Final Review Flashcards

(182 cards)

1
Q

Characteristics of living things

A

1: maintain internal order
2: capable of reproduction
3: capable of growth and development
4: energy use and metabolization
5: maintain homeostasis
6: respond to environment
7: capable of evolution

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Vertical Evolution

A

-progression of changes in a lineage
-new species evolve from pre existing species by the accumulation of mutations that are filtered by natural selection
EXAMPLE: horse

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Horizontal Gene Transfer

A

genetic exchange between different species, extremely rare.

EXAMPLE: antibiotic resistant bacteria

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Binomial Nomenclature

A
  • gives each species a unique scientific name
  • (Genus)(Species)
  • Both italicized, only Genus is capitalized
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Genome

A

the complete genetic makeup of an organism. Genomics, analyzes DNA sequences

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Proteome

A

Complete complement of proteins that a cell or organism can make. The genome carries info to make the proteome.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Steps of scientific method

A
  • make observations
  • form hypothesis
  • design experiment
  • record data
  • analyze data
  • draw conclusions
  • make new hypothesis
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Deductive Reasoning

A

General to specific

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Inductive Reasoning

A

Specific to general

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Control group

A

Untreated test subject used as benchmark

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Experimental Group

A

a group of subjects that are exposed to the variable of a control experiment.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Independent Variable

A

manipulated by the investigator

what is being tested

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Dependent Variable

A

Represents the result of the manipulation of the experimental variable.
what is being measured

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Atoms

A
  • smallest functional units of matter
  • cannot be further broken down into other substances
  • each specific type of element is a chemical element
  • entire atom has no net electric charge
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

three subatomic particles and there charges

A
  • protons(+)
  • neutrons(0)
  • electrons(-)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Isotopes

A

atoms of an element that differ in the number of neutrons they carry

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

How are electrons held in atoms

A
  • electrons held in orbitals
  • each orbital can hold only 2 electrons
  • any atom with more than 2 electrons has more than 1 orbital
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Covalent Bonds

A
  • atoms share a pair of electrons
  • occurs between atoms whose outer electron shells are not full
  • strong chemical bonds because electrons behave as if they belong to each atom
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Polar Covalent Bonds

A

-oxygen has higher electronegativity
-molecule has partial negative region and partial positive region
shared electrons spend more time near the oxygen atom
EXAMPLE: H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Nonpolar covalent

A

bonds between atoms with similar electronegativities, equal sharing of electrons
EXAMPLE:O2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Hydrogen Bonds

A

hydrogen atom (slight + charge) from one polar molecule is attracted to an electronegative atom.

  • do not share electrons
  • individually weak
  • collectively strong bond
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Ionic Bonds

A

complete transfer of electrons

-ions are formed when an atom loses or gains an electron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

properties of water

A
  • cohesion
  • high heat of vaporization
  • high heat capacity
  • density and temperature
  • solvent
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

cohesion

A

bonds between molecules stick together, responsible for surface tension and viscosity of water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Acids
dissolve in water and release hydrogen ions.
26
strong acids
almost completely dissociate HCL into H_ and cl-
27
weak acids
some of the acid does not dissociate
28
Bases
accept H+ in solutions
29
Isomers
Identical molecular formulas but different structures and characteristics
30
Structural Isomers
Contain the same atoms but in different bonding relationships
31
Cis-trans Isomers
contain the same atoms in different positions around double bonds
32
enantiomers
type of stereoisomer in which the molecules are mirror opposites
33
dehydration reaction
forms macromolecules by removing H2O
34
hydrolysis reaction
breaks polymers back down into monomers hy adding H2O
35
4 categories of carbs
- monosacharrides - disaccharides - oligosaccharides - polysaccharides
36
monosaccharides
- simplest form of carbohydrate | - usually 5(pentose) or 6 carbon(hexose)
37
glucose
all living things contain glucose. Glucose is very soluble in water circulates in the blood or fluids of animals where it can be transported accross cell membranes. Once inside a cell enzymes can break down glucose into smaller molecules, releasing energy that was stored in the chemical bonds of glucose.
38
disaccharides
2 monosaccharides joined together by a dehydration reactin that forms what is called a glycosidic bond
39
polysaccharides
- giant polymers connected by glycosidic linkages - sometimes used to store energy - some provide structural roles (chitin)
40
Lipids
hydrophobic molecules composed mainly of hydrogen and carbon atoms.
41
triglycerides "fats"
formed by bonding glycerol to 3 fatty acids. Important for storing energy
42
Steroids
- four interconnected rings of carbon atoms - not very water soluble - hormones and vitamins
43
waxes
provide a barrier to water loss
44
saturated fats
when all carbons in a fatty acid contain covalent bonds
45
unsaturated fats
contain double bonds
46
Primary protein structure
- amino acid sequence | - determined by genes
47
secondary protein structure
- folding in repeating patterns | - either alpha helix or beta pleated sheets
48
tertiary protein structure
folding gives complex three dimensional shape - caused by interaction of side chains - random coils
49
quarternary protein structure
- made up of 2 or more polypeptides | - multimeric proteins
50
purines
- adenine | - guanine
51
pyrimidines
- thymine - cytosine - uracil
52
volume
determines the amount of chemical activity in a cell per unit volume
53
surface area
determines the amount of substances that can pass the cell boundary per unit time
54
Cytosol
region of eukaryotic cell outside the organelles but inside the plasma membrane. Includes everything inside the plasma membrane. Central coordinating region for many metabolic activities.
55
Cytoskeleton
structure: network of three different types of protein filaments, actin, intermediate, and microtubules function: shape & support, movement, tracks for "motor proteins"
56
Nucleus
structure: contains a nucleolus where ribosomes are formed, and surrounded by a nuclear membrane. The nuclear membrane is a double layered endomembrane system. There is also a nuclear envelope consisting of two lipid bilayers that is perforated with nuclear pores function: contains most DNA, DNA duplications
57
Ribosomes
sites of protein synthesis that can be found assembled in the nucleolus, free in cytoplasm, in mitochondria, bound to the ER, in chloroplasts. Made up of ribosomal RNA
58
Rough ER
studded with ribosomes. sorts and folds, inserts proteins into ER membrane, glycosylation.
59
Smooth ER
Lacks ribosomes, continuous with rough ER, function depends on cell type. detoxification, crb metabolism, calcium balance, synthesis and modification of lipids
60
Golgi Apparatus
structure: stack of 3-23 saccules, vesicles transport materials between stacks function: sorting, processing, secretion
61
Lysosomes
specialized vesicles, phagocytosis, autophagy, destroy invaders, apoptosis, uses hydrolytic enzymes to break things down
62
Vacuoles
varied functions, central vauoles in plants, contractile vacuoles in plants, phagocytic vacuoles in white blood cells, store wastes and toxic compounds, store antocyanins (pigment)
63
Peroxisomes
structure: contain specific digestive enzymes including catalase function: breakdown toxic hydrogen peroxide. Found in cells that breakdown large amounts of lipids, liver cells, germinating seeds
64
Plasma Membrane
structure: boundary between cell and extracellular environment. function: membrane transport, cell signalling, cell adhesion, homeostasis
65
Mitochondria
structure: outer and inner membrane, intermembrane space, mitochondrial matrix, contain there own DNA function: make ATP, divide by binary fission
66
Chloroplasts
photosynthesis
67
cell membrane
- bilayered dynamic structure - forms boundaries between cells - regulates movement of molecules into and out of cells - made up of phospholipids, proteins & carbs
68
Membrane Lipid
- framework is the phospholipid bilayer - phospholipids are ampipathic molecules - hydrophobic region faces in - hydrophilic region faces out
69
Cholesterol
- only found in animal cells - stabilizes membranes at high temps - makes more fluids at lower temps
70
integral membrane proteins
- intrinsic - transmembrane proteins - lipid-anchored proteins
71
peripheral membrane proteins
-extrinsic -bound to regions of integral membrane proteins that project out from the membrane or bound to polar head groups of phospholipids
72
membrane carbs
- glycosylation - recognition signals for other cellular proteins - cell surface recognition - protective effects
73
diffusion
net movement of molecules or ions from a region where they are more concentrated to a region where they are less concentrated
74
factors influencing diffusion
- size - temp - steepness of concentration gradient - charge - pressure
75
Passive diffusion
diffusion of a solute through a membrane without transport protein
76
facilitated diffusion
diffusion of a solute through a membrane with the aid of a transport protein
77
passive transport
does not require an input of energy, going down a concentration gradient
78
active transport
requires an input of energy moving against a concentration gradient, primarily using a pump
79
Osmosis
- diffusion of water across a semi permeable membrane | - water diffuses from a region with lower solute concentration to an area with higher solute concentration
80
Endocytosis
process by which materials packaged in vesicles are broken down within the cell
81
exocytosis
Process by which materials packaged in vesicles are secreted from the cell
82
Laws of thermodynamics
1: energy can be transferred and transformed but it cannot be created 2: the total disorder/entropy of the system and its surroundings always increases as the enegy changes (becomes less usable)
83
formula for usable energy
G=H-TS enthalpy (H) free energy (G) entropy (S)
84
if delta G is positive
- free energy is required | - this is the case for anabolic reactions
85
if delta G is negative
- free energy is released | - this is the case for catabolic reactions
86
Exergonic
Product has less free energy than the reactant, spontaneous
87
Enderonic
Product has more free energy than the reactant, requires energy input
88
ATP
- adenosine triphosphate - capture, tranfer and storage of energy - some of the free energy released by exergonic reactions is captured in ATP which then can release free energy to drive endergonic reactions
89
3 Primary ways in which enzymes work
1: orienting substrates, positioning substrates to promote a reaction. 2: inducing strains on substrates 3: adding charges to substrates * *wokr like lock and key**
90
factors affecting enzymes
temp. ph
91
OIL RIG
Oxidation Involves Loss | Reduction Involves Gain
92
Redox Reactions
an electron is removed from one molecule and added to another.
93
overall goal of cellular respiration
to release energy from glucose, and use that energy to make ATP
94
Glycolysis
- 1st metabolic pathway - can happen with or wihtout oxygen, steps nearly identical in all species, breaks down glucose into 2 pruvate - nets 2 ATP - produces 2NADH+H+
95
phases of glycolysis
- phase 1 (steps1-3): energy investment phase invests 2 ATP - phase 2 (steps 4-5): Cleavage phase breaks 6 carbon into 2-3 carbon - phase 3 (steps 6-10): Energy liberation phase broken down into 2 pyruvate
96
breakdown of pyruvate
- broken down by pyruvate dehydrogenaise input: 2 pyruvate, 2 coA, 2 NAD output: 2 acetyl coA, 2 NADH+2H+, 2 co2
97
Alcoholic fermentation
anaerobic pathway that produces ATP and ethyl alcohol
98
Lactate fermentation
Anaerobic pathway that produces ATP and lactate
99
Respiration vs Fermentation
When o2 is not available molecules are unable to make ATP using o2 has final electron acceptor, therfore fermentation allows molecules to produce ATP but much less
100
Whats is the purpose of cell signalling
- respond to a changing environment | - cell to cell communication
101
Direct intercellular signaling
signal passes through a cell junction from the cytosol of one cell to adjacent cells
102
contact dependent signaling
membrane bound signals bind to receptors on adjacent cells
103
Autocrine signaling
cells release signals that affect themselves and nearby target cells
104
Paracrine signaling
cells release signals that affect nearby target cells
105
Endocrine signaling
Cells release signals that travel long distances to reach target cells
106
stages of cell signaling
- receptor activation - signal transduction - cellular response
107
receptor activation
ligand binds to receptor with high degree of specificity. Causes a conformational change that activates the receptor. Once ligand is released receptor is no longer activated.
108
signal transduction
signaling molecule binds to cell surface receptor, usually stimulates signal transduction pathways that lead to a cellular response.
109
Cellular Response
Alter the activity of 1 or more enzymes. Alter structural protein function, change gene expression
110
second messengers
- relay signals inside cells | - EXAMPLES: cAMP, Ca2+
111
2 advantages of cAMP
- signal amplification | - speed
112
protein kinase
enzyme that modifies other proteins by phosphorylation. This phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location or association with other proteins
113
anchoring junctions
attach cells to ECM and each other
114
4 types of animal tissue
- epithelial - connective - nervous - muscle
115
collagen
structural protein that provides tensile strength (bone, cartilage, tendon, skin)
116
elastin
structural protein that provides elasticity, expands and returns to original shape. (lungs, blood vessels)
117
Griffith
used bacteria to form a transformation principle
118
Hershey & Chase
performed experimen using E.coli, result supported that DNA was the genetic material
119
3 components of DNA structure
1: phosphate group 2: penstose sugar 3: nitrogenous bases
120
Levels of DNA structure
- nucleotides - form a strand - double helix - chromosomes - Genome
121
DNA replication
1. hydrogen bonds between the two strands are broken | 2. new nucleotides covelently bonded to each growing strand via DNA polymerase
122
DNA polymerase
-primary replication enzyme that binds to template strand
123
leading strand
DNA strand that is in the correct orientation given DNA's anitparallel nature
124
lagging strand
DNA strand that is in the wrong orientation given DNA's antiparallel nature. During replication, lagging strand must grow small discontinuous pieces known as okazaki fragments
125
Telomerase
enzyme that attaches many copies of DNA repeat sequence to the ends of chromosomes, function reduced as organism ages. -99% of all type of human cancers have high levels of telomerase
126
Central Dogma
DNA undergoes transcription to form RNA, then RNA undergoes translation to form protein.
127
3 stages of prokaryotic transcription
- intiation - elongation - termination
128
What happens in the initiation stage of transcription
- signal factor causes RNA polymerase I to recognize promoter region - stage complete when DNA strands separated near promoter to form open complex
129
What happens in the elongation stage of transcription
- RNA polymerase synthesizes RNA - template or coding strand use for RNA synthesis - synthesized 5'-3' - Uracil substituted for thymine
130
what happens in the termination stage of transcription
- RNA polymerase reaches termination sequence | - causes it and newly made RNA transcript to dissociate from DNA
131
splicing (RNA processing)
-most genes have one or more introns, spliceosomes remove introns precisely
132
codons
- sequence of 3 bases in an mRNA molecule - read in groups of 3 - most specify a particular amino acid, also start and stop codons - degenerate - start codon (AUG) defines reading frame, stop codon ends it.
133
tRNA
- cloverleaf structure - amino acid binding - basically carries amino acids and adds them to the growing protein structure
134
Ribosomes (RNA processing)
- receive amino acids from tRNA and assemble the protein.
135
Why must genes be regulated
- environmental response - cellular differentiation - organismal development
136
repressors
inhibit transcription
137
activators
increase the rate of transcription
138
lac operon
cluster of genes under transcriptional control that contains genes for lactose metabolism
139
Negative control of lac operon (lactose absent)
- lac repressor binds to lac operator site preventing transcription - RNA polymerase can bind but not move
140
Negative control of lac operon (lactose present)
- 4 allolactose molecules bind to repressor and prevent repressor from binding - process called induction
141
point mutation
- base substituition | - add or remove a single base pair
142
silent mutation
-causes no change
143
missense mutation
-changes a single amino acid in a polypeptide -may not alter function if substituted amino acid is similar in chemistry to original EXAMPLE:sickle cell
144
nonsense mutation
- changes from a normal codon to a stop codon | - produces a truncated polypeptide
145
frameshift mutation
- addition or deletion of nucleotides (excluding multiples of 3) - completely different amino acid sequence downstream from mutation
146
germ-line mutation
- gives rise to gametes | - mutation can occur in sperm or egg cell, or in gamete progenitor cells
147
somatic mutation
- all other body cell besides gametes - can occur early or late in development - give a genetic mosaic with patches of mutant tissue
148
Nucleotide Excision Repair
- damaged DNA is removed - Undamaged strand used for synthesis of complementary strand - found in all eukaryotes and prokaryotes
149
oncogenes
- caused by mutation in genes for cell growth signaling proteins - promote cancer by keeping the cell division pathway in permanent "on" position
150
what types of mutations have been known to lead to cancer
- missense mutations - gene amplifications - chromosomal translocations - retroviral insertions
151
gene amplifications
-increase in copy number results in too much protein
152
chromosomal translocations
- two chromosomes break and switch ends | - can create chimeric genes
153
retroviral insertions
-viral DNA inserts into a chromosome putting a viral promoter right next to a proto-oncogene
154
tumor suppressor genes
normal role is to prevent cancer growth
155
checkpoint proteins
-check the integrity of the genome and prevent a cell from progressing past a certain point in the cycle
156
Cell Cycle
- g1 - s - g2 - mitosis and cytokinsesis
157
what 3 stages make up interphase
- g1 - s - g2
158
G1 phase
the first interval or gap of cell growth, the time before DNA replication when cells engage in their metabolic business
159
S phase
the time of synthesis (DNA replication) when the cell prepares to divide
160
G2 phase
second interval or group when the cell makes proteins that will drive cell division
161
Phases of mitosis
prophase metaphase anaphase telophase
162
prophase
- nuclear membrane disappears, centrosomes migrate, spindle fibers appear - DNA coils into chromosomes
163
metaphase
-chromosomes line up in middle at metaphase plate
164
anaphase
-centromeres divide, sister chromatids migrate to opposite poles, cytokinesis begins
165
telophase
-nuclear membranes form, spindle disappears, cytokinesis occurs
166
homologous chromosomes
chromosomes with the same length, shape, and set of genes. Each individual receives one from their mother and one from their father.
167
Dominant trait
trait that will be expressed
168
recessive trait
trait that will be masked by dominant trait
169
allele
alternate form of a gene
170
Law of segregation
states that alleles separate during gamete formation
171
Law of independent assortment
alleles of different genes assort into gametes independently of each other. all possible combinations of factors can occur **seperate genes for separate traits are passed independently of one another from parents to offspring **
172
polygenic inheritance
a situation in which interaction of several gene pairs guides the development of a specific characteristic such as height, skin color and eyesight
173
sex determination
determined by specific pair of chromosomes called the sex chromosomes Males:XY Females: XX
174
codominance
situation in which two different alleles for a genetic trait are both expressed
175
formula for allele frequency
allele frequency=# of copies of a specific allele in a population/ total # of all alleles for that gene in a population
176
formula for genotype frequency
genotype frequency=# of individuals with a particular genotype in a population/ total # of individuals in a population
177
what is the purpose of the hardy weinberg principle
- shows the relationship between allele and genotype frequencies when a population is not evolving - its a theoretical reference point, genetic equilibrium occurs when the allele frequencies of a population do not change
178
what five conditions are required by the hardy weinberg principle
- random mating - large population size - no mutations - no immigration or emigration - no selection
179
stabilizing selection
intermediate phenotype is favored, selection against extreme phenotypes, stable environment
180
directional selection
one extreme phenotype is favored, adjusting to a changing environment
181
disruptive selection
two or more extreme phenotypes are selected
182
sexual selection
one sex prefers to mate with individuals of the opposite sex that have specific characteristics. These characteristics imply increased fitness