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Bio 145 > Cell Bio And Genetics Exam 1 > Flashcards

Cell Bio And Genetics Exam 1 Flashcards

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Biology 101 flashcards
1
Q

How do organisms evolve?

A

Natural Selection- evolving in response to environment

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2
Q

Adaption by Heritage changes

A

Survival of fittest, mutations occur then are passed down.

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3
Q

3 parts of cell theory

A
  1. Cells are structural unit of life
  2. All organisms are composed of cells
  3. All cells arise from pre-existing cells
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4
Q

Endosymbiotic Hypothesis

A

Origin of eukaryotic cells from prokaryotic cells phagocytosis, once symbiosis become obligatory, transfer of DNA to nucleus of prokaryotic cell.

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5
Q

3 domains of life

A
  1. Bacteria
  2. Archea
  3. Eukarya
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6
Q

Selective pressures

A
  1. Cells must be large enough to accommodate all DNA
  2. Must be able to get solute across cell in a reasonable amount of time
  3. Must be able to communicate with the enviornment
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7
Q

SA/V ratio

A

V= volume of cytoplasm
Want small volume so the nucleus has more control over the cell to respond to the environment

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8
Q

Organic Molecules

A

Always contain C+H dissolve in water

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9
Q

Inorganic molecules

A

Ionic bonding, no c, dissolves into ions

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10
Q

Biotic evolution(def and mechanisms)

A

Def: genetic change in pop that is inherited
Mechanisms: genetic variation and natural selection

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11
Q

Chemical evo(accepted origin)

A

Accepted origin: formation of complex organic molecules created by smaller inorganic atoms/molecules in the ocean. Depends fundamentally on atomic structure.

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12
Q

6 atoms used in organic molecules and why

A

CHNOPS (almost always polar covalent) and are highly electronegative

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13
Q

Electronegativity of an atom is defined by:

A
  1. Number of protons in atomic nucleus
  2. Distance b/t protons in nucleus and valence e- (extra shells are harder to control)
  3. E- repell each other
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14
Q

Cation

A

Positive ion

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15
Q

Anion

A

Negative ion

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16
Q

Water special props (why its important)

A
  1. Polar
  2. Excellent solvent
  3. High specific heat
  4. Can be s,l, or g within temps suitable for life
  5. Solid form less dense
  6. Hydrogen bonds\
    These properties make probiotic life possible
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17
Q

Urey and Miller proved…

A

Organic molecules can originate from non-organic precursors such as air

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18
Q

How old is chemical evo and bio evo?

A

Chem evo: 4.2 bill yrs ago
Bio evo: 3.8 bill yrs ago

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19
Q

2 larger functions proteins perform. Examples?

A

Metabolism: enzymes, hormones, gene regulation, transporters
Structure: contractive, antibodies, support

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20
Q

Amphipathic

A

Having both hydrophobic and hydrophilic ends

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21
Q

Steps of building a protein

A

DNA (transcription)
mRNA (translation)
Amino acid sequence (folding)
Alpha helix or beta sheets

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22
Q

Glycine

A

Smallest amino acid r group (just H)

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23
Q

Proline

A

Covalent bond back from R-group to amine group causing it to be cyclic. Causes kink in beta sheet protein folding is nonpolar

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24
Q

Cystine

A

Disulfide bonds important to folding through disulfide bonds

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25
Q

Who was the first to identify cells?

A

Anton van Leeuwehoek Dutch 1600s simple microscopes
Robert Hook British 1600s compound microscope

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26
Q

What did Schleiden study?

A

plant cells

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27
Q

what did schwann study

A

animal tissues

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28
Q

anaerobic

A

Fermentation in cytosol (pyruvate is converted to lactate where most free energy remains and 2ATP are released

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29
Q

thermophiles

A

able to live in very hot enviornment

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30
Q

how long ago did pigments like chlorophyll form

A

2.5 bill yrs ago

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31
Q

oxygenic photosynthesis

A

Energized membrane ADP + P= ATP and a decreased energy membrane

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32
Q

aerobic prokayrotes evolved…

A

2 bill years ago

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33
Q

eukaryotes evolved…

A

1.2 bill yrs ago

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34
Q

metazonas(plants and animals) evolved

A

60 mill yrs ago

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35
Q

Why is Microbial diversity immense?

A

evolving for 3.8 bill yrs

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36
Q

How was Spontaneous Generation(abiogenesis) refuted

A

Louis Pasteur’s swan-necked flask experiment elliminating air showing that water won’t form life spontaneously

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37
Q

Whittaker: 5 kingdoms

A

plants, animals, protists, monera, and fungi

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38
Q

Carl Woese (1972)

A

16SrRNA as exmaple to popose 3 domains

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39
Q

Endosymbiosis and the Evolution of Eukarya

A

An alpha mitochondria (proteobacterium) or a cyanobacterium was recognized and engulfed by a primitive anarobic eukaryote, but wasn’t distroyed. Bacterium underwent both physiological and genetic integration, creating obligatory dependency.

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40
Q

Evidence to support Endosymbiosis

A
  1. mitochondria and chloroplasts resemble bacteria size and appearance
  2. like bacteria, mitochondria, and chloroplasts have their own DNA
  3. the ribosomes of chloroplasts resemble those of bacteria
  4. 16SrRNA sequences found in mitochondria and chloroplasts support their deriviatio from prokaryotes
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41
Q

Eukaryotic mRNAs are typically composed of…

A

introns (noncoding) and exons (coding) sequences

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42
Q

Genes are transcribed into… and processed into… in the….

A

mRNA… mature transcripts… nucleus

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43
Q

mature mRNAs are then …. to the… where they are… into… at the ….

A

transported… cytoplasm… translated… protiens… ribosomes

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44
Q

4 parts of an amino acid aside from central carbon

A

amino group, carboxylic acid group, hydrogen atom, and r group

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45
Q

peptide bonds (what are they and how are they formed)

A

covalent bonds between amino acids, formed by dehydration/condensation reactions formed between a carboxyl group and a amino group

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46
Q

N terminus

A

the amino terminus at the start of a protien

47
Q

C terminus

A

the carboxyl terminus which is the growing end of the protien, where more aminos are added

48
Q

4 groups of amino acids

A

Polar charged residues, polar uncharged residues, non polar amino acids, special amino acids

49
Q

polar charged residues (examples)

A

such as aspartic acid and glutamic

50
Q

polar uncharged residues

A

are not charged despite the fact there is an uneven distribution of electrons

51
Q

non polar amino acids

A

often associated with lots of methyl groups, example, alanine, valie, leucince, isoleucine, phenylalanine, tryptohtan

52
Q

special amino acids

A

glycind- smallest cysteine- forms disulfide bonds which are important to folding proline- forms covalent bond with amine group and r group

53
Q

How do amino acids make a difference in resulting protien?

A
  1. polar vs nonpolar
  2. hydropillic vs hydrophobic
  3. charged vs uncharged
  4. small vs large (based on r groups)
54
Q

Primary Structure

A

sequence of amino acids within protien that determines protien’s 3d structure peptide bonds

55
Q

Secondary structure

A

refers to conformation of small portions of polypeptide chai alpha helix and beta pleated sheet. hbonds

56
Q

Tertiary structure

A

3d conformation of the protien, h-bonds, other noncovalent interactions (vander walls force, disulfide bonds)

57
Q

Quarternary Struct

A

Some protiens are not comprised of a single polypeptide chain, but rather multiple chains

58
Q

Protiens are dynamic

A

Can change confirmation, especially when something binds to it. Can make certain protiens active or inactive

59
Q

Hydrophilc

A

Polar attracts water

60
Q

Hydrophobic

A

Non-polar, repells water

61
Q

Enzymatics

A
  1. Almost all enzymes are protiens
  2. ES complex is non covalently bound
  3. Chemical reactions can happen w/o action of enzymes but occur slowly
  4. Enzymes speed up rate at which ractions occur
  5. Enzymatic reactions are bidirectional, and the concentration of substrate and product determines direction that rxn will occur
  6. has a reaction rate r
62
Q

exergonic and endogonic rxns are ….

A

coupled energy created from exergonic rxns are used to preform endogonic

63
Q

2 laws of thermodynamics

A
  1. energy can not be created or destroyed only transferred or transformed
  2. events in universe occur “down hill” from higher to lower energy state
64
Q

Free Energy G… delta G

A

is the energy that is avaliable to do work… is the free energy released when reactants are converted into products understandard conditions

65
Q

Steady State metabolism

A

reactants and products are constant because:
1. the products of one reaction become substrates for the next
2. new substrate is brought ffrom outside of the cell, and terminal products are removed

66
Q

How do enzymes lower activation energy

A

Enzymes bind more tightly to the transition state than to reactantss. this binding stablizes teh activated complex and decreases the energy

67
Q

lock and key model

A

just as locks are unique to their keys, the enzyme has a shape that is complementary to that of its specific substrate

68
Q

induced fit model

A

not all enzymes will fit the substrate like a lock and key; rather, the interaction of E and S enduces the fit. Namely the substrate induces a confirmational change in the enzyme such that E/S is induced

69
Q

active site

A

where the substrate binds to te enzyme

70
Q

membrane functs

A
  1. barrier- seperates interior of cell from enviornment
  2. transport- regulates entry and exit of solutes
  3. intercellular interaction- cell adhesion
  4. response to external stimuli- cell signaling
  5. scaffold for reactions- it coordinates metabolic pathways
71
Q

membrane made of

A

lipids- phospholipids, glycolipids, sphingolipids, sterols
protiens-glycoprotiens, lipoporitens, integral, periphrial
carbs- covalently linked glycolipids

72
Q

membrane structure

A

phospholipid bilayer- hydrophobic tails and hydrophilic heads

73
Q

fluid mosaic model

A

the cell membrane as a tapstry of phospholipids, cholesterols, and protiens that are constntly moving

74
Q

2 experiments that support fluid mosaic model

A
  1. cell fusion expeiments
  2. FRAP
75
Q

FRAP is most effective when most of the lipids are…

A

unsaturated

76
Q

How does cholesterol affect phase transition temperature of a membrane?

A

A pure phospholipid bilayer changes from a gel to liquid rather quickly. This is because it impacts the ability for hydrophilic tails to densely packed.

77
Q

sphingolipids

A

consists of a sphingosine consists of a log FA chain attached to a glycerol moiety, not via the acyl ester linkage.

78
Q

alloysteric inhibition

A

binds to protien causing confirmational changes and effects the ability of enzyme to attach to substrate

79
Q

competetive inhibition

A

inhibitor attaches to active site of enzyme stopping it from creating product

80
Q

2ndary active transport

A

transport across concentration gradient use ATP generated by passive transport from another molecule moving with concentration gradient

81
Q

cotransporter

A

moving two solutes at a time

82
Q

symport

A

cotransport of solutes moving in the same direction

83
Q

antiport

A

cotransport moving solute in oppisite directions

84
Q

outer membrane of mitochondria

A

50% lipid

85
Q

outer membrane of mitochondria

A

3:1 protein:lipid (cristea) where the e- chain takes place is highly impermeable has lots of special transporters for molecules and ions. Some specific to Ca2+ transport since another mitochondrial role is to regulate cytosolic calcium concentrations.

86
Q

Substrate level phosphorlation

A

Where an enzyme creates ATP through attaching a P to an ADP, does not yield a lot of ATP

87
Q

NAD+ is a….carrier
NADH is considered…

A

Hydrogen
Reducing power

88
Q

Glycolysis

A

Glucose secondary active symbiotic transport
C6H12O6—- 2 pyruvate
2ADP + 2P—— 2 ATP (substrate lvl phosphorylation)
2NAD+ +2H—— 2NADH(reducing power) +H+ (high energy e-)

89
Q

Phophofructokinase

A

An allosteric regulator of glycolysis takes off phosphate group from ATP

90
Q

TCA cycle

A

Happens in mitochondrial matrix
2 pyruvate—- 6CO2 completely oxidized
3NAD+ +2FAD—- 8 NADH +2FADH2
2GDP + P—— 2 GTP (substrate level phosphorylation)

91
Q

E- transport chain

A

Occurs in Cristea (outer membrane)
NADH +H—- NAD+
H is split into e- and protons
Creates water and H20

92
Q

What happens to protons in the e- transport chain

A

Pumped across then gets brought back across membrane through ATP synthase and creates ATP using energy from protons crossing the gradient

93
Q

ATP synthase

A

An enzyme attached to a pump using the energy created from the dissipation of proton motive force to create atp from adp

94
Q

PMF

A

Proton motive force

95
Q

Mitochondrial Matrix

A

Many enzymes and ribosomes plus double stranded DNA(its own genome!) inner mitochondria

96
Q

NADPH vs NADH

A

NADPH moves e- around w anabolic reactions
NADH moves e- around w catabolic reactions

97
Q

Aerobic respiration

A

In mitochondria pyruvate is completely oxidized to CO2 and a lot of high energy electrons ultimately makes 32-36ATP

98
Q

Chemiosmosis

A

The processes by which energy stored in e- is converted into chemical energy in the form of ATP

99
Q

NADH dehydrogenase

A

Accepts H atoms and donates them to next player in ETS (NAD-NADH)

100
Q

Flavoproteins

A

Derived from riboflavin. Can accept h atoms and donate e-. Here where the H is split into protons and electron considuents (FAD-FADH2; FMN-FMNH2)

101
Q

Cytochromes

A

Proteins with a heme prosthetic group: can accept and donate only e-

102
Q

Ubiquinone(Coenzyme Q)

A

Non-proteinaceous and lipid soluble. Can accept H atoms and donate e- (like flavoproteins)

103
Q

Iron-sulfur proteins

A

Iron containing proteins that can accept or donate e-, but the iron atoms are not associated with a heme group; rather, linked to inorganic sulfur atoms associated with cysteine residues.

104
Q

What function does O2 serve in the electron transport chain

A

O2 is very electronegative and pulls e- through the chain, acts as final e- acceptor

105
Q

ATP/ADP translocase

A

A transmembrane enzyme that moves ATP out of cell after creation

106
Q

NADH creates … ATP

A

3

107
Q

FADH2 creates…ATP

A

2

108
Q

Inter membrane space

A

Between inner and outer membranes swells during active transport

109
Q

basic amino acids are

A

positively charged

110
Q

acidic amino acids are

A

negatively charged

111
Q

cofactors

A

bind to active site are non proteins and are essential for amino acid activity

112
Q

zwitter ion

A

ionized version of an amino acid ionization varies with ph

113
Q

pyruvate dehydrogenase

A

pyruvate into acetyl CoA and Co2 before entering TCA cycle

Bio 145 (3 decks)

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