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1

describe water diagram

oxygen is negative and hydrogen end is positive

*know how to draw

charged regions can attract each other creating hydrogen bonds

oxygen and hydrogen are bonded through covalent bonds

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2

cohesion

attraction of water to itself

cohesive forces are attempting to pull the water into the smallest possible sphere

surface tension is caused by this as the water is attempting to stick together through cohesive forces while an object is penetrating the surface

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3

adhesion

due to polarity caused by hydrogen bonds

attraction of water to other substances

water is

water tends to stick to other charged substances

large number of hydrogen bonds gives forces strength

explains how water “defy” gravity as it is bonding to surface

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4

capillary action

caused by combination of adhesive and cohesive forces where water can travel along a charged medium against gravity to a degree. water binds the sides and water binds to itself causing it to slowly go along the material

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5

solvent

water can act as a good solvent because the large amount of polar attraction between water molecules interrupt intermolecular forces such as ionic bonds and cause the atoms to break down

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6

things that are hydrophillic

polar molecules, charged molecules, substances that water adheres to

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7

things that are hydrophobic

nonpolar molecules, noncharged molecules, substances that dissolve in other solvents, lipids

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8

molecules that can freely travel through the blood stream

glucose (polar molecules), amino acids (acid groups are charged, but R group may or may not be so this determines degree of solubility), sodium chloride (ionic)

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9

molecules that need something else

fats (nonpolar so carried through lipoprotein complex), cholesterol (hydrophoic so carried through lipoprotein complex)

oxygen (non-polar but soluble as temperature decreases; body temperature too high so hemoglobin in red blood cells carry the oxygen)

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10

lipoprotein complex

outside layer is phospholipid molecules with hydrophillic phosphate heads facing outwards

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11

thermal properties of water

high specific heat capacity

high heat of vaporization

high heat of fusion (amount of energy lost to change liquid water to ice)

reason: many hydrogen bonds need to be broken or formed to change temperature of water

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12

water as coolant in sweat

high temperatures causes enzymes to denature

when water is on skin, takes lots of energy to heat water up so skin underneath is safe

when water is evaporated, lots of energy is removed

skin and blood vessels are cooled

water makes up most of the body, so the body is relatively resistant to heat change. If one part of the body is cool, the cool blood will travel to other parts to cool it down

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13

main difference between methane and water

methane is non-polar and water is polar

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14

why can we not say that water has memory

some dumbasses put antibodies in water and saw a reaction did serial dilution and saw the same thing

many people tried to repeat it but it didn’t work and too small population

pseudoscience - they didn’t follow scientific method

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15

4 most common elements in living organisms

carbon, hydrogen, nitrogen, and oxygen

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16

role of other elements

nitrogen - protein

sulfur - protein

potassium - transmit nerve impulses

sodium - transmit nerve impulses

iron - found in hemoglobin

calcium - teeth and bones

phosphorus - found in nucleic acid, ATP, and cell membrane structures

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17

why is carbon able to form macromolecules

has 4 valence electrons so can form 4 covalent bonds

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18

metabolism

- all enzymatic reactions in body

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19

anabolism

- synthesis of macromolecules from simpler molecules (H2O removed to form bonds) ex: lactose

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20

catabolism

  • macromolecules being broken down to release energy, ex: digestion, cell respiration

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21

KNOW TO DRAW WATER MOLECULE

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22

why is water polar

unequal sharing of electrons and unsymmetrical shape of molecule

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23

carbohydrates

monosaccharide

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24

lipids and fats

fatty acid

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25

nucleic acid

nucleotides

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26

protein

aminoi acids

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27

why is carbon so important

has four valence electrons so it can form 4 covalent bonds

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28

vitalism

theory that living organisms are alive because of a vital principle distinct from chemical forces

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29

how was vitalism falsified

urea: excretes excess amino acids

organic compounds could be created in lab

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30

carbohydrates

carbon compounds consisting of one or more simple sugars (CH2O)

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31

glucose

monosaccharide that is the basic unit of many polymers

respiration to produce ATP

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32

galactose

also a hexose sugar but less sweet

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33

ribose vs deoxyribose

pentose sugar and backbone of RNA

bottom right if OH is ribose if H is deoxyribose

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34

fructose

sweetest naturally occurring carbohydrate

energy source of fruits and honey

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35

triglyceride formation

3 fatty acid and glycerol

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36

lipids hydrolysis

glycerol and fatty acids

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37

lactose conformation

galactose and glucose

energy source in milk

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38

sucrose formation

glucose and fructose

convenient form of transferring water throughout the plant

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39

maltose

disaccharide of 2 glucose molecules

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40

glycogen

repeating glucose subunits branched

short term energy storage in liver and muscles

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41

starch

major carbohydrate reserve

contains several million amylopectin molecules with many smaller amylose molecules

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42

cellulose

repeating glucose units linear

multiple hydrogen bonds form between strands creating microfibrils

structural component of cell wall

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43

lipids

fats, oils and waxes

biological fuels, hormones, and structural components of membranes

not macromolecules

nonsoluble in water but soluble in nonpolar solvents

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44

neutral fats

most common lipid with ester links

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45

saturated fatty acid

maximum number of fatty acids

no double bonds

straight chains

solid at room temperature

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46

unsaturated fatty acid

some carbon atoms are double bonded

liquid at room temperature

kinks in straight chains

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47

cis isomers

commmon in nature

hydrogen atoms are on same side of the two carbon atoms

double bond causes bend

loosely packed

low melting points

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48

trans isomers

rare in nature (margarine from vegetable oils)

opposite side of the 2 carbon atoms

double bond does not cause bend in fatt acid chain

tightly packed

high melting points

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49

common lipids

oleic acid, a-linolenic acid, and caproic acid

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50

phospholipid

one fatty acid group of triglycerol is replaced with a phosphate group

glycerol molecule, two fatty acid chains, and a phosphate

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51

steroids

three 6 carbon atom rings and one 5 carbon atom ring

examples: sex hormones, hormones such as cortisol and aldosterone, and cholesterol

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52

triacylglycerols (triglyceride)

glycerol is an alcohol containing 3 carbon bonded to a hydroxyl group

hydrolysis will break down triglycerides into subunits

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53

lipids functions

structure: phospholipids are main component of cell membrane

hormonal signaling: steroids

insulation: fats serve as heat insulators

protection: triglycerides form tissue layer around many key internal organs and provide protection against physical injury

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54

storage of energy

triglycerides are used as long term energy source

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55

energy ratio

fat:carb:protein

2:1:1

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56

bmi

identify possible weight problems

=mass (kg) / height (m^2)

kg/m^2

monogram: draw line from weight to height using ruler to see where it intersects

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57

proteins

made up by amino acids

shaped based on sequence of amino acids

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58

acid amino acids charge

basic amino acids charge

negative

positive

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59

start codon

AUG (methiomine)

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60

R groups

give amino acids their properties

acidic vs basic

polar vs nonpolar

hydrophillic vs hydrophobic

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61

what is responsible for sequence of amino acids

genes

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62

polypeptide formation

2 amino acids bonded together

peptide bond is formed between carbon and nitrogen

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63

what determines function of protein

structure

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64

primary structure

amino acid sequence linked by peptide bonds

interaction between R groups of amino acid determines shape

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65

what is shape of protein

conformation

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66

secondary structure

shape of polypeptide chain

shape is result of hydrogen bonds

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67

2 common shapes of secondary structure

alpha helix coils

beta-pleated sheets

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68

tertiary structure`

the protein’s fold

folds with the help of chaperone proteins and interactions between R group

hydrogen bonds, hydrophobic interactions, ionic interactions, disulfide bridges

determines function

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69

quaternary structure

not all proteins have this

those that do have polypeptides that aggregate together

ex: hemoglobin

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70

why can proteins perform a variety of functions

quartenary and tertiary structures

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71

fibrous protein

long and narrow

structural

genearllly insoluble in water

less sensitive to changes in heat, pH etc.

collagen

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72

globular protein

rounded and spherical

functional

generally soluble in water

more sensible to heat, pH

catalase

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73

rubisco

fixes carbon dioxide from the atmosphere

enzyme

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74

insulin

hormone - signals cells to take and absorb glucose

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75

immunoglobulins

antibodies

respond to huge range of pathogens

provokes an immune response

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76

rhodospin

pigment that absorbs light

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77

collagen

rope-like proteins

quarter of all protein in the human body

give strength and structure to various parts of the body

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78

spider silk

extensible and resistant to breaking

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79

genome

genes of organism that gives an idea of what the proteome could be

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80

environment factors

influences proteins needed based on surroundings

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81

proteome

proteins produced by organism that reveals what is happening at a certain point in time

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82

denaturation

when proteins are outside a specific range of temperature and pH

interruption of bonds which means interruption of structure which means interruption of function

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83

temperature

as heat energy increases, molecules within the bonds vibrate violently breaking bonds

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84

pH

pH measures amount of free-flowing H+ ions there are

when one of the H+ ions attaches to the amino acid, charge is changed thus breaking bonds and denaturing

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85

enzyme

globular proteins that speed up reations by lowering the activation energy threshold

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86

induced fit model vs lock and key model

enzyme changes shape slightly to put stress on bonds vs fits perfectly

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87

collision theory

in order for enzymatic action to coccur, enzymes must come into contact with substrate

when heated, easier to combine because enzymes move faster meaning more chance to collide

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88

common uses of enzymes

lactose, restriction enzymes, pcr reactions, and detergent

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89

immobilized enzymes

attached to material so their movement is restricted

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90

advantages

Concentration of substrate can be increased as enzyme will not dissolve

Recycled enzymes can be reused, enzymes can be separated easier

O

Separation of products is straightforward and easier

Stability is increased with more resistance to temperature and pH changes

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91

lactose milk produced

lactase beads, milk is poured through repeatedly, lactase breaks lactose into glucose and galactose

result: sweetened

reduce crystalisation of ice cream

shorten production time for yogurt and cheese

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92

how do enzymes lower activation energy of reaction

due to binding, bonds in substrate are stressed

progresses reaction

lowers overall energy level of transition state

activation state is reduced

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93

normal enzyme graph

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94

example of competitive inhibition

relenza

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95

example of noncompetitive inhibition

cyanide

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96

anabolic

small molecules are used to create larger ones

condensation

synthesis

endothermic

two substrates enter an enzyme which creates chemical bonds to connect them

need energy

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97

catabolic

break down larger molecules into smaller subunits

exothermic

one substrate into 2

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98

metabolic pathways (essay)

body requires several reactions to produce required product

metabolic pathways consist of chains and cycles of enzyme-catalyzed reactions

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99

end product inhibition

there is enough end product and the metabolic pathways shut down

end product will bind to first enzyme allosterically to inhibit the enzyme until it is needed again

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100

threonine into isoleucine

when there is too much isoleucine end product, isoleucine travels back to the first enzyme and inhibits it until there is low concentrations of isoleucine again

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