Unit 1 Flashcards
1
Q
organic chemistry:
A
organic molecules formed by a carbon frame
2
Q
catenation:
A
the ability for carbon to make chains w itself
3
Q
hydro carbons
A
organic molecules that are formed when carbon is bonded to hydrogen alone
4
Q
condensation reaction:
A
atoms are removed when 2 small molecules join to make 1 big molecule
5
Q
condensation reactions are how ________ _____ _____ are made
A
synthetic natural polymers are preformed
6
Q
dehydration reaction:
A
form of condensation where the removed molecule (to connect the 2 smaller ones) is water.
7
Q
hydrolysis reaction:
A
(opposite reaction). the cutting (or lysing) of a large molecule into smaller molecules using water.
8
Q
hydrolysis is…
A
an important process in living systems as our body used this process to break down proteins, fats, carbs, nucleic acids and more
9
Q
redox reaction aka _____:
A
oxidation-reduction
10
Q
oxidation:
A
when an atom or molecule loses electrons
11
Q
reduction:
A
when an atom or molecule gains electrons
12
Q
in living systems, redox reactions…
A
involve the transfer of free energy from one molecule to another
13
Q
a simpler way to identify a redox reaction is when…
A
a hydrogen or oxygen atom is gained or lost
14
Q
reduction (in perspective of oxygen and hydrogen) is when…
A
oxygen is lost
or
hydrogen is gained
15
Q
oxidization (in perspective of Oxygen and hydrogen) is when…
A
Oxygen is gained
or
Hydrogen is lost
16
Q
carbohydrate:
A
provides body with energy
17
Q
monosaccharide:
A
(simple sugars) simplest form of a carb that contains 1 ring
18
Q
ex of monosaccharide glucose:
A
- can be shown in a linear chain or ring structure
- carries in the blood and transported to the cells to make cellular energy-
19
Q
various types of sugar include:
A
galactose, xylose, fructose + more. (they have similar structures but different arrangement of atoms
20
Q
how many carbon structures make up a DNA structure:
A
5 carbon structures make up the dna structure. such as monosaccharides, ribose, and deoxyribose
21
Q
disaccharides:
A
combination of 2 monosaccharides (through a dehydration/ hydrolysis reaction) to form a disaccharide. (2 rings)
22
Q
ex: table sugar (sucrose) is a disaccharide of:
A
glucose and fructose joined by a hydrolysis reaction
23
Q
disaccharide linkages are called:
A
glycosidic linkages
24
Q
polysaccharides:
A
(large molecules w 3 or more rings) these carbohydrates are polymers made up of many monosaccharides joined together.
25
polysaccharides are thousands...
of sugars in linear or branched structures. (includes molecules such as cellulose (wood) and starch which is found in rice and pasta).
26
starch in chloroplast is componentized as:
aylose and amylopectin
27
aylose:
straight chain
28
amylopectin:
branches & coils (insoluble in water)
29
cellulose:
polysaccharide in plants that can’t be broken down by humans
30
glycogen:
energy storage in heterotrophs like amylopectin but more branches stores in liver and muscles
31
fats/lipids:
carbon, hydrogen, oxygen
32
hydrophobic:
molecules that don’t like water
33
types of fats:
triglycerides
phospholipids
steroids
34
fats:
concentrated source of energy
35
lipids:
- in cell membrane maintain fluidity
- protection around organs and joints
- surround neeve cellsnto speed up nerve impulse
- insulates body
36
triglycerides:
fats made of glycerol + 3 molecules of fatty acid
37
fatty acids vary in:
vary in length and saturation
38
esterification reaction:
a reaction where each hydroxyl group of glycerol can connect to a fatty acid
39
fatty acids:
long hydrocarbon chains (w a carbonyl group on the end to make an acid)
40
OH groups from glycerol react w COOH groups from the fatty acid to...
form a fat through dehydration synthesis
41
steroids:
fats based on the structure of cholesterol
42
cholesterol is important in..
the structure of cell membranes (& in synthesis) of many hormones in the body such as testosterone, estrogen, aldoesteron, and more
43
high cholesterol levels in blood leads to..
leads to atherosclerosis
44
atherosclerosis:
a disease where plaque builds up inside your arteries
45
trans fat promotes:
-build up of plaque on arteries & cholesterols
| bad cholesterols build up plaque
46
phospholipids:
phosphate based structure & 2 fatty acids (important in cell membrane structure)
47
phospholipids are similar to triglycerides but
1 fatty acid is replaced by a highly polarphosphate group
48
hydrophilic:
where water is attracted
49
essential amino acids...
8 of 20 can’t be synthesized by the human body so we MUST be supplied by food sources
50
proteins:
made of amino acids linked by covalent bonds (called peptide bonds)
51
residue:
amino acids
52
the sequence of amino acids is...
specific for each protein
53
proteins primary structure:
long sequence of amino acids
54
important roles of proteins:
- enzymes
- cell surface makers
- cell membrane protein channels
55
secondary, tertiary, and quaternary structures:
when 2 or more polypeptides join together and interact in specific way
56
alpha helix (pleated sheet):
when a primary sequence of a protein can be folded on itself forming two visible secondary structures
57
alpha helix (or pleated sheet) is held by:
hydrogen bond
58
the tertiary structure:
the 3 dimensional globular structure
59
what are tertiary structures held by?
interactions w amino acids, hydrogen bonds, and disulfide linkage
60
quartenary structure
when 2 or more polypeptides join tighter and interact in specific ways
61
allosteric site:
site separate from the active site
62
proteins have a globular structure which...
is not rigid!
63
globular structures..
are flexible and can often change shape
64
when a substance binds to an allosteric site,....
the enzyme ⬆️’s or ⬇️’s the productivity of the enzyme
65
how to shut down an enzyme:
to activate it or shut it down by having another molecule bind to the allosteric site to regulate its activity
66
allosteric regulation:
changing the shape of an enzyme so the substrate can no longer fit the active site (other molecules fit into the allosteric site)
67
enzymes:
protein molecules that act as biological catalysts
68
catalyst:
provides surface to break bonds between the reactant molecules. then rearranges atoms in order to create binds to form the products
69
if no catalyst is present...
reactant molecules must collide with enough energy (& correct orientation in order to break bonds)
70
activation energy:
energy required to reach a state where reactant bonds are breaking and product bonds are forming (transition state)
71
speeding up a chemical reaction can be done in a lab and not...
in a living system where organisms are made of proteins that will denature upon heating
72
exergonic:
products that have a higher energy than reactants (system gives off energy)
73
endergonic reaction:
products have a lower energy than reactants (system requires energy)
74
in the lock and key theory phase 2 the enzyme...
slightly changes shape so when substrate enters, it precisely fits
75
there are many different enzymes to catalyze all the different reactions and they are all..
specific to each substrate
76
enzyme regulation:
enzyme activity needs to be controlled by cell.
| - prevents unwanted accumulation of substrate and products.
77
one method for controlling enzyme activity is through
the allosteric site (substance that binds to the allosteric site is often a product / substrate)
78
when a certain product is needed, the substrate can ..
activate the enzyme by binding to the allosteric site and turning the enzyme on
79
feedback inhibition:
when the cell turns off the enzyme by having the product molecule bind to the allosteric site. this gives enzyme feedback when there r high concentrations of product
80
coenzymes
organic molecules
81
cofactors
inorganic ions
82
non protein substances such as coenzymes and cofactors...
work w an enzyme to help the enzyme function
83
many vitamins from your diet work as ..
coenzymes
84
many minerals from your diet work as..
cofactors
85
inhibition:
enzymes can be inhibited in many different way
86
the two general methods of inhibiting an enzyme:
competitive and non competitive inhibition
87
competitive inhibition
another molecule other than the substrate competes for the active site of the enzyme
88
when substrate concentration increases...
more substrate molecules are available to compete for the active site and overcome competitive inhibition
89
non competitive inhibition
the inhibitor fits into another enzyme site other than the active site
90
during the process of non comp inhibition
the shape of enzyme is altered and once changed, the substrate no longer fits into the active site (the enzyme cannot catalyze the reaction)
91
what will not affect non comp inhibition
adding substrate
92
the inhibitior molecule may release the allosteric site making ...
non comp inhibition reversible as in the case of allosteric regulation
93
if the inhibitor binds permanently (or permanently alters the enzyme shape) for comp inhibition...
it is non reversible
94
cell membrane:
separates living cells from non living
| - selectively permeable membrane surrounding the cell
95
fluid mosaic model:
the cell membrane is a fluid mosaic of various macromolecules that are fluid (capable of motion) within the membrane
96
proteins:
(found in plasma membrane) have various functions acting as channels such as receptor sites, connections, identification markers
97
marker proteins: (peripheral)
rest on one side or the other of the membrane
98
transport proteins: (integral proteins)
span both sides of the membrane
99
diffusion:
movement of molecules from an area of high conversation to low concentration (molecules such as O and H2O move in and out of cell through diffusion) ex: perfume
100
diffusion does not require:
energy to be expended by the cell. (a natural process)
101
osmosis:
special type of diffusion.
| movement of water from high concentration to low though a semipermeable membrane
102
ex of osmosis:
water lines into cell where concentration is lower and expands blood cell
103
hypertonic:
has a lower water concentrations outside vs inside cell
104
hypotonic:
has more water outside than inside
105
active transport:
carries molecules against a concentration gradient and requires cellular energy
106
active transport uses..
a carrier protein
107
molecules require energy supplied by
atp
108
molecules move in opposite direction in active transport
than the natural occurring direction during diffusion
109
atp
adenosine triphosphate (molecules that carries energy into cell)
110
when the cell needs energy
atp is broken down
111
atp is broken down by
removing a phosphate group and releasing the energy to where it is needed in the cell
112
atp is the only form of energy...
cells can use. releases chemical energy
113
bulk transport:
a way to get large molecules into or out of the call that cannot pass though the membrane or protein channel
114
endocytosis:
used to transport material into the cell
115
exocytosis
used to transport molecules such as proteins and cell products from inside cell to our
116
3 types of endocytosis
1. phagocytosis
2. pinocytosis
3. receptor-mediated endocytosis
117
phagocytosis:
process where large molecules are brought into cell
118
pinocytosis:
process where small molecules are brought into the cell
119
receptor - mediated endocytosis:
requires a receptor (protein) to be activated for a vesicle to be made
120
endocytosis molecules are dissolved:
in water or liquids
121
exocytosis requires:
packaging from golgi of cellular products into a vesicle
| - then merges and fuses w plasma membrane and is released it exyracellular fluid or bloodstream
122
polypeptides:
chains of amino acids
123
proteins are made of:
1 or more polypeptides molecules
124
amino acids linked ..
covalently by peptide bonds
