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lecture 2 Flashcards

1
Q

what are 99% of cells made up of

A

hydrogen
carbon
oxygen
nitrogen

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2
Q

what are the 2 covalent bonds

A

polar
non polar

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3
Q

what are covalent bonds

A

sharing of electrons

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4
Q

what are the 4 noncovalent bonds

A

ionic bonds
hydrogen bonds
hydrophobic interactions
van Der wall forces

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5
Q

what determines how atoms interact

A

valence electrons

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6
Q

what are covalent bonds characterized by

A

bond angles
bond length

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7
Q

is more energy required to break double bonds

A

yes

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8
Q

is there free rotation around double bonds

A

no

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9
Q

what is electronegativity

A

the tendency to attract electrons

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10
Q

what are electrons in a polar covalent bond

A

shared unequally

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11
Q

what are the electrons in non polar covalent bonds

A

shared equally

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12
Q

what increases reactivity of molecules

A

strongly polarized bonds

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13
Q

what do most biologically important polarized molecules have

A

one or more electronegative atoms

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14
Q

what biological molecules are amphipathic

A

proteins
phospholipids

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15
Q

what is bond strength

A

the amount of energy required to break a bond

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16
Q

is bond strength or thermal energy stronger

A

bond strength

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17
Q

how are ionic bonds formed

A

through the loss or gain of electrons

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18
Q

what attractions are very important in biological systems

A

electrostatic interactions

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19
Q

are covalent bonds within the same atom

A

No

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20
Q

what is a hydrogen bond

A

a hydrogen covalently bound to an electronegative atom and to an electronegative atom from another molecule

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21
Q

are polar molecules hydrophilic or hydrophobic

A

hydrophilic

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22
Q

are non polar molecules hydrophilic or hydrophobic

A

hydrophobic

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23
Q

what do van Der walls forces hold together

A

neutral molecules

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24
Q

what is a unique property of water

A

all 3 atoms can hydrogen bond

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25
what is an amphoteric molecule
acts as either an acid or a base
26
what do buffers do
resist changes in pH
27
what do bases do
accept protons
28
what do acids do
release protons
29
what are compounds produced by living organisms called
biochemicals
30
what do macromolecules have
large organic molecules within cell
31
how are macromolecules formed
by linking smaller building blocks (monomers) together
32
what is polymerization
process of linking monomers
33
what is hydrolysis
the process of undoing monomers
34
what are the 4 types of biological molecules
carbohydrates lipids nucleic acids proteins
35
what do carbohydrates do
store energy building material biological construction
36
whats a polysaccaride
type of carbohydrate that consists of long chains of monosaccharide (simple sugar) units linked together
37
what are carbohydrates also called
glycans
38
whats the general formula for sugars
(CH2O)n
39
what is a glycosidic bond
covalent bond that links sugar
40
what is an energy storage for animals
glycogen
41
what is glycogen made of
branched glucose polymers
42
what is starch made of
both branched and unbranched glucose polymers
43
what is cellulose
plant cell wall
44
what is chitin
insect outer skeleton
45
where are glycosaminoglycans found
extracellular space and connective tissue
46
what are cellulose, chitin, and glycosaminoglycans
structural polysaccarides linked by glucose monomers
47
are lipids polar or non polar
non polar
48
are lipids soluble
no
49
what is the composition of fat
glycerol backbone + 3 fatty acids
50
what kind of linkages are in fat
ester
51
whats the main component of body fat in humans
fats
52
what are fats in regard to water
amphipathic
53
what are saturated fatty acids
they do not have carbon carbon double bonds can be packed tightly solid at room temp
54
what are unsaturated fatty acids
they have carbon carbon double bonds and cannot be packed tightly liquid at room temp
55
whats the composition of steroids
class of lipids that have a 4 - ringed hydrocarbon skeleton
56
whats an example of a steroid
cholesterol
57
where is cholesterol found
animal cell membranes
58
what does a phospholipid resemble
fats
59
how many chains does a phospholipid have
two fatty acid chains
60
what gives the membrane its properties
phospholipids
61
what do proteins do
carry out cellular activities
62
what are proteins made of
polymers of amino acids (polypeptide chains)
63
what are amino acids in proteins linked by
peptide bonds
64
what gives proteins their diverse structures and activities
the side chain variability
65
what are the positive amino acids
arginine lysine and histidine
66
what are the negative amino acids
aspartic acid + glutamic acid
67
what do disulphide bridges do
help stabilize the shapes of proteins
68
what are the four levels or protein organization
primary, secondary, tertiary, quaternary
69
what does a primary structure look like
sequence of amino acids
70
what do the amino acids in a primary structure contain
3D structure and function of protein
71
what structure ultimately determines the levels of structure
primary
72
whats the driving force for protein folding
hydrophobic interactions
73
what is sickle cell anemia
blood cells are in a crescent or sickle shape
74
what causes sickle cell anemia
single amino acid change glutamate to valine
75
what are the 2 secondary structures
alpha helix beta sheets
76
what is a secondary structure
the shape that is formed due to hydrophobic interactions - best shape to optimize hydrogen bonding
77
what is secondary structure preferred conformation
wherever it is optimizing hydrogen bonding
78
what is a tertiary structure
3D conformation of the entire polypeptide
79
is the 3D structure entirely fixed in a tertiary structure ?
no not yet
80
what is primary sequence similarity for
to identify proteins with similar function/structure
81
what is a tertiary structure for
to predict protein interactions and enzymatic activity
82
can proteins with different primary structures have similar tertiary structures?
Yes
83
what is the structural unit of a tertiary structure
domains
84
do domains fold independently
yes
85
how many domains do eukaryotic proteins have
more of equal to 2 domains
86
how many levels of structure are there for proteins with a single polypeptide chain
3
87
what is a protein with multiple subunits or chains ?
a quaternary structured protein
88
what are molecular chaperones
helper proteins
89
can all proteins assume their final tertiary structure by self assembly
no they need molecular chaperones
90
what do molecular chaperones bind to
hydrophobic amino acids
91
what do nucleic acids do
store and transmit genetic information
92
what are the 3 parts of a nucletide
sugar (5 carbon) nitrogenous base phosphate group
93
what are nucleic acids
RNA/DNA
94
what makes up a nucleic acid
nucleotides
95
whats the sugar in RNA
ribose
96
whats the sugar is DNA
deoxyribose
97
whats on the C2 atom of RNA
OH group
98
whats on the C2 of DNA
H
99
whats the composition of purines
2 rings
100
what are the purines
guanine adenine
101
what are the pyrimidines
cytosine thymine uracil
102
what are purines and pyrimidines
nitrogenous bases
103
whats the backbone of DNA
sugar phosphate backbone
104
how might RNA have catalytic activity?
the ribozymes are capable of catalytic activity
105
what specifies the precise shape of a macromolecule
non covalent bonds
106
what binds subunits (Amino acids) and macromolecules
covalent bonds
107
what binds macromolecules and macromolecule assembly
non covalent bonds
108
what are the 4 types of macromolecules
proteins nucleic acids carbohydrates lipids

BMSC 220 (22 decks)

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