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Biology II > Test 1 > Flashcards

Test 1 Flashcards

1
Q

olWhat are the most common elements in the human body

A

C,O,N,H, Ca

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2
Q

T or F: Covalent bonds are all polar, therefore they are all electronegative

A

F. C-C bonds are covalent and not polar at all.

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3
Q

Are polar molecules hydrophobic or hydrophilic?

A

Hydrophilic

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4
Q

Define hydrogen bonding

A

Bond caused by a molecule w/ a partial -ve charge and an H atom covalently bonded to an electro-ve element. They are weak but are very strong when grouped in large numbers.

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5
Q

Define Vaan Der Waals bonding

A

Interactions between molecules that don’t involve hydrogen

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6
Q

Why does water, Si, and acetic acid expand when going from a liquid to a solid

A

The crystal lattice formed from the arrangement of the atoms/molecules result in the expansions of volume taken up by one particle. The structure end sup being less dense.

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7
Q

define surface tension

A

How hard it is to break/stretch the surface (due to cohesion)

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8
Q

define adhesion

A

how much one substance is attracted to another

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9
Q

what is the photosynthesis formula

A

6H2O+6CO2 = C6H12O6+6O2

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10
Q

which rx causes the synthesis of a molecule

A

dehydration

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11
Q

which rx causes the breaking up of a molecule

A

hydrolysis

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12
Q

what happens when a non-ionic polar bond is dissolved

A

there is no dissociation involved.

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13
Q

What is the difference between heat and temperature

A

heat: total amount of energy regarding the movement of atoms and molecules in a body of matter
temperature; average speed of the molecules

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14
Q

what is special about water and heat

A

water absorbs lots of the energy that surrounds it. Since it has such a high specific heat value, it is more resistant to temperature change.

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15
Q

how do bodies remain in the same temperature change required to undergo chemical rx

A

evaporative cooling aka sweating

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16
Q

what is so good about carbon

A

-its ability to bond with four other atoms/molecules allows for a wide variety of substances that can be made
- it can form polar and non-polar bonds
-3 isotopes

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17
Q

define organic compound

A

C backbone molecule that comes from a biological source.

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18
Q

the properties of an organic compound depends on…

A
  1. carbon skeleton arrangement
  2. substituents
  3. degree of branching
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19
Q

Name all the functional groups that can bond to a carbon skeleton (7)

A

Hydroxyl group (OH), Carbonyl group, Carboxyl group, amino group, sulfhydryl group, phosphate group, methyl group

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20
Q

list the qualities of the hydroxyl group

A
  1. provides polarity (level of polarity depends on the # OH grps on the molecule relative to its size)
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21
Q

list the qualities of the carbonyl (aldehydes and ketones) group

A
  1. Provides a degree of polarity due to a charged oxygen atom (double bonded to a C)
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22
Q

whats is the difference between and aldehyde and a ketone

A

aldehyde: Carbonyl C is bonded to at least one hydrogen
ketone: Carbonyl C is always bonded to two other C

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23
Q

why is glucose not an alcohol?

A

Because the carbonyl group has higher priority than its hydroxyl group

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24
Q

what are the names for monosaccharides with carbonyl groups?

A

aldoses and ketoses

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25
Q

list the qualities of the carboxyl group

A
  • Incorporated a CdblO covalently bonded to an OH through a C
  • Provides polarity, but also provides stability since it can donate H+ in a solution
    -weakly acidic
    -important amino acids (all amino acids have carboxyl groups)
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26
Q

list the qualities of the amino group

A
  • provides polairty due to NH bond
  • can accept an H+
  • weakly basic
  • works as a buffer do to its ability to donate or accept H+
  • R group determines the properties of an amino acid
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27
Q

list the qualities of the sulfhydryl group

A
  • SH
  • forms a bond between another SH grp to form a disulphide bridge that stabilizes the internal structures of proteins
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28
Q

list the qualities of the phosphate group

A
  • provides polarity to the parent molecule
  • nucleotides have an N base, a 5C sugar, and a phosphate group. The phosphate group contributes to the pH the most.
  • ATP has 3 phosphate groups and contains high levels of energy due to -ve charge and repulsion (which causes instability)
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29
Q

list the qualities of the methyl group

A
  • acts like “identity tags” or signals which is read by enzymes
    -not very polar
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30
Q

define isomers

A

same molecule formula, but different structures and properties

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31
Q

what are the two categories of isomers

A

structural (constitutional) and geometric/stereoisomers (enantiomers and diastereomers)

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32
Q

define macromolecules

A

large molecules composed of thousands of covalently bonded atoms
- small organic molecules are joined together
- monomers from larger molecules by condensation rx (dehydration rx)

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33
Q

what are the monomer and polymer names for
carbohydrates
lipids
protein
nucleic acid

A

monomer: monosaccharides, amino acid, nucleotide
polymer: polysaccharides, polypeptide/peptide, DNA/RNA

LIPIDS DO NOT POYMERIZE LIKE CARBS PROTEINS AND NUCLEIC ACID

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34
Q

define polymer

A

polymer: agglomeration of monomers
polymerize via dehydration

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35
Q

what are the function of carbs

A

-short-term (sugars) and intermediate-term energy storage
-structural components in cells are made of carbs (e.g. chitin)
- contains CHO in a 1:2:1 ratio
- carbs are aldehydes and ketones with multiple OH groups

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36
Q

what are the most common sugars (# of carbons)

A

trioses, pentoses, hexoses

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37
Q

what are the most common sugars? (all with the fomula C6H2O6) which is thr most common of the 3 ?

A

glucose, fructose, glactose

GLUCOSE

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38
Q

what happens to glucose when placed in water?

A

glucose turn into a cyclic compound (C1 aldehyde bond with the C5 OH group)

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39
Q

what is the difference between an alpha glucose and a beta glucose ? Which one is biologically active?

A

alpha glucose (BIOLOGICALLY ACTIVE) has both Oh groups pointing downward while alpha glucose has one OH group pointing downwards and the other pointing up. It is the OH group on the C1 that changes orientation.

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40
Q

give a quick explanation of glucose and glucagon in the body

A

hormones in the pancreas (e.g insulin and glucagon) increases or decreases the conc. of glucose in the blood.

Insulin: stores sugars in muscles and prevents the breaking down of glycogen. It also stimulates adipose cells to store glucose as fat

Glucagon: stimulates conversion of glycogen to glucose in the liver, breaks down proteins and fats

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41
Q

what is the difference between type 1 and type 2 diabetes

A

1: defeciency of insulin
2: decreased response to insulin in target isssues

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42
Q

T or F glucose is found commonly in its monosaccharide form in food

A

F. usually found in its disaccharide or starch form, fructose is most commonly found in food, though.

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43
Q

quickly explain lactose intolerance

A

lactose intolerance is caused by the absence or sudden decrease in the presence of lactase (enzyme that can break down lactose). If the enzyme is not there to break down lactose, bacteria in the large intestine does it instead. This releases gas and causes the discomfort felt after eating something with dairy. additionally, lactose will take in water from surrounding tissue (causing the runs lol)

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44
Q

what part of the body absorbs card as monosaccharides. what happens to undigested disaccharides?

A

the small intestine. undigested disaccharides go to the large intestine

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45
Q

define ogliosacchardies

A

relatively small sugar polymers that consist of 2-6 monosacchardie units. found in beans and legumes and are digested by bacteria

-msot often attached to glycoproteins (part of cell-to-cell adherecne, identification, and protection) and glycolipids

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46
Q

define polysaccharides

A

consists of thousands of monosaccharides linked together via dehydration

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47
Q

what are the two types of polysaccharides

A
  1. Easily broken down, used for energy storage (starch and glycogen)
  2. structural polysaccharides (e.g. chitin)
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48
Q

T or F beta linkages allow for the chained molecules to be digested by eukaryotes

A

F. only alpha linkages allow this.

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49
Q

which two common polysaccharides have alpha linkages. which one has beta linkages

A

glycogen + starch

cellulose. cellulose can be digested by archea groups, explaining the existence of specialozed bacteria in the stomachs of cows, for example

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50
Q

how do you differentiate from alpha and beta linkages ?

A

alpha: pointing downwards
beta: pointing upwards

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51
Q

give some quick traits of glycogen

A
  • primary storage polysaccharide of animals
  • broke down to glucose-6-phosphate
    -good for short-term metabolism
  • stored and broken down in muscle cells
  • stored and broken down in liver for blood
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52
Q

give some traits of starch

A

-main sotrage for plants
- found in roots and seeds
-can be hydrolyzesd into the disaccharide maltose by amylase

53
Q

give some traits of cellulose

A
  • beta-glucose molecules (beta 1,4 linkages)
  • beta-linkages cause fro strong hydrogen bonds, which promote the agglomeration of the molecules in fibers
    -dietary fiber to humans
54
Q

what is it about chitin that makes it slightly different to other carbs?

A

it has an amino group

55
Q

peptidoglycans : quick summary

A
  • polysaccharide in cell wall
  • when gram +ve it will be killed by penecilin (pink)
56
Q

why don’t lipids fir the polymer model

A

they group together since they hydrophobic

57
Q

what are the three types of lipids

A

neutral fats
steroids
phosphlolipids

58
Q

list the common carbohydrates

A

glucose
fructose
galactose
deoxyribose
ribose
DISACCHARIDES
sucrose (glu+fru)
lactose (glu+gal)
maltose (glu+glu)
POLYSACCHARIDES
starch
glycogen
cellulose
chitin
peptidglycan

59
Q

list the common lipids

A

TRIGLYCERIDES water insoluble
lard, suet, olive oil, peanut oil butter
FATTY ACIDS water insoluble
omega-3 and omega-6 oils
STEROIDS (membran component, hormones)
estrogen, vitamin D, cholesterol, testosterone
PHOSPHOLIPIDS (amphpathic, membrane component)
lecithin

60
Q

what are lipids primarily composed of?

A

hydrocrabons, this makes them soluble in non-polar solvents

61
Q

define triglycerides

A

composed of fatty acids (lipid molecule composed of often logn hydrogen tail (usually 16c or 18c) with a carboxyl group ((-COOH) at one end) and glycerol (3-C alcohol containing 3 OH groups)

62
Q

what are the 3 types of fatty acids

A
  1. saturated fatty acids : contains the maximum # of H
  2. monosaturated fatty acids: constains one double bond (e.g. oils and liquids)
  3. polyunsaturated fatty acids: contains more than one double bond (e.g. oils)
63
Q

what do ester linkages do

A

joind together 3 fatty acids and 1 glycerol molecule

64
Q

explain the implications of having cis and trans unsaturated fatty acids

A

cis fatty acids: Both H atoms are located on the same side of the double bond, causing a bend in the structure
trans fatty acids: H is on opposing sides, causing a rigider, straighter but it still has a bend. This accumulates in our bodies.

65
Q

define liporteins

A

spherical moelcules with hydrophobic interirors and hydrophilic exteriori composed of water-soluble prteins and phosphlipids

66
Q

how are fats digested

A
  1. emulsified in the digestive tract by bile salts
  2. emulsofoed fats are the hydolyzed by into fatty acids + monoglycerides so it can be absorbed by mucosal cells in the small intestine
  3. fatty acids are them packaged into lipoproteins called chylomicrons
  4. chylomicrons deliver fats to the cells in the body
  5. fats and cholesterol that is not taken in is brought to the circulatory system by lipoprteins
67
Q

what are VLDLs

A

very low density lipoproteins carry triglycerides produced by the liver to the body’s cells

68
Q

define steroids

A

C skeleton of 4 interconnected hydrocarbon rings with varous functional groups attatched. 3 of the rings contain 6C and the 4th contains 5C

69
Q

define cholesterol

A

common component of animal cell, transported by VLDLs and HDLs, precursor to how steroids are synthesized , important fluid buffer in cell membranes

70
Q

what does bad cholesterol refer to?

A

the quantity of HDLs and LDLs .

Trans fats impede uptake of LDL uptake by cells, causing them to keep circulating in your blood
more ldls=more adhesion to blood vesse; walls= plaque= blocked arteries

71
Q

what refers to good cholesterol

A

quantity of HDLs in the blood as they take up excess cholesterol from blood/ body inot cells and take it to the liver

72
Q

whats can increase HDLs

A

omega-3 and omega-6 (esstential fatty acids our body does not produce) intake along with exercising

73
Q

what is the differecne between omega-3 and omega-6 fats

A

where the last double bond is

74
Q

what are the two types of phopholipids

A
  1. phosphoglycerides
    -contain glycerol, fatty acids, posphate, and an alcohol
  2. sphingolipids
    - contains sphingosine (long chain amino alcohol) instead of glycerol
75
Q

how many naturally occuring amino acid monomers do we have

A

20

76
Q

what determines protein fucntion

A

protein shape and amino acid sequence

77
Q

what si the common amino acid structure

A

alpha C, carboxyl group, amino group, and R subsituent

78
Q

what are the most common amino acids forms

A

alpha (always bonded to carboxyl group), beta (carboxyl group is not bonded to central C), gamma

79
Q

what are gamma amino acids used for

A

neurotransmitters

80
Q

what are the two enantiomers of amino acids

A

D and L

81
Q

what enatiomer is used for building proteins? D or L?

A

L amino group is on the LEFT

82
Q

at pH 7.4… amino acids are present in their dipotic ionic state called…

A

zwitterions

83
Q

what are some indicators ot determine whether an amino acid is hydrophobic or hydrophilic,

A

hydrophobic: nonpolar. no double bonds, no electronegative atoms
hydrophilic: polar, double bonds (excluding rings), OH groups (anything with a + is acidic, anything with a -ve is basic)

84
Q

what are the 8 essential amino acids for adult humans

A

tryptophan
methionine
valine
theronine
phenylalanine
isoleucine
lysine

85
Q

amino acids are linked via ….

A

polypeptide bonds

86
Q

why do all polypeptides have a N-terminus and a C-terminus

A

confers polarity to the polypetide

87
Q

what are the four protein structures

A

primary structure
secondary structure
tertiary structure
quatenary strcture

88
Q

recall primary structures

A
  • specific and unique sequence of amino acids that compose a polypeptode
    -determine s by nuclotode sequence a gene codes for
89
Q

recall secondary structures

A

-H bonds form between amino groups and carboxyl groups and form alpha helixes or beta pleated sheets
-alpha helixes can break causing the helix to strecth under tension. fibers can recoil and reform
-beta pleated sheets are not elastic due to covalent bonding

90
Q

recall tertiary structures

A
  • 3D shape of the folded proteins resulting from the interaction between R-groups of different amino acids composing the plypeptide backbone.
  • composed of four interactions : hydrogen bonding, hydrophobic interactions, disulfide bridges, and ionic bonds.
91
Q

what are the two teritary structures

A

globular (alpha helixes and beat pleated sheets) and fibrous (only alpha helixes)

92
Q

recall quatenary structures

A

-formed by interations among plopeptide chains that comprise the protein
-NOT ALL PROTEINS WILL HAVE QUATENARY STRUCTURES

93
Q

define chaperonins

A

transformation occurs in steps often within protein which seperate new polypeptides from the potentially disruptive chemical conditions within the cytoplasm

94
Q

define monomeric

A

proteins made of a single poltpeptide

95
Q

define ogliometric

A

consists of two or more polypeptides

96
Q

define simple protein

A

only made of amino acids

97
Q

define conjugated protein

A

amino acids and another chemical group aka prosthetic group

98
Q

define protein denaturation

A

disruption and possible destruction of both 2,3,and 4 structures

99
Q

factors that denaturate proteins

A
  1. heat
    causes molcules to vibrate rapidly and causes the shape to unravel
  2. alcohol: causes h bonds between alcohol molecules and protein side chains
  3. protein misfolding: prion diseases, toxic plaques
  4. acidity/alkalinity
100
Q

what are the main fucntions of proteins

A
  1. enzymatic proteins
  2. storage proteins
  3. chemical messengers
  4. contractile and motor proteins
  5. defensive proteins
  6. transport protein
  7. receptor proteins
  8. structural proteins
101
Q

define chemical energy

A

form of potential enrgy stored in molecules due to atom arrangement. CE is released when a chemic rx rearranges the atoms of molecules

102
Q

what are the 2 laws of thermodynamics

A
  1. energy can be transferred and transformed, never created nor destroyed
    - energy cant be transformed with 100% effeciency due to loss of heat as well as the creation of biomass
  2. every transformation transfer increased the overall entropy in the universe
    - loss of heat contributes to overall entropy
    - lving organisms take organized froms of matter and disorganizes them
103
Q

defien free energy

A

quantification of the potential energy of a rx

104
Q

T or F
the less G the greater potential to do work.

The less order, the less G in a system

A

F
T

105
Q

what defines a spontenous rx

A

a -ve deltaG

106
Q

define endergonic and exergonic rx

A

endergonic: gain of G (rectants contain less energy than products)
exergonic: loss of G (reactants contain more energy than products)

107
Q

define metabolism

A

totality of an organism’s chemical rx

108
Q

what does metabolism allows cells to do?

A

allows cells to convert energy from one form to another

109
Q

what are the two types of metabolic pathways

A

1.catabolic: release energy by breaking down complex molecules into simpler compounds (mostly exergonic), spontaneous
2. anabolic: consumes energy to build complex molecules from simple ones (endergonic)

110
Q

define energy coupling

A

energy released by catabolic rx being used to fuel anabolic rx

111
Q

what is atp (name) what does it do ?

A

adenine triosphate

  • mediates energy transfers between catabolic and anabolic rx
  • energy is released by ATP drives endergonic rx
  • shuttled around cell to rpvide energy for endergonic rx
  • directly used in cellular work
    -provides cellular transport across membranes via transport proteins
  • generates work with motor proteins
112
Q

what is ATP made of?

A
  • adenine (N base)
  • Pentose sugar - ribose
  • 3 PHOSPHATE GROUPS, PROVIDE SLOTS OF ENERGY
113
Q

how does ATP transfer energy?

A

the transfer of a P group to another molecule (phospholyation)

114
Q

what is the rx of an ATP breakdown?

A

ATP= ADP+Pi+cellular work
- this rx is reversible
ADP+ Pi+ enzyme +energy = ATPPP

115
Q

where is the energy for the breaking down of atp is sourced from

A

glucose molecules.

116
Q

what else provides energy to a cell

A

the transfer of e- (redox rx)

117
Q

why are enzymes soooo important?

A

spotenous rx are not always fast. The enzyme acts as a catalyst that will lower the activation energy of a rx, speeding up the rx and allowing it to take place at an organism’s basal body temperature

118
Q

why cant we just have an elevated basal body temperature that will allow the chemical rx in our body to occur without enzymes

A

protein denaturation

119
Q

what allows enzymes to act as acatalyst

A

the enzymes msut be in direct contact with the substrate

120
Q

define induced fit

A

the active site where the substrate enter and is envelopped by the enzyme. interaction between the usbstrate and the amino acids of the protein cause the active site to fit more snuggly around the substrate

121
Q

what are the acceptor molecules inr edox rx

A
  1. nicotinamide adenine dinucleotide (NAD+)
  2. Nictinamide adenine dinucleotide phosphate (NADP+)
  3. Flavin adenine dinucleotide (FAD)
  4. Cytochromes
122
Q

how do enzymes lower the EA

A
  • template for substrate moelcules to come together
  • stress the substrate molecule bonds
    -participate in chemical rx
  • provides a favourable microenvironment for the rx
123
Q

what are the steps of an enzyme acting as a catalyst?

A
  1. enzyme binds to substrate
  2. enzyme-substrate complex forms induced-fit, stresses bonds, lowers ea
  3. rx occurs
  4. products leave
  5. enzymes return to their natural shape
124
Q

what affects rx rates

A
  1. temperature
  2. pH
  3. the chemical environment
  4. substrate conc.
125
Q

the greater the substrate conc. …

A

the more liekly it is to come in contact witht he enzyme’s active site

126
Q

how si enzyme activity regulated ?

A
  1. switching genes on/off
  2. cofactors (inhibitors competitive and non-competitive)
127
Q

what is the differecne between a competitive and non competitive inhibitor?

A

competitve: bind to the same site as the substrate on the enzyme, reduce the productivity by blocking substrates

non-competitive: bind to a different site on the enzyme than the substrate , causes the enzyme molecule to change substrate conformation which makes it less effective

128
Q

define allosteric site

A

site other than the active site

Biology II (6 decks)

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