69

golgi body structure

has a “receiving” side (trans face) and a “shipping” side (cis face)

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70

Which linkages belong to which type of macromolecule?

  • carbohydrates: glycosidic linkages

  • lipids: ester linkages

  • proteins: peptide bonds

  • nucleic acids: phosphodieter linkages

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71

primary structure of proteins

linear sequence of amino acids

<p>linear sequence of amino acids</p>
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72

secondary structure of proteins

folding patterns of the polypeptides (alpha-helix or beta-pleated sheets)

<p>folding patterns of the polypeptides (alpha-helix or beta-pleated sheets)</p>
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73

tertiary structure of proteins

3-dimensional shape of a single polypeptide chain; determined by interactions between amino acid side chains

<p>3-dimensional shape of a single polypeptide chain; determined by interactions between amino acid side chains</p>
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74

quaternary structure of proteins

arrangement of multiple polypeptide chains within a protein complex

<p>arrangement of multiple polypeptide chains within a protein complex</p>
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75

glycosidic linkages

linkage/bond for carbohydrates

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76

ester linkages

linkage/bond for lipids

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77

peptide bonds

linkage/bond for proteins

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78

phosphodieter linkages

linkage/bond for nucleic acids

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