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Freshman > Chapter 1-3 Biology > Flashcards

Chapter 1-3 Biology Flashcards

1
Q

5 characteristics of life

A
  1. Membrane-bound cells
  2. Replication (cells come from other cells)
  3. Information (central dogma)
  4. Energy (ATP)
  5. Evolution
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2
Q

3 Unifying Theories in Biology

A
  1. Cell Theory (Pasteur’s broth)
  2. Chromosomal Theory of Inheritance (Boveri-Sutton)
  3. Theory of Evolution (Darwin’s Finches)
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3
Q

Parts of the scientific method

A
  1. Theory
  2. Hypothesis
  3. Experiment
  4. Prediction
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4
Q

Theory v.s. Hypothesis v.s. Law

A

Theory is a broad explanation based on repeated observations and patterns.

Hypothesis is a testable and specific.

Law is a summary or mathematical statement that is known to be a fact.

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5
Q

Central Dogma:
DNA to RNA (__) to Protein (__)

A

transcription, translation

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6
Q

DNA base pairs?

A

Adenine to Thymine
Guanine to Cytosine

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7
Q

RNA base pairs?

A

Adenine to Uracil
Guanine to Cytosine

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8
Q

DNA is ___, meaning when DNA replicates, one strand is used as a template for synthesizing a new strand

A

Semi-conservative

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9
Q

Proteins= function,
___= function

A

Structure

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10
Q

Population

A

Group of individuals of the same species living in the same area at the same time

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11
Q

What are the 2 conditions that need to be met for natural selection to occur?

A
  1. Individuals in a population must vary in heritable traits.
  2. Versions of heritable traits must help individuals reproduce in certain environments.
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12
Q

Natural selection acts on ___.

A

Individuals

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13
Q

Evolutionary change occurs in ___.

A

Populations

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14
Q

____ occurs when populations diverge to form new species.

A

Speciation

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15
Q

Fitness

A

The ability to reproduce and pass on heritable traits.

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16
Q

Adaptation

A

Trait that increases fitness

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17
Q

Main differences between Eukaryotes and Prokaryotes

A

Only Eukaryotes have a nucleus.
Eukaryotes are larger.
Eukaryotes have membrane-bound organelles.

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18
Q

Independent variable

A

What you change

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19
Q

Dependent variable

A

What is being measured

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20
Q

Control variable

A

What you are comparing to
ex: the straight flask in Pasteur’s experiment

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21
Q

What did Louis Pasteur’s experiment disprove?

A

Spontaneous Generation

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22
Q

Genes

A

DNA segments on chromosomes that code for all cell products

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23
Q

What did Rosalind Franklin discover?

A

DNA’s double helix

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24
Q

5 Types of Bonding

A
  1. Covalent
    a) Polar
    b) Nonpolar
  2. Ionic
  3. Hydrogen
  4. Hydrophobic Interactions
  5. Van der Waals Interactions
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25
Q

Which bond involves the unequal sharing of electrons?

A

Polar covalent

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26
Q

Which bond involves the equal sharing of electrons?

A

Nonpolar covalent

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27
Q

Which bond has partial charges?

A

Polar covalent

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28
Q

Which bond involves the sharing of electrons?

A

Ionic

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29
Q

Which bond has no charge?

A

Nonpolar Covalent

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30
Q

Which bond has a full charge?

A

Ionic

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31
Q

Hydrogen Bonding

A

When the partial positive charge of a H is attracted to a partial negative charge of another polar molecule.

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32
Q

Which came first, chemical or biological evolution?

A

Chemical

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33
Q

Which type of bond is hydrophobic? What should you look for?

A

Nonpolar covalent; Lots of C and H

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34
Q

Which type of bond is hydrophilic? What should you look for?

A

Polar covalent; Lots of N, O

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35
Q

Key Physical Characteristics of Water

A
  1. Small size
  2. Bent shape
  3. Highly polar covalent bonds
  4. Overall polarity
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36
Q

Molecules with more electronegativity are more ____

A

Polar

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37
Q

6 Properties of Water

A
  1. Good solvent (bc of polarity)
  2. Polar
  3. Cohesion, adhesion, surface tension
  4. Less dense as a solid
  5. High capacity for energy absorption
  6. Important in acid-base reactions
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38
Q

Cohesion v.s. Adhesion

A

Cohesion: attraction b/w like molecules
Adhesion: attraction b/w unlike molecules

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39
Q

Specific Heat

A

The amount of energy needed to raise temperature of 1g of substance by 1 degree celsius.

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40
Q

Why is the reason behind water’s high specific heat?

A

Hydrogen Bonds

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41
Q

Higher polarity mean ___

A

More energy needed to change the temperature

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42
Q

Buffers minimize changes in __

A

pH

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43
Q

Endothermic v.s. Exothermic

A

Endothermic must absorb thermal energy to proceed and exothermic must release it.

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44
Q

First Law of Thermodynamics

A
  1. Energy is conserved
  2. Energy can’t be created or destroyed
  3. Energy can’t be transferred or transformed
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45
Q

Second Law of Thermodynamics

A

Entropy, or the amount of disorder in a system, always increases

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46
Q

What makes a chemical reaction spontaneous?

A
  1. Proceed on their own
  2. No added energy needed
47
Q

If products have lower potential energy than reactants then the reaction is __

A

Spontaneous

48
Q

A reaction is spontaneous then the products are __ ordered than reactants.

A

Less (more polarity or electronegativity means less potential energy)

49
Q

What did Miller’s Spark Discharge find?

A
  1. Heat and electrical charges formed the precursors of life
  2. Amino acids were created within the time the experiment was held
50
Q

6 Functional Groups

A
  1. Hydroxyl
  2. Phosphate
  3. Sulfhydryl
  4. Amino
  5. Carboxyl
  6. Carbonyl
51
Q

SH

A

Sulfhydryl

52
Q

NH2

A

Amino

53
Q

PO4

A

Phosphate

54
Q

COOH

A

Carboxyl

55
Q

CO or COOH

A

Carbonyl

56
Q

OH

A

Hydroxyl

57
Q

Functional groups found in amino acids

A

Carboxyl and Amino

58
Q

Monomers are the building blocks of __

A

Polymers

59
Q

Condensation

A

Monomer in, water out

60
Q

Hydrolysis

A

Water in, monomer out

61
Q

Explain why even though proteins are one of the main components of life, why they are not capable for being the sole reason of life.

A

Think about the five characteristics of life. Although amino acids could have polymerized to form small proteins, these proteins would need to replicate, evolve, and possess information to be considered alive.

62
Q

Four Levels of Protein Structure

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
    (remember structure= function)
63
Q

5 Parts of an Amino Acid

A
  1. H atom
  2. NH2 (amino functional group)
  3. COOH (carboxyl)
  4. R-group
  5. Central Carbon
64
Q

Primary Structure

A

Linear structure of amino acids (there are 20 types of amino acids)

65
Q

Which amino acid has a charge and which one doesn’t?

A

Amino acids in water would have a charged functional group (ionized), and amino acids not in water don’t (non-ionized)

66
Q

Charges on a functional group help in what ways?

A
  1. Help amino acids stay in solutions
  2. Affect amino acid reactivity
67
Q

Properties of an amino group are based on their __

A

R-group

68
Q

Functional groups can participate in ___

A

Chemical reactions

69
Q

If there is no functional group, there are a lot of __ and __

A

C, H

70
Q

An acid has a ___ charge in their side chain and bases have a ___ charge.

A

Negative, Positive

71
Q

Polar side chains have a ___ charge and can form ___ bonds.

A

Partial, Hydrogen

72
Q

You should look for __ in polar side chains.

A

O

73
Q

Nonpolar side chains have __ charge and you should look for __ and __.

A

no, C and H

74
Q

Which has a more soluble r-group, hydrophilic or hydrophobic?

A

Both, hydrophobic is more soluble in hydrophobic solvents and vice versa.

75
Q

A peptide bond is between the ___ group of one amino acid and an ___ group of another. __-__ Covalent bond results from the condensation reaction.

A

Carboxyl, Amino, C-N

76
Q

R-groups interact with each other and ___

A

Water

77
Q

Polymers are written from __ to __.

A

N-terminus to C-terminus

78
Q

T/F : A peptide bond cannot rotate

A

True, double bonds restrict movement

79
Q

T/F: Amino acid chains are not flexible

A

False, single bonds on either side of the peptide bond can rotate

80
Q

Oligopeptide

A

Chain of fewer than 50 amino acids

81
Q

Polypeptide

A

Chain of 50+ amino acids

82
Q

Protein

A
  1. Term describing amino acid residue
  2. Complete function form of molecule
83
Q

N-terminus –> __
C-terminus –> __

A

Nitrogen amino group
Carboxyl amino group

84
Q

Which of the following is true of the peptide bond?
a) It attaches the carboxyl group of one amino acid to the carboxyl group of another
b) It’s a covalent bond formed via condensation
c) It attaches one amino group to another
d) It can rotate

A

b

85
Q

Amino acids have which two functional groups?

A

Amino group and Carboxyl group

86
Q

The secondary structure is formed by ___ bonds between
1. ___ group of one amino acid and
2. ___ group of another amino acid

A

Hydrogen bonds
Carbonyl
Amino

87
Q

In the hydrogen bonds within a secondary structure, the partially positive __ is attracted to the partially negative O in the carbonyl group.

A

H

88
Q

2 types of secondary structures

A

Alpha helix (curly)
Beta pleated

89
Q

Tertiary structures result from interactions between __

A

R-groups/side-chains

90
Q

Distinctive Shape of Tertiary Structure

A

Bending and folding

91
Q

Van der Waals

A

Weak electrical interactions between hydrophobic side chains, quick, instantaneous

92
Q

Bonds between sulfhydryl groups (disulfide)

A

Covalent, non polar

93
Q

The backbone of secondary structures is which two groups?

A

Carbonyl and Amino

93
Q

A chemical that breaks disulfide bonds might destroy which level of protein structure?

A

Tertiary

94
Q

In the tertiary structures there are hydrogen bonds between the ___

A

R-groups

95
Q

Quaternary structure is the bonding of 2+ distinct polypeptide ___. Multiple polypeptides interact to form a single functional structure.

A

Subunits
Think k-pop: BTS is one functional structure. Subunits are the rap line and vocal line

96
Q

Dimers

A

Proteins with two polypeptide subunits

97
Q

Homodimers

A

Two identical subunits

98
Q

Heterodimers

A

Un-identical subunits

99
Q

Protein structure is ___

A

Hierarchal

100
Q

Fully functional – folded
Non-functional –> unfolded/ ____

A

Denatured

101
Q

Which level of protein structure does not depend on any of the other levels?

A

Primary

102
Q

Folding is __

A

Spontaneous

103
Q

Why is a folded molecule more energetically stable than an unfolded molecule?

A

Folded molecule has less potential energy.

104
Q

Molecular Chaperones

A
  1. Help facilitate protein folding
  2. Block inappropriate interactions between unfolded proteins
105
Q

A hydrophobic R-group would most likely be found ___.

A

In the interior of a protein

106
Q

Misfolding can be infectious because of ___, because they can tell other proteins to change their shape

A

Prions

107
Q

6 Protein Functions

A
  1. Structure
  2. Catalysis -speed up chem reactions
  3. Protection -antibodies
  4. Transport - facilitate enter/exit
  5. Movement -motor proteins move cells
  6. Signaling -convey signals between cells
108
Q

Enzymes are proteins that are ___. They hold __ in a precise orientation, so they bind to the ____ on the enzyme.

A

Catalysts, Substrates, Active-site

109
Q

Another word for substrate is __

A

Reactant

110
Q

Lock and Key Model

A

One specific substrate will bind to one specific enzyme.

111
Q

Acids ___ protons and bases ___ protons

A

Donate, Receive

112
Q

The higher the pH, the __ the protons

A

Fewer

Freshman (8 decks)

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