Bio Exam 3

Front 1

What is the most common way to examine gene functions? Who discovered this way?

Back 1

Using loss of function alleles, or knock out alleles that are defective and don't work. Beadle and Tatum

Front 2

One gene, One Enzyme hypothesis

Back 2

Claimed that each gene contains the information needed to make an enzyme

Front 3

Metabolic Pathway

Back 3

The steps that organisms synthesize arginine

Front 4

How did Horowitz and Srb test the one gene one enzyme hypothesis?

Back 4

They used radiation to create a large number of mutant cells and used a genetic screen to find out the specific gene that knocked out a step in the pathway and documented a correlation between specific genetic defects and defects at a specific point in a metabolic pathway

Front 5

Genetic Screen

Back 5

Any technique for picking certain types of mutant out of many randomly generated mutants

Front 6

What do genes do?

Back 6

Contain instructions for making proteins

Front 7

The Genetic Code Hypothesis

Back 7

Cricks proposal that different combinations of different bases could specify the 20 amino acids, just as different combinations of dots and dashes specify the 26 letters of the alphabet

Front 8

Messenger RNA

Back 8

Short lived RNA molecules that act as carriers for genetic information out of the nucleus from the DNA to the site of protein synthesis

Front 9

RNA Polymerase and how does it function?

Back 9

Polymerizes ribonucleotides into strands of RNA and does this according to the information provided by the sequence of bases in a particular stretch of RNA

Front 10

The central dogma

Back 10

Summarizes the flow of information in cells, so genes basically code for protiens

Front 11

Transcription

Back 11

Process of copying hereditary information in DNA to RNA

Front 12

Translation

Back 12

The process of using the information in nucleic acids to synthesize proteins

Front 13

Phenotype

Back 13

Physical traits that are the result of the proteins produced by the sequence of bases

Front 14

Genotype

Back 14

determined by the sequence of bases in DNA

Front 15

Reverse Transcriptase

Back 15

A specialized viral polymerase synthesizes a DNA version of RNA genes. Therefore, the information flows from RNA back to DNA. That is "reverse" from the way that DNA flows into RNA according to the central dogma

Front 16

Genetic Code

Back 16

The rules that specify the relationship between a sequence of nucleotides in DNA or RNA and the sequence of Amino Acids in a protein.

Front 17

Who came up with the Triplet Code Hypothesis? What is the Triplet Code and how many bases different amino acids can it represent?

Back 17

George Gamow came up with the hypothesis of the Three base code for an amino acid, allowing for 64 different amino acid to be represented in the sequence.

Front 18

Codon

Back 18

Three base code that specifies a particular amino acid

Front 19

Reading Frame

Back 19

Sequence of codons

Front 20

Start Codon

Back 20

Signalsthat protein synthesis should begin at that point on the mRNA molecule.Thestart codon specifies the amino acid methionine

Front 21

Stop Codon

Back 21

Called termination codons, signal that the protein iscomplete, they do not code for any amino acid, and they end translation.

Front 22

What are the different properties of the genetic code?

Back 22

The code is redundant- Amino acids are coded by more than one codon

The code is unambiguous- a single codon only codes for one protein

The code is non overlapping- once the ribosome locks onto a codon, it reads each separate codon after that

The code is nearly universal- All codons specify the same amino acids in all organisms

The code is conservative- When two codons specify the same amino acid, the first two bases are almost always identical.

Front 23

Nirenberg and Leder

Back 23

They devised a system for synthesizing specific codon, and were able to determine which of the 64 codons coded for each of the 20 amino acids

Front 24

Mutation

Back 24

Any permanent changes in an organisms DNA , or a modification to the cells information archive causing a change in its genotype. Mutations create new alleles.

Front 25

Whatdoes having the code be conservative serve to do in an organism?

Back 25

Ifa DNA error occurs during translation, having the only the third codon affectedit is less likely to change the amino acids in the final protein.

Front 26

Whatare the two things that biologists can predict and determine using the geneticcode?-

Back 26

Predict the codons and amino acid sequence encoded by aparticular DNA sequence. Determine the set of mRNA and DNA sequences that wouldcode for a specific set of amino acids.

Front 27

Alleles

Back 27

One or more form of a gene caused by mutations and are found at the same place as a chromosome

Front 28

Point Mutation

Back 28

A mistake during DNA synthesis that results in a mutation in which a single based is changed

Front 29

Missense Mutation

Back 29

A Point mutation that causes a change the amino acid sequence of a protein

Front 30

Silent Mutation

Back 30

A point mutation in which the change of the single base does not affect the sequence of amino acids

Front 31

Frame-shift Mutation

Back 31

A point mutation in which the deletion or addition of a single base causes the whole amino acid sequence to be thrown off and alters the meaning of all subsequent codons.

Front 32

What are the three categories that biologists divide mutations into?

Back 32

Beneficial, nuetral, and deleterious.

Beneficial- Any mutation that increases the fitness of an organism.

Nuetral- any mutation that doesn't have an affect on the fitness of an organism.

Deleterious- any mutation that lowers the fitness of an organism.

Front 33

what are the four different types of chromosome mutations?

Back 33

Inversion, Translocation, Deletion, Duplication

Front 34

Inversion

Back 34

A chromosomal mutation in which the segments of a chromosome may be flipped and rejoined

Front 35

Translocation

Back 35

A chromosomal mutation in which a segment of a chromosome becomes attached to another chromosome

Front 36

Deletion

Back 36

A chromosomal mutation in which a segment of a chromosome is lost

Front 37

Duplication

Back 37

A chromosomal mutation in which additional copies of a segment are present

Front 38

aneuploidy

Back 38

Addition or deletion of individual chromosomes

Front 39

Polyploidy

Back 39

The addition in the number of chromosomes

Front 40

Transcription

Back 40

The conversion of genetic information from DNA to RNA specifically mRNA

Front 41

Beadle and Tatum proposed the one-gene, one-enzyme hypothesis based on __________.

Back 41

Knock out mutants that lacked the ability to synthesize certain compounds

Front 42

Knock Out Allele

Back 42

A gene altered so that it no longer produces intended proteins

Front 43

Describe the genetic screen done by Srb and Horowitz to determine the metabolic pathway for arginine synthesis.

Back 43

The key design in their study was that they found three different mutants and raised them with different intermediates in the arginine pathway. This allowed them to demonstrate that each mutant (or gene) was responsible for a particular enzyme along the pathwa

They irradiated N. crassa cells, grew all the mutants on arginine, and then grew each mutant on medium containing a different intermediate in the arginine pathway.Basically they wanted to see if an individual cell could grow in the presence of arginine but failed without the arginine, then that meant that the individual could not make its own arginine

Front 44

What is the function of mRNA?

Back 44

To carry information from DNA out of the nucleus to the site of protein synthesis

Front 45

What required the rethinking of the central dogma theory?

Back 45

The discovery of retroviruses and their mechanism of replication required scientists to rethink the central dogma of molecular biology. Based on this information, RNA → DNA → RNA → protein represents an appropriate adjustment to the central dogma.

Front 46

Which enzyme allows RNA to be coded into DNA?

Back 46

Reverse Transcriptase

Front 47

What is an exception to the central dogma of molecular biology?

Back 47

Single stranded RNA from a virus is used as a template for producing DNA that inserts into the host genome. This uses reverse transcriptase to synthesize the DNA to RNA

Front 48

HIV virus is an example of a virus that uses what polymerase?

Back 48

Reverse transcriptase. Several prescribed drugs for AIDs patients fight the infection by poisoning the HIV reverse transcriptase.

Front 49

How many amino acids are represented in the genetic code by just one codon?

Back 49

2- Tryptophan and Methionine

Front 50

Nonsense Mutation

Back 50

A point Mutation that causes an early termination of protein synthesis because the change causes the sequence for a stop codon.

Front 51

How many types of RNA polymerase do Eukaryotic cells have?

Back 51

3

Front 52

What is RNA Polymerase, does it need a primer?

Back 52

It is the enzyme that is responsible for synthesizing mRNA from the template strand, and there is no primer needed, unlike DNA polymerase

Front 53

Template Strand

Back 53

The Strand that is read by the enzymes.

Front 54

Coding Strand

Back 54

The strand that is not the template strand, whose sequence matches that of the RNA that is transcribed from the template strand to code for the polypeptide

Front 55

Bacteria have how many versions of RNA polymerase?

Back 55

1

Front 56

What base does RNA have that differs from that of DNA

Back 56

Uracil

Front 57

Whatdirection does RNA polymerase perform template directed synthesis?

Back 57

Always in the 5' to 3' direction

Front 58

What is the initiation phase in bacteria, and it involves what enzyme and group of proteins?

Back 58

A stage in transcription in which the RNA polymerase ishelped by a protein that signals where to start transcription.

Front 59

Sigma

Back 59

Promoter recognizing protein subunit of bacterial RNA polymerase holoenzyme

Front 60

Whatdoes the Bacterial RNA polymerase and Sigma form?

Back 60

Holoenzyme

Front 61

What does a holoenzyme consist of?

Back 61

A core enzyme ( RNA polymerase) which contains the activesite for analysis, and then a group of proteins (sigma)

Front 62

When does transcription begin in bacteria? What makes initial contact with the promotor?

Back 62

When sigma binds to the -35 and -10 boxes.This will determine in which direction the RNA polymerase will start synthesize RNA

Front 63

What happens after the holoenzyme is bound to the promotor?

Back 63

The DNA helix is opened by RNA polymerase, creating two separate strands of DNA

Front 64

Elongation phase of transcription- When does it begin and what is it?

Back 64

It is the phase that begins once the RNA polymerase begins moving along the DNA template synthesizing RNA

Front 65

Termination phase of transcription

Back 65

In bacteria, transcription stops when RNA polymerase transcribes a DNA sequence that functions as a transcription-termination signal

Front 66

RNA polymerase II

Back 66

The only polymerase that transcribes protein-encoding genes

Front 67

TATA Box

Back 67

Eukaryotic promotor sequence centered about 30 base pairs upstream of the transcription start site.

Front 68

Basil Transcription Factors

Back 68

The protein used instead of sigma in order for RNA polymerase to recognize promoters

Front 69

How is eukaryotic transcription terminated?

Back 69

Using a short sequence called a poly signal. Soon after the signal is transcribes, the RNA is cut down by an enzyme downstream of the poly signal.

Front 70

Primary Transcript

Back 70

The initial product of transcription. The RNA needs to undergo multistep processing before it is functional

Front 71

What did Sharp and Roberts discover?

Back 71

The presence of introns-sections of genes that are not expressed in the final RNA product.

Front 72

What is Splicing? What protein is involved?

Back 72

The process in which the introns within the growing RNA strand are removed.The splicing of introns is catalyzed by RNA's called small nuclear RNA's (nRNA) and works with a complex of proteins called small nuclearribonucleoprotiens (snRNP's).

Front 73

Describe the process of Splicing RNA within the nucleus

Back 73

1. snRNPs bind to the start of intron and an A base within the intron

2.snRNP's assemble to form a splicosome ( a complex group of proteins

3.Intron forms a loop

4 The loop is cut, and phosphodiester linkages links the exons on either side, producing a continuous coding sequence- the mRNA

Front 74

What is the step after splicing to complete RNA processing in eukaryotes? How do they help?

Back 74

Adding caps and tails.

They help to protect from degradation along with enhancing the efficiency of translation.

Front 75

Which end are caps added to, and what are they?

Back 75

The caps are added to the 5' end of the pre-mRNA emerges from the RNA polymerase by enzymes, and are composed of a modified guanine nucleotides

Front 76

Which end are poly(A) tails added to, and what are they?

Back 76

To being, an enzyme cleaves the 3' end of the pre-mRNA, then another enzyme adds a long row of 100-250 adenine nucleotides downstream of the poly signal.

Front 77

How do the untranslated region help the mRNA?

Back 77

The regions help stabilize the mature RNA and regulate its translation.

Front 78

Translation

Back 78

The translation of RNA molecules into a sequence of amino acids in a polypeptide.

Front 79

Where does protein synthesis occur?

Back 79

They are synthesized at the ribosome and then released

Front 80

Why do transcription and translation occur concurrently in bacteria?

Back 80

Because there is no nuclear envelope to separate the two processes

Front 81

Describe translation in Bacteria.

Back 81

Ribosomes attach to mRNA's and begin synthesizing proteins even before transcription is complete. Multiple ribosomes attach to each mRNA forming polyribosomes,

Front 82

Describe Translation in Eukaryotes.

Back 82

The mature mRNA is exported to the cytoplasm. This means that translation and transcription occur separately in time and space. As in bacteria, polyribosomes form. When mRNA interacts with a ribosome, instructions encoded in nucleic acids are translated into a different chemical language- the amino acid sequences found in proteins. Transfer RNA transfers the amino acids from the RNA to a growing polypeptide.

Front 83

Anticodon

Back 83

A set of three nucleotides that forms base pairs with the mRNA codon

Front 84

What is universal of the structure of tRNAs?How do they differ?

Back 84

They are shaped like an upsidedown "L". They vary at the anticodon and attached amino acid.

Front 85

How are amino acids attached to RNA's?

Back 85

Enzymes called ammoniacal-tRNA syntheses catalyze the addition of amino acids to tRNA's. Each enzyme has a binding sight for a particular amino acid and a particular tRNA.

Front 86

aminoacyl-tRNA

Back 86

The combination of a tRNA molecule covalently linked to an amino acid.

Front 87

Wobble Hypothesis

Back 87

the hypothesis that states that non standard base pairs like G U are acceptable in the third position of a codon and do not change the amino acid that the codon specifies.

Front 88

Ribosomes, and the three step protein synthesis process.

Back 88

Ribosome is a macromolecular machine that synthesizes protein as follows:

1)An ammoniacal tRNA diffuses into the A site; if its anticodon matches a codon on mRNA , it stays in the ribosome.

2.)A peptide bond forms between the amino acid held by the ammoniacal tRNA in the A site and the growing polypeptide, which was held by tRNA in the P site.

3) The ribosome moves down the mRNA by one codon, and all three tRNA's move one position within the ribosome. The tRNA in the E site exits; the tRNA in the P site moves to the E, and the tRNA in the A site switches to the P site.

Front 89

N terminus and C terminus

Back 89

The N terminus is the amino end of a polypeptide, and the C terminus is the carbozyl end of the polypeptide

Front 90

How is translation initiated?

Back 90

1)The mRNA binds to a small ribosomal subunit

2)the initiator ammoniacal tRNA binds to the start codon

3)The large ribosomal subunit binds, completing the complex

Front 91

When is the invitation phase of translation complete?

Back 91

When the large subunit joins the complex

Front 92

Initiation Factors

Back 92

Proteins that mediate the interactions between the small sub unit of the ribosome, the mRNA and the tRNA. They help prepare the ribosome for translation and bind the first aminoacyl tRNA

Front 93

Elongation Phase of Translation

Back 93

The phase in which the polypeptide is extended.

Front 94

What are the three sites of the large subunit of the ribosome? Which performs which action?

Back 94

The A site, the P site, and the E site.

A site- Active Site Accepts the new tRNA's where its anticodon base pairs with the mRNA codon

P Site-Peptide bonds form

E site- Exit Site

Front 95

Describe the process of elongation

Back 95

tRNA anticodon pairs with mRNA codon

Peptide Bond Forms

The polypeptide chain moves one codon down the mRNA

Front 96

What catalyzes the formation of peptide bonds on the active site during translation?

Back 96

RNA

Front 97

Translocation

Back 97

The process in which thee polypeptide chain is transferred from the tRNA in the P site to the amino acid held by the tRNA in the A site. This opens up the A site, and the tRNA found in the E site is ejected into the cytosol. This is made possible by elongation factors.

Front 98

How is translation terminated?

Back 98

When the translocating ribosome reaches one of the stop codons, a protein called a release factor recognizes the stop codon and fills the A site.

Front 99

Post translational Modifications

Back 99

This includes the step requires before a protein is functional. This include the folding- which is speeded up by proteins called molecular chaperones, and chemical modifications like phosphorylations, or the addition of sugar or lipid groups.

Front 100

TATA Box

Back 100

Eukaryotic promoter sequence centered about 30 base pairs upstream of the transcription start site.

Front 101

What are Amino Acids and what is their common structure?

Back 101

The building blocks of proteins- there are twenty.

The structure consists of:

1.H- a hydrogen atom

2. NH2- Amino acid functional group

3.COOH-A carboxyl functional group

4.A distinctive R-group

Front 102

What part of an amino acid is acidic? Why is it acidic?

Back 102

The carboxyl group- it is acidic because two oxygen atoms are highly electronegative

Front 103

R-groups

Back 103

Varying side chains of Amino acids. Each of the 20 R-groups is unique

Front 104

What are the 3 most common structural formulas of side chains? What do they mean?

Back 104

Non polar side chains-No charge

Polar Side chains-Partial charges form hydrogen bonds

Electrically charged side chains- Charged side chains can form ionic and hydrogen bonds.

Front 105

What do different R- groups affect?

Back 105

The reactivity of an amino acid

Solubility-some dissolve and and some don't depending on whether they are polar or non polar

Front 106

What are the three questions to determine what type of amino acid it is?

Back 106

1)Does the side chain have a negative charge? If so, it has lost a proton and is acidic

2)Does the side chain have a positive charge? if so, it has taken a protein so it must be basic

3)If the side chain is uncharged, does it have an oxygen atom? If so, it is an uncharged polar.

If all three questions are no, then the amino acid is non polar.

Front 107

Monomer

Back 107

Molecular subunit like an amino acid.

Front 108

Polymer

Back 108

When a large number of monomers are bonded together

Front 109

Polymerization

Back 109

The process of linking monomers together

Front 110

Macromolecule

Back 110

Biologists use this word to denote a very large molecule made up of similar molecules joined together.

Front 111

Proteins

Back 111

Macromolecules, or polymers that consist of amino acid monomers.

Front 112

How do monomers polymerize?

Back 112

Through condensation or dehydration reactions

The newly formed bond between monomers results in the loss of a water molecule

Front 113

Hydrolysis

Back 113

Breaks polymers apart by adding a water molecule, which reacts with the bonds, then separates one monomer from the polymer chain

Front 114

Peptide bond

Back 114

The C-N covalent bond that forms from a condensation reaction. They are usually stable linkages

Front 115

What are the three key points to note about the peptide bonded backbone

Back 115

1)R-group directionality-The side chains extend out from the back bone and make it possible for them to react with each other and with water

2)Directionality- N terminus (Where protein synthesis begins) to C- terminus

3)Flexibility-The single bonds on either side of the peptide bond can rotate, so the structure as a whole is flexible.

Front 116

Polypeptide

Back 116

Polymers that contain 50 or more amino acids

Front 117

Protein

Back 117

Often used to describe any chain of amino acids, but refers to complete functional form of the molecule.

Front 118

Primary Structure of Proteins

Back 118

The unique sequence of amino acids in a protein. The number of combinations of the acids are limitless.

Front 119

Secondary Structure of proteins

Back 119

The second level of the hierarchy created by hydrogen bonding between components of the peptide bonded backbones. The hydrogen bonds form alpha helix or beta pleated sheet

Front 120

Ionic Bonding

Back 120

Ionic bonds form between groups that have full and opposing charges, such as the ionized acidic and basic side chains

Front 121

Quaternary structure of a protein

Back 121

When proteins contain multiple polypeptidess that interact to form a single structure, this combination of polypeptides gives protein a quaternary structure

Front 122

Macromolecular Machines

Back 122

Groups of proteins that assemble to carry out a particular function

Front 123

How is protein folding directed?

Back 123

By the sequence of amino acids present in the primary structure

Front 124

Denatured (Protein)

Back 124

Unfolded- this happens by treating proteins with compounds that break hydrogen bonds and disulfide bonds

Front 125

Molecular Chaperones

Back 125

Proteins that help to facilitate protein folding. They belong to a family of proteins called heat-shock proteins

Front 126

Protein function is depended on what?

Back 126

A proteins shape, controlling when or where it is folded will regulate the proteins activity

Front 127

Prions

Back 127

Proteins that folded into infectious, disease-causing agents. The infectious form propagates by inducing conformational changes in normal proteins that cause them to adopt the alternative, infectious shape.

Front 128

What does the final shape of a protein depend on?

Back 128

The proteins folding, or the function of protein

Front 129

Proteins are crucial to most tasks for cells to exist. These 6 are...

Back 129

Catalysis

Defense

Movement

Signaling

Structure

Transport

Front 130

Active Site

Back 130

The location where the substrate binds to the enzyme and where catalysis occurs

Front 131

Why are enzymes good catalysts?

Back 131

They bring reactant molecules, called substrates, together in precise orientation so he atoms involved in the reaction can interact.

Front 132

Fertilization

Back 132

The process of uniting a sperm and an egg

Front 133

Gametes

Back 133

Reproductive cells such as sperm and eggs

Front 134

Who hypothesized gamete formation and how did he do it?

Back 134

August Weissman proposed that there must be a distinctive type of cell division that leads to the reduction in chromosome numbers

Front 135

Meiosis

Back 135

Nuclear division that leads to a halving in of chromosome number and ultimately to the production of the sperm and egg.

Front 136

sex chromosomes

Back 136

The X and Y chromosomes that are associated with an individuals sex.

Front 137

Autosomes

Back 137

Non sex chromosomes

Front 138

Homologous Chromosomes

Back 138

Chromosomes that are the same size and shape, and have the same content or the same genes. They can, however carry different alleles.

Front 139

Gene

Back 139

A section of DNA that influences some hereditary trait of an individual

Front 140

Allele

Back 140

Different versions of the same gene. For example, the gene for eye color is the same. But homologs can contain different alleles which are blue and green eye color.

Front 141

Karyotype

Back 141

The number and types of chromosomes present

Front 142

Diploid

Back 142

Organisms that have two alleles of each gene

i.e. humans, insects, trees

Front 143

Haploid

Back 143

Organisms whose cell contains just one type of each chromosome.

ie bacteria, fungi

Front 144

Haploid number

Back 144

The letter n that stands for the number of distinct types of chromosomes in a given cell

Front 145

Ploidy

Back 145

Combination of sets and n is termed the cells ploidy

Diploid cells are designated 2n, because two chromosomes of each type are present-one from the mother and one from the father

Front 146

Polyploidy

Back 146

Having three or more of each type of

Front 147

What happens in Meiosis 1?

Back 147

The homologs in each chromosome pair separate from each other, and two haploid cells are created

Front 148

What happens in Meiosis 2?

Back 148

sister chromatids from each chromosome separate. The cells produced by Meiosis 2 also have one of each type of chromosome, but now the daughter chromosomes are no longer replicated

Front 149

How do chromosomes move during Meiosis?

Back 149

By microtubules of the spindle apparatus that attaches to kinetochores located at the centromere of each chromosome.

Front 150

When does meiosis begin?

Back 150

after chromosomes have been replicated in the S phase

Front 151

Early Prophase 1

Back 151

The stage in Meiosis one in which the chromosomes condense, spindle apparatus forms, the nuclear envelope starts to break down, and the homologous pairs come together

Front 152

Synapsis

Back 152

The pairing of homologous chromosomes that creates a bivalent or a tetrad

Front 153

Late prophase 1

Back 153

The second stage of meiosis 1 in which the nuclear envelope breaks down and microtubules of the spindle apparatus attach to kinetochores. Non sister chromatids begin to separate

Front 154

Chiasmata

Back 154

The crossover points where the chromosome stays joined at certain locations

Front 155

Crossing Over

Back 155

The reciprocal changes between different homologs that creates non sister chromatids that have both paternal and maternal segments. This increases diversity of genes.

Front 156

Metaphase 1

Back 156

The third stage of meiosis 1 in which the kinetochore microtubules move the pairs of homologous chromosomes to a region called the metaphase plate in the middle of the spindle apparatus

Front 157

Anaphase 1`

Back 157

The fourth stage of Meiosis 1 in which the homologs separate and begin moving toward opposite ends of the cell

Front 158

Telophase 1 and Cytokinesis

Back 158

Chromosomes move to opposite poles of the spindle apparatus and the spindle apparatus disassembles

Front 159

Prophase 2

Back 159

The first stage of meiosis 2 in which the spindle apparatus forms, nuclear envelope breaks apart

Front 160

Metaphase 2

Back 160

The second stage of Meiosis 2 in which Replicated chromosomes, consisting of two sister chromatids, are lined up at the metaphase plate

Front 161

Anaphase 2

Back 161

The third stage of Meiosis 2 in which the sister chromatids separate and the daughter chromosomes that result begin moving to opposite poles of the spindle apparatus

Front 162

Telophase 2

Back 162

The last phase of Meiosis 2 in which the chromosomes move to opposite poles of the spindle apparatus. A nuclear envelope forms around the haploid chromosomes.

Front 163

Cohesins

Back 163

The proteins that hold the sister chromatids together

Front 164

synaptonemal complex

Back 164

A network of proteins that holds the two homologs tightly together

Front 165

Asexual Reproduction

Back 165

any mechanism of producing offspring that does not involve the production and fusion of gametes. It produces exact clones of the parents.

Front 166

How many pairs of chromosomes does each cell in our bodies contain

Back 166

23 pairs, so 46 chromosomes in total

Front 167

Genetic recombination

Back 167

The appearance of new combinations of alleles

Front 168

The principle of independent assortment

Back 168

The phenomena that each daughter cell gets a random assortment of maternal and paternal chromosomes