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100 Terms

1
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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
2
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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
3
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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
4
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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
5
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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
6
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things that are hydrophillic
polar molecules, charged molecules, substances that water adheres to
7
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things that are hydrophobic
nonpolar molecules, noncharged molecules, substances that dissolve in other solvents, lipids
8
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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)
9
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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)
10
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lipoprotein complex
outside layer is phospholipid molecules with hydrophillic phosphate heads facing outwards
11
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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
12
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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
13
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main difference between methane and water
methane is non-polar and water is polar

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14
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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
15
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4 most common elements in living organisms
carbon, hydrogen, nitrogen, and oxygen
16
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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
17
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why is carbon able to form macromolecules
has 4 valence electrons so can form 4 covalent bonds
18
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metabolism

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\- all enzymatic reactions in body
19
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anabolism
\- synthesis of macromolecules from simpler molecules (H2O removed to form bonds) ex: lactose

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20
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catabolism
- macromolecules being broken down to release energy, ex: digestion, cell respiration
21
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KNOW TO DRAW WATER MOLECULE
22
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why is water polar
unequal sharing of electrons and unsymmetrical shape of molecule
23
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carbohydrates
monosaccharide
24
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lipids and fats
fatty acid
25
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nucleic acid
nucleotides
26
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protein
aminoi acids
27
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why is carbon so important
has four valence electrons so it can form 4 covalent bonds
28
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vitalism
theory that living organisms are alive because of a vital principle distinct from chemical forces
29
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how was vitalism falsified
urea: excretes excess amino acids

organic compounds could be created in lab
30
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carbohydrates
carbon compounds consisting of one or more simple sugars (CH2O)
31
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glucose
monosaccharide that is the basic unit of many polymers

respiration to produce ATP
32
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galactose
also a hexose sugar but less sweet
33
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ribose vs deoxyribose
pentose sugar and backbone of RNA

bottom right if OH is ribose if H is deoxyribose
34
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fructose
sweetest naturally occurring carbohydrate

energy source of fruits and honey
35
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triglyceride formation
3 fatty acid and glycerol
36
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lipids hydrolysis
glycerol and fatty acids
37
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lactose conformation
galactose and glucose

energy source in milk
38
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sucrose formation
glucose and fructose

convenient form of transferring water throughout the plant
39
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maltose
disaccharide of 2 glucose molecules
40
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glycogen
repeating glucose subunits branched

short term energy storage in liver and muscles
41
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starch
major carbohydrate reserve

contains several million amylopectin molecules with many smaller amylose molecules
42
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cellulose
repeating glucose units linear

multiple hydrogen bonds form between strands creating microfibrils

structural component of cell wall
43
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lipids
fats, oils and waxes

biological fuels, hormones, and structural components of membranes

not macromolecules

nonsoluble in water but soluble in nonpolar solvents
44
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neutral fats
most common lipid with ester links
45
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saturated fatty acid
maximum number of fatty acids

no double bonds

straight chains

solid at room temperature
46
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unsaturated fatty acid
some carbon atoms are double bonded

liquid at room temperature

kinks in straight chains
47
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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
48
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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
49
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common lipids
oleic acid, a-linolenic acid, and caproic acid
50
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phospholipid
one fatty acid group of triglycerol is replaced with a phosphate group

glycerol molecule, two fatty acid chains, and a phosphate
51
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steroids
three 6 carbon atom rings and one 5 carbon atom ring

examples: sex hormones, hormones such as cortisol and aldosterone, and cholesterol
52
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triacylglycerols (triglyceride)
glycerol is an alcohol containing 3 carbon bonded to a hydroxyl group

hydrolysis will break down triglycerides into subunits
53
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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
54
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storage of energy
triglycerides are used as long term energy source
55
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energy ratio
fat:carb:protein

2:1:1
56
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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
57
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proteins
made up by amino acids

shaped based on sequence of amino acids
58
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acid amino acids charge

basic amino acids charge
negative

positive
59
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start codon
AUG (methiomine)
60
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R groups
give amino acids their properties

acidic vs basic

polar vs nonpolar

hydrophillic vs hydrophobic
61
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what is responsible for sequence of amino acids
genes
62
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polypeptide formation
2 amino acids bonded together

peptide bond is formed between carbon and nitrogen
63
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what determines function of protein
structure
64
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primary structure
amino acid sequence linked by peptide bonds

interaction between R groups of amino acid determines shape
65
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what is shape of protein
conformation
66
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secondary structure
shape of polypeptide chain

shape is result of hydrogen bonds
67
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2 common shapes of secondary structure
alpha helix coils

beta-pleated sheets
68
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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
69
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quaternary structure
not all proteins have this

those that do have polypeptides that aggregate together

ex: hemoglobin
70
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why can proteins perform a variety of functions
quartenary and tertiary structures
71
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fibrous protein
long and narrow

structural

genearllly insoluble in water

less sensitive to changes in heat, pH etc.

collagen
72
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globular protein
rounded and spherical

functional

generally soluble in water

more sensible to heat, pH

catalase
73
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rubisco
fixes carbon dioxide from the atmosphere

enzyme
74
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insulin
hormone - signals cells to take and absorb glucose
75
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immunoglobulins
antibodies

respond to huge range of pathogens

provokes an immune response
76
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rhodospin
pigment that absorbs light

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77
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collagen
rope-like proteins

quarter of all protein in the human body

give strength and structure to various parts of the body
78
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spider silk
extensible and resistant to breaking
79
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genome
genes of organism that gives an idea of what the proteome could be
80
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environment factors
influences proteins needed based on surroundings
81
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proteome
proteins produced by organism that reveals what is happening at a certain point in time
82
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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
83
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temperature
as heat energy increases, molecules within the bonds vibrate violently breaking bonds
84
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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
85
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enzyme
globular proteins that speed up reations by lowering the activation energy threshold
86
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induced fit model vs lock and key model
enzyme changes shape slightly to put stress on bonds vs fits perfectly
87
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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
88
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common uses of enzymes
lactose, restriction enzymes, pcr reactions, and detergent
89
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immobilized enzymes
attached to material so their movement is restricted
90
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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
91
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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
92
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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
93
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normal enzyme graph
94
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example of competitive inhibition
relenza
95
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example of noncompetitive inhibition
cyanide
96
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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
97
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catabolic
break down larger molecules into smaller subunits

exothermic

one substrate into 2
98
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metabolic pathways (essay)
body requires several reactions to produce required product

metabolic pathways consist of chains and cycles of enzyme-catalyzed reactions
99
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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
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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