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118 Terms

1

molecule

substances composed of two or more covalently bonded atoms

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2

elements that make up the chemical foundation of life

CHNOPS - carbon, hydrogen, nitrogen, oxygen, phosphorus, sulfur

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3

intramolecular forces

forces within molecules that hold atoms together: covalent bonds or ionic bonds

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4

electronegativity

property of how strong an atom attracts electrons,

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5

polar covalent bond

unequal sharing of electrons

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6

non-polar covalent bond

when two atoms of similar electronegativities equally share electrons

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7

intermolecular forces

between molecules and determine how same type molecules interact, weaker than intramolecular forces, responible for attracting molecules but will break with enough force

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8

hydrogen bond

involves hydrogen atom and oxygen/nitrogen atoms, aqueous environments, hyrdophilic

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9

hydrophobic

non-polar that don’t form hydrogen bonds

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10

functional group

cluster of atoms that always behave in a certain way, contains ONPS

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11

structural formulas

show how the atoms are bonded together

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12

macromolecule

large complex molecules composed of repeating units of smaller molecuels, linked by covalent bonds

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13

polymers

long chain like substances that make up macromolecules

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14

monomers

a molecule that can be bonded to other identical molecules to form a polymer

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15

types of macromolecules

carbs, lipids, protien, nucleic acids

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16

carbohydrates

contain CHO, (CH2O)#carbon atoms, usually polar, sugars and starches

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17

monosaccharides

single carbon based monomer stuctures, simple sugar with 3 to 7 carbon atoms, glucose, fructose, galactose, energy

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18

disacchardies

two monosaccharides joined by glycosidic linkage, surose, lactose, energy

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19

glycosidic linkage

a type of ether bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate

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20

condensation reaction

forms glycosidic linkage, one monomer gives up hydroxyl group and other hydrogen, requires energy

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21

hydrolysis reaction

how glycosidic linkage is broken, water is split into hydroxyl group and hydrogen, releases energy

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22

polysaccharides

long chains of carbohydrate molecules, composed of several smaller monosaccharides, glycogen, starch, cellulose, storage, support/structure

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23

function of carbs

energy, storage, support/stucture

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24

functional groups of carbs

hydroxyl and carbonyl

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25

triglycerides

lipid molecules formed from one glucerol molecule bonded by ester linkages to three fatty acid molecules

<p>lipid molecules formed from one glucerol molecule bonded by ester linkages to three fatty acid molecules</p>
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26

ester linkage

formed between the oxygen molecules of glycerol and the hydroxyl molecules of fatty acids

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27

fatty acid

hydrocarbon chain ending in a carboxyl group

<p>hydrocarbon chain ending in a carboxyl group</p>
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28

saturated

no double bonds between carbon, straight line, solid

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29

unsaturated

monounsaturated (one double bond between carbond) or polyunsaturated (more than one double bond), bent, liquid

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30

phospholipids

main components of cell membranes, similar to triglycerides but phosphate group replaces third fatty acid

<p>main components of cell membranes, similar to triglycerides but phosphate group replaces third fatty acid</p>
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31

steriods

lipids composed of four attached carbon based rings, used for sending signals and membrane fluidity, differ based on functional groups

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32

waxes

lipids made of long carbon based chains, used for protection, solid

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33

functions of lipids

long term energy(tri), membranes(phospho), sending signals(steriods), protection(wax)

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34

functional groups of lipids

hydroxyl, carboxyl,

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35

dual nature of phospholipids

they have a polar head and non polar tail which creates a hydrophobic interior and the basics of a cell membrane when placed in water. the tails move together and the hydrophilic heads move outwards facing the water

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36

proteins

macromolecules composed of amino acids and linked by covalent bonds, made of polypeptides

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37

amino acid

orgainic molecules composed of central carbon atom bonded to an amino group, carboxyl group, hydrogen, variable R group

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38

functions of protein

  • transport

  • structural support

  • mobility

  • signals/hormones (regulating cellular processes)

  • defence (antibodies)

  • speed up reaction

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39

type of linkage in proteins

covalent bonds called peptide bonds, form between carboxyl group and amino group

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40

polypeptides

polymers composed of many amino acids linked by colvant bonds, protiens are composed of one or many polypeptides, vary in number and sequence of amino acids

<p>polymers composed of many amino acids linked by colvant bonds, protiens are composed of one or many polypeptides, vary in number and sequence of amino acids</p>
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41

levels of organization in proteins

  • primary - linear sequence of amino acids

  • secondary - hydrogen bonding contributes to an alpha helix or beta pleated structure

  • tertiary - 3D folding based on hydrophobic and hydrophilic interactions

  • quaternary - multiple polypeptides joining more than one polymer chain of amino acids

<ul><li><p>primary - linear sequence of amino acids</p></li><li><p>secondary - hydrogen bonding contributes to an alpha helix or beta pleated structure</p></li><li><p>tertiary - 3D folding based on hydrophobic and hydrophilic interactions</p></li><li><p>quaternary - multiple polypeptides joining more than one polymer chain of amino acids</p></li></ul>
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42

denaturation

breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein molecule that are responsible for the highly ordered structure of the protein in its natural state and is caused by extreme temp changes and chemical exposure.

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43

functional group of proteins

hydroxyl, carboxyl, amino

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44

monomers of nucleic acids

nucleotides

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45

polymers of nucleic acids

DNA and RNA

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46

4 main types of chemical reactions

neutralization, oxidation-reduction, condensation, hydrolysis

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47

acid

substance that produces hydrogen ions (pH under 7)

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48

base

substance that produces hydroxide ions (pH over 7)

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49

neutralization reaction

acid and base react together, base accepts hydrogen ions, produces salt and water

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50

normal range of human pH

7.35 fo 7.45 (below 7 or aboive 7.8 is fatal)

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51

alkalosis

blood pH over 7.5, dizziness and agitation, caused by breathing quickly or taking too many antiacids

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52

acidosis

low blood pH, kidney disease or vomiting

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53

buffers

substances the minimize changes in pH, give H2 when basic and take H2 when acidic

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54

oxidation reactions

when a molecule loses electrons and becomes oxidized

OIL

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55

reduction reactions

when a molecule accepts electrons and is reduced

RIG

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56

example of a buffer system

carbonic acid - hydrogen carbonate ion buffer system is used when the blood is too basic.

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57

example of redox reaction

cellular respiration used redox to oxidze sugar through small steps to slow the release of energy - stored in chemical bonds

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58

condensation reaction

joins molecules covalently, produces water, requires energy

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59

hydrolysis reaction

breaks apart large molecules, uses water, releases energy

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60

activation energy

energy requires to begin a chemical reaction, large activation energy means slow reaction

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61

catalysts

substances that speed up chemical reactions by lowering activation energy, proteins

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62

enzymes

specifics proteins that acts as catalysts in organisms, made of long chains of amino acids, globular shapes with indents called active sites

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63

active sites

pockets or indents on the surface of an enzyme

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64

enzyme substrate complex

when active sites and substate join together

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65

induced fit

slight cahnge to the shape of the enzyme to fit the substate

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66

catalytic cycle

cycle of a enzyme

<p>cycle of a enzyme</p>
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67

addtional moleules needed to catalyze a reaction

coenzymes and cofactors

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68

what affects enzyme activity

temperature and pH change and how much substate is present because enzymes encouter them less frequently

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69

inhibitors

molecules that interact with enzymes, they reduce the activity of the enzyme by interfering with its interaction with the substrate

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70

activators

molecules that can bind to an allosteric site to cause an increase in enzyme activity

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71

feedback inhibition

process where biochemical reaction are grouped and regulated

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72

competitive inhibitior

interfers with the active sites so substrate cannot bind to enzyme

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73

noncompetitive inhibitor

changes the shape of the enzyme so substrate cannot bind

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74

nucleus

manages or controls all the cell functions in eukaryotic cell, membrance bound

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75

cytoplasm

fills the interior of the cell except for nucleus

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76

cytosol

liquid of the cytoplasm

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77

nucleoplasm

fills the nucleus

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78

nuclear membrane

phospholipid membrane bilayer barrier around the nucleus

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79

nuleolus

site where ribosomes are made

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80

ER

connects to the nucleus and has 2 parts

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81

rough ER

membrane bound tubules and sacs associated with ribosomes, sites of protein synthesis, transports materials within the cell

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82

ribosome

synthesises proteins for export from the cell or membrane formation

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83

smooth ER

synthesises lipids and lipid containing molecules, packages proteins

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84

endomembrane system

system for transortation and product processing, proteins are synthesized and modified

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85

golgi apparatus

sorts packages and distributes lipids, manufactures macromolecules, produced lysosomes/pectin, closely packed and flattened sacs

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86

peroxisomes

manufacture cholesterol and bile acids, off the ER

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87

vesicles

transort materials ouside of cell and temportary storage of substances

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88

vacuoles

large vesicles in plant cells, store water ion sugar amino acids and macromolecules

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89

lysosomes

digests worn-out cell parts, food particles, and invading viruses or bacteria

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90

mitrochondria

break down energy-rich molecules to convert stored energy into useable energy

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91

cell wall

provides protection and supprt in plants and fungi, made of cellulose

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92

cytoskeleton

innner network of protein fibres which provide structure and anchoring to cell membrane and organelles

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93

microtubules

maintain shape, facilitate movement of organelles, cell division (spindle formation)

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94

intermediate filaments

maintain shape, anchor organelles, form internal scaffolding of nucleus

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95

microfilaments

maintain shape, muscle contractions, assits in cell division (cleavage furrow)

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96

nuclear pores

regulate transport in and out of nucleus

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97

cilia

move cells by a wave lengh movement, can sense things, sweep out debirs in respirary tract

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98

flagella

tails and move cells with a whip like motion

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99

fluidity of the cell membrane is affected by

  • temperature (more mallable w/ temp)

  • presence of double bonds (more double bonds more fluid)

  • length of fatty acid tail (longer length less fluid)

  • presence of cholesterol (more choesterol less fluid)

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100

what does the fluid mosaic model feature in a cell membrane

semi-fluid phospholipid bilayer with proteins, non-polar proteins and non-polar bilayer come in contact with each other, other proteins and molecules float in/on bilayer, made of two leaflets that slide across each other

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