Midterm Flashcards
Unit 1 and 2 (168 cards)
1
Q
general to specific (big to small)
A
deductive
2
Q
specific to general (small to big)
A
inductive
3
Q
an emerging idea that has yet to be widely tested
A
hypothesis
4
Q
concept supported by a broad range of observations, experiments, and conclusions
A
theory
5
Q
- untreated subjects used as tested benchmark
- group of test subjects left untreated or unexposed to some procedure and then compared with treated subjects in order to validate the results of the test
A
control group
6
Q
group of subjects that are exposed to the variable of a control experiment
A
experimental group
7
Q
is manipulated by the investigator, what is being tested
A
independent variable
8
Q
represents the result of the manipulation of the experimental variable, what is being measured
A
dependent variable
9
Q
all variables that must be held constant in both the control and experimental groups
A
standardized variable
10
Q
steps of the scientific method
A
- make observations
- make hypothesis
- design the experiment
- record data
- analyze data
- draw conclusions
- make a new hypothesis
11
Q
all living things are composed of __
A
matter
12
Q
all matter is composed of __
- smallest functional unit of matter
- can’t be further broken down into other substances
- each specific type is a chemical element
- entire __ has no net electric charge
A
atoms
13
Q
organization of living things
A
- atoms
- molecules
- organelles
- cells
- organs
- organisms
- population
- communities
- ecosystem
- biosphere
14
Q
negative subatomic particle
A
electron
15
Q
positive subatomic particle
A
proton
16
Q
neutral subatomic particle
A
neutron
17
Q
95% of the atoms in living organisms (three total)
A
- water= hydrogen + oxygen
- nitrogen= proteins
- carbon= building blocks
18
Q
less than 1% in living organisms
A
mineral elements
19
Q
less than 0.01% in living organisms
A
trace elements
20
Q
atoms of an element that differ in the number of neutrons their atoms carry
A
isotopes
21
Q
an electrons state of potential energy
A
energy level or electron shell
22
Q
region in which an electron travels
- can only hold 2 electrons
A
orbital
23
Q
2 or more atoms bonded together
A
molecule
24
Q
molecule composed of 2 or more elements
A
compound
25
an attractive force that links two atoms together
chemical bond
26
three types of bonds
1. covalent (polar and nonpolar)
2. hydrogen
3. ionic
27
atoms share a pair of electrons
- occurs between atoms whose outer electron shells are not full
- STRONG BONDS
covalent bonds
28
electrons NOT always shared equally
- sharing with different electronegativities
-example: bonds within H2O
polar covalent bonds
29
EQUAL sharing of electrons
-bonds between atoms with SIMILAR electronegativities
- example: O2
nonpolar covalent bonds
30
hydrogen atom from one polar molecule is attracted to an electronegative atom (N, F, O)
- do not share electrons
- individually WEAK but collectively STRONG bond overall
hydrogen bond
31
complete transfer of electrons
- ions are formed when an atoms loses or gains electrons: cations (+) or anions (-)
ionic bonds
32
structure and special properties of water (5 total)
1. cohesion
2. high heat of vaporization
3. high heat capacity
4. relationship between density and temperature
5. solvent
33
H bonds between molecules
- tends to stick together: surface tension and viscosity
cohesion/adhesion
34
take a large amount of heat for molecules to separate and enter the gas phase
high heat of vaporization
35
takes a great deal of energy to change the temperature of water
high heat capacity
36
-water becomes more dense as it cools until 4c
- lower then 4c it decreases density
-why ice floats
density and temperature
37
living organisms are over 70% water by weight and many reactions take place in this watery environment
- ions and molecules that contain polar covalent bonds will dissolve in water
- solution in a substance (the solute) dissolved in a liquid (solvent)
solvent
38
functions of water (6 total)
1. participate in chemical reactions (hydrolysis or dehydration)
2. provide support
3. detoxify
4. evaporate cooling
5. cohesion and adhesion
6. surface tension
39
organic molecules contain __
carbon
40
large, complex organic molecules
macromolecules
41
groups of atoms with special chemical features that are functionally important
- each type exhibits the same properties in all molecules in which it occurs
function groups
42
two molecules with an identical molecular formula but different structures and characteristics
isomers
43
contain the same atoms but in different bonding relationship
-examples: glucose and galactose
structural isomers
44
identical bonding relationships, but the spatial positioning of the atoms differs in the two isomers
- example: alpha and beta glucose
stereoisomers
45
positioning around double bond
cis-trans isomers
46
mirror image molecules
enantiomers
47
links monomers to form polymers
-releases water
condensation or dehydration reaction
48
polymers broken down into monomers
- needs waters
hydrolysis reaction
49
composed of carbon, hydrogen, and oxygen atoms
- most of the carbon atoms are linked to a hydrogen atom and a hydroxyl group
carbohydrates
50
simplest sugars
- most common are 5 or 6 carbons: pentose (ribose or deoxyribose) and hexose (glucose)
- ring or linear
monosaccharides
51
composed of two monosaccharides
- joined by dehydration or condensation (glycosidic bond)
- broken apart by hydrolysis
-example: sucrose, maltose, lactose
disaccharides
52
many monosaccharides linked together to form long polymers
- example: energy storage (starch, glycogen) and structural (cellulose, chitin, glycosaminoglycan)
polysaccharides
53
composed predominantly of hydrogen and carbon atoms
- defining feature is that they are nonpolar and very insoluble in water
- comprise about 40% of the organic matter in the average human body
-examples: fats, phospholipids, steroids, waxes
lipids
54
aka triglycerides
- formed by bonding glycerol to 3 fatty acids
- joined by dehydration; broken apart by hydrolysis
- important for energy storage
- can also be structural by providing cushioning and insulation
fats
55
all carbons linked by single bonds
- tend to be solid at room temperature
saturated
56
contain one or more double bonds
- tend to be liquid at room temperature
- cis form naturally; trans form artificially
- trans are linked to disease
unsaturated
57
formed from glycerol, two fatty acids and a phosphate group
- amphipathic: polar hydrophilic head and nonpolar hydrophobic tail
phospholipids
58
four interconnected rings of carbon atoms
- usually insoluble in water
- specific biological properties
- example: cholesterol
steroids
59
composed of carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements, notably sulfur
- building block are amino acids
- common structure with variable sidechain that determines structure and function
proteins
60
amino acids joined by dehydration reaction; broken down by hydrolysis
- polymers of amino acids
- proteins may be formed from one or several
polypeptide formation
61
- amino acid sequence
- encoded directly by genes
primary structure
62
chemical and physical interactions cause protein folding
- alpha helices and beta pleated sheets (key determinants of protein characteristics)
- "random coiled regions", not alpha or beta (shape is specific and important to function)
secondary structure
63
folding gives protein complex 3D shape
- final level of structure for a single polypeptide protein
tertiary structure
64
made up of two or more polypeptides
- composed from different polypeptides
quaternary structure
65
factors that promote protein folding and stability (5 total)
1. hydrogen bonds
2. ionic bonds and other polar interactions
3. hydrophobic effects
4. van der waals forces
5. disulfide bridges
66
responsible for the storage, expression, and transmission of genetic information
- DNA or RNA
nucleic acids
67
- performed in vitro: no other cellular components present
- chemical that disrupt bonds caused the enzyme to lose function; removal of those chemicals restored function
- conclusion: even in the complete absence of any cellular factors or organelles, an unfolded protein can refold into its functional structure
Anfinsen's Ribonuclease experiment
68
made up of phosphate group, five carbon sugar, and a single or double ring or carbon and nitrogen known as base
nucleotide
69
ratio between size of the image and the actual size
magnification
70
ability to observe two adjacent images as distinct
resolution
71
how different a structure looks from another structure
contrast
72
uses light waves
- electron beam through sample
- cross sectional
- good for looking at organelles and things inside the cell
- examples: mitochondria, nucleus, most bacteria, most plant and animal cells
light microscopes
73
uses a beam of electrons
- electron beam bounces off surface
- surface structure
- good for looking at details on the surface
- examples: lipids, proteins, ribosomes, smallest bacteria, mitochondria, nucleus, most bacteria, most plant and animal cells
electron microscopes
74
- all living organisms are composed of one or more cells
- cells are the smallest unit of life
- new cells come only from pre existing cells by cell division
cell theory
75
controls entrance and exit of materials (all cells have)
plasma membrane
76
water, salts, sugars, organelles, etc. (all cells have)
cytoplasm
77
structure influences function
proteome
78
- no membrane bound organelles
- smaller
- domains: bacteria and archaea
prokaryotic
79
- membrane bound organelles
- typically larger
- domains: eukarya
eukaryotic
80
-region of cell within the cell membrane
- water and dissolved materials
- functions: metabolic, cell shape and movement
cytosol
81
- internal network of protein filaments (microtubules, intermediate, actin)
- structural support
- ability to move
cytoskeleton
82
- tubulin proteins
- can lengthen and shorten
microtubules
83
- relatively permanent
- tension bearing
intermediate filament
84
- actin proteins
- can lengthen and shorten
actin filament
85
- use ATP to move along filaments
- carry materials or cause movements
motor proteins
86
contains DNA in the cell
chromatin
87
genes coding for ribosome subunit
nucleolus
88
-double membrane
-pores
nuclear envelope
89
protein factories of the cell (decode genetic material, arrange amino acids in precise order)
- each cell contains thousands of ribosomes
- located in: cytoplasm, rough ER
ribosomes
90
network of membranes
- smooth and rough
endoplasmic reticulum
91
- ribosomes embedded
- location where proteins are made
rough ER
92
- no ribosomes
- detoxfication
- manufacture lipids or carbohydrates
- store calcium in muscle cells
smooth ER
93
accepts proteins shipped from the ER and modifies, activates, and tags proteins
golgi apparatus
94
- membranous vesicles filled with enzymes
- break down waste products, damaged organelles, bacteria, and food particles
lysosomes
95
- plants, fungi, some protist
- storage of water, pigments, or other materials
- important for plant cell growth
- water excretion
vacuole
96
- break down toxins or organic molecules
- uses hydrogen peroxide
peroxisomes
97
- cellular respiration
- two membranes: cristae and matrix
mitochondria
98
- mitochondria and chloroplast have symbiotic relationship between bacteria and host cell
- all eukaryotic cells have mitochondria
- plant cells also have chloroplast
endosymbiosis theory
99
- estimate 20 to 30% of your genes code for membrane proteins
- transmembrane
- lipid anchored
- peripheral
membrane proteins
99
- controls entrance and exit of materials
- forms compartments
- provides a substrate for metabolic reactions
- cell signaling and communication
- adhesion of cells to each other and the extracellular matrix
plasma membrane
99
- non polar substances pass freely (oxygen, carbon dioxide gas, small lipids)
- polar substances do not pass freely (water, ions, sugars, proteins)
selective permeability
100
- with gradient so no energy needed
- simple or facilitated
passive diffusion
101
against gradient so energy needed
- uniporter, symporter, antiporter
active transport
102
passive diffusion of water across a semi permeable membrane
- high WATER concentration: low solute concentration
- low WATER concentration: high solute concentration
osmosis
103
if solute concentration of the solution is greater than the cell
hypertonic
104
if solute concentration of the solution is less than the cell
hypotonic
105
transports a single solute in one direction (active transport)
uniporter
106
two solutes move in the same direction (active transport)
symporter
107
move two solutes in opposite directions (active transports)
antiporter
108
movement of membrane
exocytosis
109
3 Na released out of cell and 2 K brought into cell
- important for neurons and muscle cells
sodium potassium pump
110
potential energy stored in chemical bonds
chemical energy
111
random motion or particles (kinetic)
heat
112
kinetic movement of charged particles
electrical energy
113
directly moves matter (kinetic)
mechanical energy
114
electromagnetic energy (kinetic)
radiant energy
115
energy can be transferred and transformed but not created or destroyed
first law of thermodynamics
116
energy conversion reduce the order of the universe; entropy increases
second law of thermodynamics
117
these reactions produce energy
exergonic
118
these reactions require input of energy
endergonic
119
negative free energy change
favors products
120
positive free energy change
favors reactants
121
- proteins
- specific (have a specific shape)
- catalyst (lower the activation energy of a reaction)
enzymes
122
affects rate of enzyme action (5 total)
1. substrate concentration
2. temperature
3. anything that can change the proteins structure
4. inhibitors
5. non protein molecules or ions
123
bind to the active site
competitive inhibition
124
bind to another spot and change the active site
noncompetitive inhibition
125
-larger molecules to smaller molecules
- usually exergonic
- polymers to monomers (hydrolysis)
catabolic reactions
126
- use smaller molecules to build larger molecules
- usually endergonic
- monomers to polymers (dehydration)
anabolic reactions
127
adds elections
reduction
128
removes elections
oxidation
129
- process by which living cells obtain energy from organic molecules
- primary aim to make ATP and NADH
- aerobic respiration uses oxygen
- primarily use glucose but other organic molecules also used
cellular respiration
130
occurs with or without oxygen
- stage 1 of cellular respiration
- three phases: energy investment, cleavage, energy liberation
glycolysis
131
- steps 1 to 3
- 2 ATP hydrolyzed to create fructose 1, 6 bisphosphate
energy investment (glycolysis)
132
- steps 4 to 5
- 6 carbon molecules broken into two 3 carbon molecules of glyceraldehyde 3 phosphate
cleavage (glycolysis)
133
- steps 6 to 10
- two glyceralydehyge 3 phosphate molecules broken down into two pyruvate molecules: produces 2 NADH and 4 ATP (NET YIELD OF 2 ATP)
energy liberation (glycolysis)
134
- stage 2 of cellular respiration
- in eukaryotes, pyruvate is transported into the mitochondrial matrix
- broken down by pyruvate dehydrogenase
- molecule of CO2 removed from each pyruvate
- remaining acetyl group attached to CoA to make acetyl CoA
- yields 1 NADH for each pyruvate
breakdown of pyruvate
135
- stage 3 of cellular respiration
- metabolic cycle: some molecules enter while other leaves and series of organic molecules regenerated in each cycle
- acetyl is removed from acetyl CoA and attached to oxaloacetate to form citric acid
- releases 2 CO2, 1 ATP, 3 NADH, 1 FADH2
- oxaloacetate is regenerated to start cycle again
citric acid cycle
136
- stage 4 of cellular respiration
- high energy electrons removed from NADH and FADH2 to make ATP
- typically requires oxygen
- oxidative process involves electron transport chain
- phosphorylation occurs by ATP synthase
oxidative phosphorylation
137
- protein complexes and small organic molecules embedded in the inner mitochondrial membrane
- accept and donate electrons in linear manner in a series of redox reactions
- movement creates H+ electrochemical gradient (proton motive force)
- provides energy for next step
oxidation by ETC
138
- breakdown of organic molecules without net oxidation
- muscle cells reduce pyruvate into lactate
- yeast makes ethanol
- produces far less ATP than oxidative phosphorylation
fermentation
139
- captures free energy as H+ ions flow through
- enzyme converts energy from proton motive force of H+ gradient to chemical bond energy in ATP
ATP synthase
140
- creates the H+ electrochemical gradient used to synthesize ATP
- yields up 30 to 34 ATP/glucose
NADH oxidation
141
- lipid bilayer of inner mitochondrial membrane is relatively impermeable to H+
- protons can only pass through ATP synthase
- harness free energy to synthesize ATP from ADP
- chemiosmosis: chemical synthesis of ATP as a result of pushing H+ across a membrane
phosphorylation of ATP synthase
142
energy within light is captured and used to synthesize carbohydrates
- CO2 is reduced
- H2O is oxidized
- energy from light drives this endergonic reaction
photosynthesis
143
regions on the surface of the Earth and atmosphere where living organisms exit
- largely driven by the photosynthetic power of green plants
biosphere
144
cells use organic molecules for energy and plants replenish those molecules using photosynthesis
energy cycle
145
must eat food (organic molecules from their environment) to sustain life
heterotroph
146
makes organic molecules from inorganic sources
autotrophs
147
- use light as a source of energy
- green plants, algae, cyanobacteria
photoautotroph
148
majority of photosynthesis occurs internally in the leaves
mesophyll
149
carbon dioxide enters and oxygen exits leaf through pores
stomata
150
third choloplast membrane, contains pigment molecules
thylakoid membrane
151
stack of thylakoids
granum
152
fluid filled region between thylakoid membrane and inner membrane
stroma
153
- uses light energy
- takes place in thylakoid membrane
- produces ATP, NADPH, and O2
light reaction
154
- occurs in stroma
- used ATP and NADPH to incorporate CO2 into carbohydrate
- requires massive input of energy
- product is glyceraldehyde 3 phosphate (G3P)
- three phase: carbon fixation, reduction, regneration
calvin cycle
155
wavelength that are absorbed by different pigment
absorption spectrum
156
rate of photosynthesis by whole plant at specific wavelengths
action spectrum
157
- initial step in photosynthesis
- excited electrons travel from PSII to PSI
- oxidizes water, generating O2 and H+
- releases energy in electron transport chain (ETC)
- energy used to make H+ electrochemical gradient
- light harvesting: directly absorbs photons, energy transferred via resonance energy transfer
- reaction center: P680
photosystem II
158
- primary role to make NADPH
- addition of H+ to NADP+ contributes to H+ gradient by depleting H+ from the stroma
photosystem I
159
- electrons begin in PSII and eventually transfer to NADPH, a linear process
- produces both ATP and NADPH in equal amounts
noncyclic
160
- electron cycling releases energy to transport H+ into lumen driving ATP synthesis
- produces only ATP
- PSI electrons excited, release energy and eventually return to PSI
cyclic
161
-zigzag shape of energy curve
- involves increases and decreases in the energy of an electron as it moves from PSII through PSI
Z scheme
162
phase 1 of calvin cycle
- CO2 incorporated into RuBP using rubisco
- reaction product is a six carbon intermediate that splits into two 3PG
carbon fixation
163
phase 2 of calvin cycle
- ATP is used to convert 3PG into 1, 3 BPG
- NADPH electrons reduce it to G3P
-6 CO2 to 12 G3P
reduction and carbohydrate production
164
phase 3 of calvin cycle
- 10 G3P are converted into 6 RuBP using 6 ATP
regeneration of RuBP
165
- evolved a mechanism to minimize respiration
- make oxloacetate
- leaves have two cell layer organization: mesophyll cells and bundle sheath cells
C4 plants
166
- some C4 plants separate processes using time
- Crassulacean Acid Metabolism
- plants open their stomata at night
- stomata close during the day to conserve water
CAM plants
