Final Exam review Flashcards
1
Q
Forms of an element with different numbers of neutrons, and thus different mass numbers
A
Isotopes
2
Q
Particles with negative charge that determine the charge of an atom
A
Electron
3
Q
four most common elements in living organisms
A
Carbon, Oxygen, Nitrogen, Hydrogen
4
Q
The smallest unit of matter that retains all chemical properties of an element
A
Atom
5
Q
Particles with positive charge that identify the element.
A
Protons
5
Q
Proton, Neutron, Electron
A
Sub-atomic particles
6
Q
Particles with neutral charge that contribute to an atom’s mass
A
Neutron
7
Q
The outermost shell of an atom that determines its behavior
A
Valance Shell
8
Q
Substances used at the beginning of a reaction
A
Reactants
9
Q
Substances formed at the end of a reaction
A
products
9
Q
The attractive force that links atoms together to form molecules
A
Chemical Bonds
10
Q
Bonds where electrons are shared between atoms
A
Covalent Bonds
11
Q
Bonds where atoms give up or gain electrons
A
Ionic Bond
12
Q
The positive charge of hydrogen in a water molecule bonds/is attracted to the negative oxygen from a different water molecule
A
Hydrogen Bond
13
Q
The liquid that dissolves other things
A
Solvent
14
Q
What gets dissolved (sugar)
A
Solute
15
Q
Water molecules at the liquid-gas interface stick together due to hydrogen bonding
A
Cohesion
16
Q
The capacity of a substance to withstand being ruptured when placed under tension or stress
A
Surface Tension
17
Q
Determined by the pH (percent hydrogen) of a solution indicated
A
Acidity or Alkalinity
17
Q
Attraction between water molecules and other molecules
A
Adhesion
18
Q
Has more hydrogens
A
Higher in Acidity
19
Q
Key Component of Macromolecules
A
Carbon
20
Q
Molecules consisting of carbon and hydrogen
A
Hydrocarbons
21
Q
Molecules that have the same chemical formula but differ in placement/arrangement of atoms or types of bonds between atoms
A
Isomer
21
Isomers that have a different covalent arrangement of atoms
Structural Isomers
22
Isomers that have a different arrangement of atoms around a double bond
Geometric Isomers
23
Molecules that share chemical formula and bonds but differ in 3D placement of atoms; mirror images
Enantiomers
24
Groups of atoms within a molecule that confer consistent specific properties to these molecules
Functional Groups
25
functional group with an oxygen and a hydrogen atom
Hydroxyl
26
A functional group with a nitrogen atom bonded to two hydrogen atoms
Amino
27
A functional group with a phosphorus atom bonded to four oxygen atoms
Phosphate
28
Carbohydrates, Lipids, Proteins, Nucleic Acid
Major Classes of Macromolecules
29
Individual sub-units that macromolecules consist of
Monomers
30
Monomers that are linked together via covalent bonds
Polymers
31
The process where two molecules of glucose are linked to form the disaccharide maltose
Dehydration Synthesis
32
The process of breaking polymers down into individual monomers - also known as a dehydration reaction
Hydrolysis
33
Biological molecules that catalyze or 'speed up' reactions
Enzymes
33
Found in grains, fruits, and vegetables. Provide energy to the body in the form of glucose
Carbohydrates
34
Monosaccharides, Disaccharides, Polysaccharides
Three Main Carbohydrate Subtypes
35
Carbohydrates with 3-7 carbons
Monosaccharides
36
A monosaccharide with six carbons
Glucose
37
CH2O
Sugar Formula
37
Disaccharides are formed when two monomers are joined by a dehydration synthesis
Glycosidic Bond
38
Are created by Glycosidic
Linkages Maltose, Lactose, and Sucrose
39
Non-polar
Polarity of Lipids
40
Glycerol and Fatty Acids
Two main components of Fats
41
Formed by three fatty acids joining a glycerol backbone
Triglycerol
41
Molecules with two fatty acids and a modified phosphate group attached to a glycerol backbone
Phospholipids
42
Includes a head followed by a tail.
Phospholipid Bilayer
43
Molecules with four linked carbon rings
Steroids
44
steroid with four rings
Cholesterol
45
Catalysts in biochemical reactions
Enzyme
46
A diverse range of function
Protein
47
The monomers that make up proteins
Amino Acids
48
Amino acid monomers are linked via peptide bond formation (dehydration synthesis reaction
Peptide Bond
49
Based upon four levels of structure
Protein Shape
50
DNA and RNA
Two Types of Nucleic Acid
51
Primarily involved in protein synthesis
RNA
52
DNA and RNA Monomers
Nucleotides
53
Nucleotides' three parts are:
Nitrogenous base, Pentose sugar, and One or more phosphate groups
54
Stronger than a light microscope
Electron microscope
55
four common components of cells
Cytoplasm, Plasma membrane, DNA, Ribosomes
56
Lack membrane-enclosed organelles
Prokaryotes
57
Lacks in prokaryotes
Nucleus
58
Location of DNA in prokaryotes
Nucleoid
59
Perforate the nuclear envelope membrane
Nuclear pores
60
Site for conversion of stored energy (ATP)
Mitochondria
61
Contain digestive enzymes
Lysosomes
62
Mitochondria and chloroplasts originated as independent prokaryotic organisms, are the ancestors of eukaryotic cells
Endosymbiosis hypothesis
63
Internal membranes and organelles that modify, package, and transport lipids and proteins
Endomembrane System
64
Modifies proteins and synthesizes lipids
Endoplasmic reticulum (ER)
65
Ribosomes attach to create proteins (rough ribos)
Rough Endoplasmic reticulum
66
Synthesizes carbohydrates, lipids, steroid hormones, and stores Ca++ (smooth like butter)
Smooth Endoplasmic Reticulum
67
Transports lipids or proteins in vesicles to be stored, packaged, and tagged (amazon of cell)
Golgi Apparatus
68
Highways of cells and helps maintain the shape of cells
Cytoskeleton
69
Hairs on the cell
Cilia
70
Tails that move the cell (sperm lookin)
Flagella
71
plasmodesmata, tight junctions, desmosomes, gap junctions
types of intercellular junctions
72
Provide direct channels of communication between cells
Intercellular Junctions
73
Cytoplasm connecting channels that allow materials to move from cell to cell
Plasmodesmata
74
Watertight seals that prevent materials from leaking
Tight junctions
75
Short proteins in the plasma membrane that act as spot welds
Desmosomes
76
Protein-lined pores that allow water and small molecules to pass
Gap junctions
77
All chemical reactions of a cell or organism
Metabolism
78
Small molecules are assembled into large ones, energy is required
Anabolic
79
Large molecules are broken down into small ones, energy is released
Catabolic
80
Energy of objects in motion
Kinetic energy
81
Energy of objects that have the potential to move
Potential energy
82
Amount of energy available to do work
Gibb's Free Energy (G)
83
the reaction will happen no matter if I put energy into it
negative G value
84
energy is needed for reaction
positive G value
85
Energy required for a reaction to proceed
Activation Energy
86
Protein catalysts that speed up reactions by lowering the required activation energy
Enzymes
87
Molecules that interact at the enzyme's active site
Substrate
88
where the substrate and enzyme interact and react
active site
89
Mild shift in shape at the active site that optimizes reactions
Induced Fit
90
Modify the active site of the enzyme to reduce or prevent substrate binding
Allosteric inhibitors
91
Modify the active site of the enzyme to increase substrate affinity
Allosteric activators
92
Have a similar shape to the substrate, competing for the active site
Competitive inhibitors
93
Bind to the enzyme at a different location, causing a slower reaction rate
Noncompetitive inhibitors
94
End product of a pathway inhibits an upstream step
Feedback inhibition
95
Defining outer border, managing what enters and exits the cell, receiving external signals, adhering to neighboring cells
Plasma Membrane Functions
96
Main fabric of the plasma membrane composed of an amphiphilic lipid molecule
Phospholipids
97
Proteins that go through the membrane
Integral Proteins
98
Proteins on the side of the membrane, inside or out, never through
Peripheral Protein
99
Affected by phospholipid type, temperature, and cholesterol
Fluidity
100
Allows some molecules to pass through, but not others
Selective Permeability
101
Diffusion of substances down their concentration gradient (from high concentration to low)
Passive transport
102
Greater difference results in faster diffusion
Concentration gradients
103
Moves substances down their concentration gradients through transmembrane proteins
Facilitated transport
104
Diffusion of water across a membrane
Osmosis
105
Describes how extracellular solutions can change the volume of a cell by affecting osmosis
Tonicity
106
Extracellular fluid has lower osmolarity than the cytosol - water leaves the cell (shrivels)
Hypotonic
107
Extracellular fluid has the same osmolarity as the cytosol - water does not move (normal)
Isotonic
108
Extracellular fluid has higher osmolarity than the cytosol - water enters the cell(busts)
Hypertonic
109
Transport of ions or molecules against their concentration or electromagnetic gradient
Active Transport
110
Uses energy from ATP hydrolysis to move ions or molecules up their concentration gradient
Primary active transport
111
Uses an electrochemical gradient to move a different substance against its concentration gradient
Secondary active transport
112
Cytoplasm contains more negatively charged molecules than the extracellular fluid
Electrochemical Gradients
113
Does not require energy or ATP
Passive transport
114
Requires energy or ATP
Active transport
115
Carries one molecule or ion
Uniporter
116
Carries two different molecules or ions in the same direction
Symporter
117
Carries two different molecules or ions in different directions
Antiporter
118
Occurs when cells need to import or export large molecules/particles
Bulk Transport
119
bulk transport requires..
energy
120
Process of bringing substances into the cell
Endocytosis
121
Cell membrane surrounds a particle and engulfs it (cellular eating)
Phagocytosis
122
Cell membrane invaginates, surrounds a small volume of fluid, and pinches off (cellular drinking)
Pinocytosis
123
Uptake of a specific substance targeted by binding to receptors on the membrane
Receptor mediated endocytosis
124
Vesicles containing substances fuse with the plasma membrane and release contents to the exterior of the cell (exit)
Exocytosis
125
When a molecule gains an H, (xH)
Reduction
126
When a molecule loses an H, it has been oxidized (+)
Oxidation
127
Carries 2e- and 1H+ more than NAD
NADH
128
Result of a redox reaction
FADH and NADPH
129
Process of adding a phosphate group to a molecule, producing energy
Phosphorylation
130
Metabolic pathway that occurs in the cytosol, does not require oxygen
Glycolysis
131
Occurs when there is no or not enough oxygen in the cell
Fermentation
132
Occurs when there is oxygen in the cell
Cellular respiration
133
Outcome of glycolysis
Pyruvate
134
Result of the oxidation of pyruvate
Acetyl CoA
135
Metabolic pathway that results in reduced molecules and oxaloacetate
Citric Acid Cycle
136
Involves electrons, electron carriers, protons, and oxygen
Oxidative Phosphorylation
137
Allow electrons to pass through
Electron carriers
138
Final electron acceptor in Oxidative Phosphorylation
Oxygen
138
Found in the intermembrane space, move down the electron gradient to create ATP
Protons
139
Macromolecules that can be broken down
Lipids, Fats, and Proteins
140
Converts light energy to chemical energy, occurs in the thylakoid membrane
Light reaction
141
Location where light reaction occurs
Thylakoid membrane
142
Occurs in the stroma of chloroplasts, fixes carbon
Calvin Cycle
143
Main pigments of thylakoid membranes
Chlorophylls
144
145
146
Type of carotenoid, main pigment of thylakoid membranes
Carotene
147
Capture light for photosynthesis
chlorophyll a, chlorophyll b and carotenoids
148
Require water and light
Photosystems
149
Molecule necessary for carbon fixation in the Calvin Cycle
RuBP
150
Process that requires carbon, occurs in the Calvin Cycle
Carbon fixation
151
Goal of the Calvin Cycle, a three-carbon sugar
G3P
152
Signals move by diffusion through extracellular matrix
Paracrine signaling
153
Signals distant cells, produce a slower response with long-lasting effect
Endocrine signaling
154
Signals cells that can also bind to the released ligand
Autocrine signaling
155
Allows small signaling molecules to move between cells
Direct signaling across gap junctions
156
Gated ion channels that open when the signaling molecule binds
Ion channel-linked receptors
157
Trigger a cellular response when the signaling molecule binds
G-protein-linked receptors
158
Receptor tyrosine kinase, triggers a cellular response
Enzyme-linked receptors
159
Transmission of a signal through the cell membrane and into the cytoplasm
Signal transduction
160
Two receptors bind to each other to form a stable complex
Dimerization
161
Chain of events that follow ligand binding to a receptor
Signaling pathway
162
Signals from different receptors merge to activate the same response
Signal integration
163
Enzyme that catalyzes the transfer of a phosphate group (kind enough to lend Ph)
Kinase
164
Series of steps where kinase is given phosphate, creating an activation cascade
Phosphorylation Cascade
165
Small molecules that propagate a signal after binding of the signaling molecule to the receptor
Second Messengers
166
Cell death, termination of cell signals
Apoptosis
167
23 of them, Contain DNA, x and y
Chromosomes
168
have 2 matched sets of chromosomes (diploid)
somatic cells
169
have half the number of chromosomes (haploid)
gametes
170
Structure of DNA
DNA double helix
171
DNA wraps around histone protein
Histone protein
172
Coiling of DNA and histone protein
Nucleosome
173
Further condensation of nucleosome
Chromatin fiber
174
Result of DNA synthesis
Duplicated chromosomes
175
Includes mitosis and cytokinesis (can tell by looking)
Mitotic Phase
176
synthesis phase, doubling of DNA
S DNA
177
growth phases
G1 and G2
178
Nuclear division
Mitosis
178
Chromosomes condense, nuclear envelope breaks down
Prophase
179
Chromosomes line up along metaphase plate
Metaphase
180
Chromatids become separated and pulled apart
anaphase
181
Chromosomes reach opposite poles and begin to decondense
Telophase
182
Completes cell division via physical separation of cytoplasmic components
Cytokinesis
183
Control points in the cell cycle at G1, G2, and metaphase of mitosis
Regulated internal checkpoints
184
Promote movement to the next step of the cell cycle
Positive regulators
185
Stop the advancement of the cell cycle
Negative regulators
186
Positive regulators of the cell cycle
Cyclins and Cyclin-dependent kinase (Cdks)
187
Negative regulators of the cell cycle
Retinoblastoma protein (Rb), p53, p21
188
Considered the father of genetics
Gregor Medel
189
Result of true breeding
Parent generation (P)
190
First filial generation from a cross between siblings (brother and sister)
F1 hybrid
191
Second filial generation produced by crossing 2 F1 individuals
F2
192
Succeeding generation after F2 (stabalized)
F3, F4, and F5
193
Characteristic version of a trait that is observable (blue eyes)
Phenotype
194
Specific versions of a gene
Alleles
195
Alleles that mask others, often designated with capital letters
Dominant
196
Specific combination of alleles that determines the phenotype
Genotype
196
Alleles that are masked by others, often designated with lowercase letters
Recessive
197
Individual with both alleles for the same trait being the same (PP - are true breeding)
Homozygote
198
Individual with alleles for the same trait being different (Pp - are non-true breeding)
Heterozygote
199
place of interest on a chromosome, usually a gene
locus
200
the most common allele in a population (normal allele)
wildtype allele
201
a rare allele in a population. reasoned to be the most recently formed allele by mutation (non-normal allele)
mutant allele
202
can be used to make genetic inferences
pedigree
203
Situation in which one allele is not completely dominant over another allele (shared dominance, mixed phenotypes)
incomplete dominance
204
using a virus as a syringe to do experiements
bacteriophages
205
was a part of the team that discovered the structure of the DNA helix (along w/ Watson and Crick)
Rosalind Franklin
206
three different parts:
sugar, nitrogenous base, and phosphate group
Each nucleiotide is made up of-
207
carbon one, carbon three, carbon five
the three important carbons
208
has the nitrogenous base
carbon one
209
hydroxl group, where reaction occurs with new nucleiotides
carbon three
210
ALWAYS attatches the the phosphate group
carbon five
211
3' end
which end do nucleotides attatch to
211
5' to 3'
direction of DNA
212
is formed when helicase separates the DNA strand at the orign of replication
replication fork
213
the enzyme the unzips (separetes top and bottom strands) DNA
helicase
214
Synthesizes RNA primers needed to start replication
primase
214
prevents the overwidening of the DNA strands (removes tension)
tomoisomerase
215
bind to the single strand of DNA tp prevent the helix from refomring (keeps the strantds open)
Single-strand binding proteins
216
synthesizes new DNA on the leading strand
DNA polymerase iii
217
bacckfilled with RNA primer
the lagging strand gets-
218
is added to the ends of DNA strands to protect and maintain DNA
Telomerase enzyme
218
seals the gaps between DNA (okazaki fragmants)
DNA ligase
218
replaces RNA primer with DNA
DNA polymerase i
219
has no effect on the protein sequence
silent mutations
220
result in an amino acid substitution
missense mutation
221
substitues a stop codon for an amino acid (confusing)
nonsene mutation
222
may result in a whole shift in the reading frame or insertion of a stop codon
frameshift mutations
223
DNA is first transcribed into mRNA, then mRNA is translated into proteins
central dogma
224
promoter (piece of upstream DNA) indicates where the RNA polymerase should bind to begin process
transcription initiation
225
RNA polymerase adds complimentary nucleotides (ACUG) to make mRNA
transcription elongation
226
include anticodons which attach to corresponding codons
tRNA (transfer RNA)
226
mRNA attaches to the smaller subunit of a ribosome
translation initiation
227
tRNA move into the appropriate amino acid in groups of three, to code into the correct protein, and the chain of proteins grows
translation elongation
228
are within the ribosome structure, mRNA moves through the order of A-P-E
E-P-A sites
229
mRNA enters and confirms the match
A-site
230
for making polypeptides, the ribosome attaches to the existing chain
P-site
231
where the codon ejects and binds to a specific structure
E-site
232
the ribosome reaches a STOP codon, the ribisome breaks and releases the mRNA
translation termination
