Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biology I > Final Review > Flashcards

Final Review Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
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
Q

Acids

A

dissolve in water and release hydrogen ions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

strong acids

A

almost completely dissociate HCL into H_ and cl-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

weak acids

A

some of the acid does not dissociate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Bases

A

accept H+ in solutions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Isomers

A

Identical molecular formulas but different structures and characteristics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Structural Isomers

A

Contain the same atoms but in different bonding relationships

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Cis-trans Isomers

A

contain the same atoms in different positions around double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

enantiomers

A

type of stereoisomer in which the molecules are mirror opposites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

dehydration reaction

A

forms macromolecules by removing H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

hydrolysis reaction

A

breaks polymers back down into monomers hy adding H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

4 categories of carbs

A
  • monosacharrides
  • disaccharides
  • oligosaccharides
  • polysaccharides
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

monosaccharides

A
  • simplest form of carbohydrate

- usually 5(pentose) or 6 carbon(hexose)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

glucose

A

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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

disaccharides

A

2 monosaccharides joined together by a dehydration reactin that forms what is called a glycosidic bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

polysaccharides

A
  • giant polymers connected by glycosidic linkages
  • sometimes used to store energy
  • some provide structural roles (chitin)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Lipids

A

hydrophobic molecules composed mainly of hydrogen and carbon atoms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

triglycerides “fats”

A

formed by bonding glycerol to 3 fatty acids. Important for storing energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

Steroids

A
  • four interconnected rings of carbon atoms
  • not very water soluble
  • hormones and vitamins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

waxes

A

provide a barrier to water loss

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

saturated fats

A

when all carbons in a fatty acid contain covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

unsaturated fats

A

contain double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Primary protein structure

A
  • amino acid sequence

- determined by genes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

secondary protein structure

A
  • folding in repeating patterns

- either alpha helix or beta pleated sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

tertiary protein structure

A

folding gives complex three dimensional shape

  • caused by interaction of side chains
  • random coils
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

quarternary protein structure

A
  • made up of 2 or more polypeptides

- multimeric proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

purines

A
  • adenine

- guanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

pyrimidines

A
  • thymine
  • cytosine
  • uracil
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

volume

A

determines the amount of chemical activity in a cell per unit volume

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

surface area

A

determines the amount of substances that can pass the cell boundary per unit time

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Cytosol

A

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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Cytoskeleton

A

structure: network of three different types of protein filaments, actin, intermediate, and microtubules
function: shape & support, movement, tracks for “motor proteins”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Nucleus

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Ribosomes

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

Rough ER

A

studded with ribosomes. sorts and folds, inserts proteins into ER membrane, glycosylation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

Smooth ER

A

Lacks ribosomes, continuous with rough ER, function depends on cell type. detoxification, crb metabolism, calcium balance, synthesis and modification of lipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

Golgi Apparatus

A

structure: stack of 3-23 saccules, vesicles transport materials between stacks
function: sorting, processing, secretion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

Lysosomes

A

specialized vesicles, phagocytosis, autophagy, destroy invaders, apoptosis, uses hydrolytic enzymes to break things down

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

Vacuoles

A

varied functions, central vauoles in plants, contractile vacuoles in plants, phagocytic vacuoles in white blood cells, store wastes and toxic compounds, store antocyanins (pigment)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

Peroxisomes

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

Plasma Membrane

A

structure: boundary between cell and extracellular environment.
function: membrane transport, cell signalling, cell adhesion, homeostasis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

Mitochondria

A

structure: outer and inner membrane, intermembrane space, mitochondrial matrix, contain there own DNA
function: make ATP, divide by binary fission

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

Chloroplasts

A

photosynthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

cell membrane

A
  • bilayered dynamic structure
  • forms boundaries between cells
  • regulates movement of molecules into and out of cells
  • made up of phospholipids, proteins & carbs
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

Membrane Lipid

A
  • framework is the phospholipid bilayer
  • phospholipids are ampipathic molecules
  • hydrophobic region faces in
  • hydrophilic region faces out
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

Cholesterol

A
  • only found in animal cells
  • stabilizes membranes at high temps
  • makes more fluids at lower temps
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

integral membrane proteins

A
  • intrinsic
  • transmembrane proteins
  • lipid-anchored proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

peripheral membrane proteins

A

-extrinsic
-bound to regions of integral membrane proteins that project out from the membrane
or bound to polar head groups of phospholipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

membrane carbs

A
  • glycosylation
  • recognition signals for other cellular proteins
  • cell surface recognition
  • protective effects
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

diffusion

A

net movement of molecules or ions from a region where they are more concentrated to a region where they are less concentrated

74
Q

factors influencing diffusion

A
  • size
  • temp
  • steepness of concentration gradient
  • charge
  • pressure
75
Q

Passive diffusion

A

diffusion of a solute through a membrane without transport protein

76
Q

facilitated diffusion

A

diffusion of a solute through a membrane with the aid of a transport protein

77
Q

passive transport

A

does not require an input of energy, going down a concentration gradient

78
Q

active transport

A

requires an input of energy moving against a concentration gradient, primarily using a pump

79
Q

Osmosis

A
  • 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
Q

Endocytosis

A

process by which materials packaged in vesicles are broken down within the cell

81
Q

exocytosis

A

Process by which materials packaged in vesicles are secreted from the cell

82
Q

Laws of thermodynamics

A

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
Q

formula for usable energy

A

G=H-TS
enthalpy (H)
free energy (G)
entropy (S)

84
Q

if delta G is positive

A
  • free energy is required

- this is the case for anabolic reactions

85
Q

if delta G is negative

A
  • free energy is released

- this is the case for catabolic reactions

86
Q

Exergonic

A

Product has less free energy than the reactant, spontaneous

87
Q

Enderonic

A

Product has more free energy than the reactant, requires energy input

88
Q

ATP

A
  • 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
Q

3 Primary ways in which enzymes work

A

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
Q

factors affecting enzymes

A

temp. ph

91
Q

OIL RIG

A

Oxidation Involves Loss

Reduction Involves Gain

92
Q

Redox Reactions

A

an electron is removed from one molecule and added to another.

93
Q

overall goal of cellular respiration

A

to release energy from glucose, and use that energy to make ATP

94
Q

Glycolysis

A
  • 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
Q

phases of glycolysis

A
  • 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
Q

breakdown of pyruvate

A
  • broken down by pyruvate dehydrogenaise
    input: 2 pyruvate, 2 coA, 2 NAD
    output: 2 acetyl coA, 2 NADH+2H+, 2 co2
97
Q

Alcoholic fermentation

A

anaerobic pathway that produces ATP and ethyl alcohol

98
Q

Lactate fermentation

A

Anaerobic pathway that produces ATP and lactate

99
Q

Respiration vs Fermentation

A

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
Q

Whats is the purpose of cell signalling

A
  • respond to a changing environment

- cell to cell communication

101
Q

Direct intercellular signaling

A

signal passes through a cell junction from the cytosol of one cell to adjacent cells

102
Q

contact dependent signaling

A

membrane bound signals bind to receptors on adjacent cells

103
Q

Autocrine signaling

A

cells release signals that affect themselves and nearby target cells

104
Q

Paracrine signaling

A

cells release signals that affect nearby target cells

105
Q

Endocrine signaling

A

Cells release signals that travel long distances to reach target cells

106
Q

stages of cell signaling

A
  • receptor activation
  • signal transduction
  • cellular response
107
Q

receptor activation

A

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
Q

signal transduction

A

signaling molecule binds to cell surface receptor, usually stimulates signal transduction pathways that lead to a cellular response.

109
Q

Cellular Response

A

Alter the activity of 1 or more enzymes. Alter structural protein function, change gene expression

110
Q

second messengers

A
  • relay signals inside cells

- EXAMPLES: cAMP, Ca2+

111
Q

2 advantages of cAMP

A
  • signal amplification

- speed

112
Q

protein kinase

A

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
Q

anchoring junctions

A

attach cells to ECM and each other

114
Q

4 types of animal tissue

A
  • epithelial
  • connective
  • nervous
  • muscle
115
Q

collagen

A

structural protein that provides tensile strength (bone, cartilage, tendon, skin)

116
Q

elastin

A

structural protein that provides elasticity, expands and returns to original shape. (lungs, blood vessels)

117
Q

Griffith

A

used bacteria to form a transformation principle

118
Q

Hershey & Chase

A

performed experimen using E.coli, result supported that DNA was the genetic material

119
Q

3 components of DNA structure

A

1: phosphate group
2: penstose sugar
3: nitrogenous bases

120
Q

Levels of DNA structure

A
  • nucleotides
  • form a strand
  • double helix
  • chromosomes
  • Genome
121
Q

DNA replication

A
  1. hydrogen bonds between the two strands are broken

2. new nucleotides covelently bonded to each growing strand via DNA polymerase

122
Q

DNA polymerase

A

-primary replication enzyme that binds to template strand

123
Q

leading strand

A

DNA strand that is in the correct orientation given DNA’s anitparallel nature

124
Q

lagging strand

A

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
Q

Telomerase

A

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
Q

Central Dogma

A

DNA undergoes transcription to form RNA, then RNA undergoes translation to form protein.

127
Q

3 stages of prokaryotic transcription

A
  • intiation
  • elongation
  • termination
128
Q

What happens in the initiation stage of transcription

A
  • signal factor causes RNA polymerase I to recognize promoter region
  • stage complete when DNA strands separated near promoter to form open complex
129
Q

What happens in the elongation stage of transcription

A
  • RNA polymerase synthesizes RNA
  • template or coding strand use for RNA synthesis
  • synthesized 5’-3’
  • Uracil substituted for thymine
130
Q

what happens in the termination stage of transcription

A
  • RNA polymerase reaches termination sequence

- causes it and newly made RNA transcript to dissociate from DNA

131
Q

splicing (RNA processing)

A

-most genes have one or more introns, spliceosomes remove introns precisely

132
Q

codons

A
  • 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
Q

tRNA

A
  • cloverleaf structure
  • amino acid binding
  • basically carries amino acids and adds them to the growing protein structure
134
Q

Ribosomes (RNA processing)

A
  • receive amino acids from tRNA and assemble the protein.
135
Q

Why must genes be regulated

A
  • environmental response
  • cellular differentiation
  • organismal development
136
Q

repressors

A

inhibit transcription

137
Q

activators

A

increase the rate of transcription

138
Q

lac operon

A

cluster of genes under transcriptional control that contains genes for lactose metabolism

139
Q

Negative control of lac operon (lactose absent)

A
  • lac repressor binds to lac operator site preventing transcription
  • RNA polymerase can bind but not move
140
Q

Negative control of lac operon (lactose present)

A
  • 4 allolactose molecules bind to repressor and prevent repressor from binding
  • process called induction
141
Q

point mutation

A
  • base substituition

- add or remove a single base pair

142
Q

silent mutation

A

-causes no change

143
Q

missense mutation

A

-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
Q

nonsense mutation

A
  • changes from a normal codon to a stop codon

- produces a truncated polypeptide

145
Q

frameshift mutation

A
  • addition or deletion of nucleotides (excluding multiples of 3)
  • completely different amino acid sequence downstream from mutation
146
Q

germ-line mutation

A
  • gives rise to gametes

- mutation can occur in sperm or egg cell, or in gamete progenitor cells

147
Q

somatic mutation

A
  • all other body cell besides gametes
  • can occur early or late in development
  • give a genetic mosaic with patches of mutant tissue
148
Q

Nucleotide Excision Repair

A
  • damaged DNA is removed
  • Undamaged strand used for synthesis of complementary strand
  • found in all eukaryotes and prokaryotes
149
Q

oncogenes

A
  • caused by mutation in genes for cell growth signaling proteins
  • promote cancer by keeping the cell division pathway in permanent “on” position
150
Q

what types of mutations have been known to lead to cancer

A
  • missense mutations
  • gene amplifications
  • chromosomal translocations
  • retroviral insertions
151
Q

gene amplifications

A

-increase in copy number results in too much protein

152
Q

chromosomal translocations

A
  • two chromosomes break and switch ends

- can create chimeric genes

153
Q

retroviral insertions

A

-viral DNA inserts into a chromosome putting a viral promoter right next to a proto-oncogene

154
Q

tumor suppressor genes

A

normal role is to prevent cancer growth

155
Q

checkpoint proteins

A

-check the integrity of the genome and prevent a cell from progressing past a certain point in the cycle

156
Q

Cell Cycle

A
  • g1
  • s
  • g2
  • mitosis and cytokinsesis
157
Q

what 3 stages make up interphase

A
  • g1
  • s
  • g2
158
Q

G1 phase

A

the first interval or gap of cell growth, the time before DNA replication when cells engage in their metabolic business

159
Q

S phase

A

the time of synthesis (DNA replication) when the cell prepares to divide

160
Q

G2 phase

A

second interval or group when the cell makes proteins that will drive cell division

161
Q

Phases of mitosis

A

prophase
metaphase
anaphase
telophase

162
Q

prophase

A
  • nuclear membrane disappears, centrosomes migrate, spindle fibers appear
  • DNA coils into chromosomes
163
Q

metaphase

A

-chromosomes line up in middle at metaphase plate

164
Q

anaphase

A

-centromeres divide, sister chromatids migrate to opposite poles, cytokinesis begins

165
Q

telophase

A

-nuclear membranes form, spindle disappears, cytokinesis occurs

166
Q

homologous chromosomes

A

chromosomes with the same length, shape, and set of genes. Each individual receives one from their mother and one from their father.

167
Q

Dominant trait

A

trait that will be expressed

168
Q

recessive trait

A

trait that will be masked by dominant trait

169
Q

allele

A

alternate form of a gene

170
Q

Law of segregation

A

states that alleles separate during gamete formation

171
Q

Law of independent assortment

A

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
Q

polygenic inheritance

A

a situation in which interaction of several gene pairs guides the development of a specific characteristic such as height, skin color and eyesight

173
Q

sex determination

A

determined by specific pair of chromosomes called the sex chromosomes
Males:XY
Females: XX

174
Q

codominance

A

situation in which two different alleles for a genetic trait are both expressed

175
Q

formula for allele frequency

A

allele frequency=# of copies of a specific allele in a population/ total # of all alleles for that gene in a population

176
Q

formula for genotype frequency

A

genotype frequency=# of individuals with a particular genotype in a population/ total # of individuals in a population

177
Q

what is the purpose of the hardy weinberg principle

A
  • 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
Q

what five conditions are required by the hardy weinberg principle

A
  • random mating
  • large population size
  • no mutations
  • no immigration or emigration
  • no selection
179
Q

stabilizing selection

A

intermediate phenotype is favored, selection against extreme phenotypes, stable environment

180
Q

directional selection

A

one extreme phenotype is favored, adjusting to a changing environment

181
Q

disruptive selection

A

two or more extreme phenotypes are selected

182
Q

sexual selection

A

one sex prefers to mate with individuals of the opposite sex that have specific characteristics. These characteristics imply increased fitness

Biology I (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions