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Bio 110 > Exam 1: Lectures 1-6 > Flashcards

Exam 1: Lectures 1-6 Flashcards

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Biology 101 flashcards
1
Q

Cell theory

A

All organisms are made of cells that come from preexisting cells (Virchow, 1859)

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2
Q

Theory of evolution by natural selection

A

When individuals within a population have varying traits that can be passed on to offspring, and when certain versions of those traits allow those individuals to survive and reproduce better than those with other versions (Darwin and Wallace, 1858)

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3
Q

Classification of organisms (general to specific)

A

Domain (general)
Kingdom
Phylum
Class
Order
Family
Genus
Species (specific)

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4
Q

Binomial nomenclature

A

The unique two-name name given to each organism; written as genus-species where genus is capitalized and species is not (Linnaeus, 1735)

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5
Q

Three domains

A
  1. Bacteria
  2. Archaea
  3. Eukarya
    (Woese, 1970)
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6
Q

Scientific Method

A
  1. Make an observation
  2. Ask a question
  3. Generate a hypothesis
  4. Make predictions
  5. Experiment to test the hypothesis
  6. Results: do they support the hypothesis?
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7
Q

Hypothesis

A

A falsifiable question/claim to explain a set of observations

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8
Q

Hypothesis testing

A

A hypothesis may be tested through experimental design

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9
Q

Components of experimental design

A
  • Control group that doesn’t receive treatment
  • All treatments handles identically to eliminate variance
  • Repeatability; large sample size and replication
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10
Q

Chromosome theory of inheritance

A

Hereditary/genetic info is encoded in genes which are located on chromosomes inside the cells; includes the central dogma that DNA can be translated to RNA and transcribed into proteins (Sutton, Boveri, and Crick, 1902)

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11
Q

Atom

A

The smallest unit of a chemical element that retains the characteristics of that element; composed of electrons (negative), protons (positive), and neutrons (neutral)

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12
Q

Chemical bonds

A

Performed by electrons; covalent or ionic bonds

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13
Q

Ionic bonds

A

Chemical bonds between ions where no electron sharing occurs; rather, electrons are completely transferred from one atom to another

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14
Q

Covalent bonds

A

Chemical bonds where atoms share electrons; can be polar or nonpolar depending on how strongly the atom attracts the electrons

  • polar: when electrons are shared unequally (electrons spend more time orbiting one atom than the other)
  • nonpolar: when electrons are shared equally
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15
Q

Moles and molarity

A

Mole: the number of molecules present in a sample (Avogadro’s number)

Molarity: the number of moles in one liter of solution

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16
Q

Chemical reactions

A

Occur when a molecule is combined with another molecule or is broken down into another substance

Reactant + Reactant –> Product

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17
Q

Endothermic

A

Reaction that absorbs heat and causes the immediate surrounding temperature to decrease

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18
Q

Exothermic

A

Reaction that releases heat and causes the immediate surrounding temperature to rise

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19
Q

1st Law of Thermodynamics

A

Energy is conserved; energy is never created or destroyed, just transferred or changed

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20
Q

2nd Law of Thermodynamics

A

Entropy (disorder) increases and order decreases in the process of a reaction

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21
Q

General properties of water

A
  1. Good solvent
  2. High specific heat
  3. High surface tension
  4. High heat of vaporization
  5. Denser as a liquid than as a solid
  6. Hydrogen bonds have a role in pH
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22
Q

General properties of carbon

A

Carbon can make many covalent bonds because it is missing four electrons in its valence shell

Carbons bound together make carbon backbones which give either chain or ring shapes to molecules

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23
Q

Amino acids

A

Monomers that bind together to make proteins; can be ionized or nonionized

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24
Q

Amino acid structures

A

There are 20 types of amino acids, all of which have the same shape with varying R-groups

A nonionized amino acid is comprised of an amino group (H2N), carboxyl group (COOH), R-group, and hydrogen atom all bounded around a carbon atom

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25
Q

Protein formation & characteristics

A

Amino acids link with peptide bonds to form proteins

Proteins have three structural characteristics:
1. Directionality: amino groups are on one side and carboxyl groups are on the other
2. Flexibility: each amino acid can rotate around the carbon in the backbone
3. R-groups: they stick out and can interact with each other or water

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26
Q

Peptide bond formation

A

Covalent bonds between the COO- of one ionized amino acid and the H3N+ of another

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27
Q

Protein primary structure

A

Simple amino acid chain held together by peptide bonds (single shoelace)

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28
Q

Protein secondary structure

A

The polypeptide bends and folds and forms hydrogen bonds, allowing different parts of the same protein to interact; can take the form of an alpha-helix or a beta-pleated sheet (untied shoelace laced into a shoe)

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29
Q

Protein tertiary structure

A

Further folding and interactions between R-groups give the protein a more 3D shape; tertiary structure contains secondary structures (shoelace fully tied)

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30
Q

Protein quaternary structure

A

Several polypeptides in their tertiary structures bond to each other (tieing two shoes together by the laces)

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31
Q

General protein functions

A
  • catalyze reaction
  • antibodies
  • motor proteins and movement
  • cell-to-cell signaling
  • cell structure
  • substance transport
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32
Q

Enzymes

A

Proteins that catalyze reactions by lowering the activation energy

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33
Q

Enzyme-substrate interactions

A

Each enzyme is specific to a given substrate (aka reactants); the enzyme binds to substrates at an active site, which holds them in close together in a particular orientation which allows the reacting groups to more easily undergo reactions

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34
Q

Activation energy

A

Kinetic energy needed for a reaction to occur; less is needed when enzymes are active, therefore threshold is reached sooner

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35
Q

Effects of temperature and pH on enzymes

A

Higher temperatures, up to a point (until denaturation), increase kinetic energy and the rate of reaction

pH affects the charges in an active site since pH affects amino acids, and the enzyme cannot bind to the substrate

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36
Q

Nucleotides

A

A monomer made of a phosphate group, 5-carbon sugar, and nitrogenous base

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37
Q

Types of nucleotides

A

Differ in nitrogenous base

Pyrimidines (CUT the Py)
- cytosine
- uracil
- thymine

Purines (PURe As Gold)
- guanine
- adenine

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38
Q

DNA structure

A

Primary structure: nucleotides connected by phosphodiester linkages

Secondary structure: phosphodiester backbone on the outside and nitrogenous bases on the inside forming two antiparallel strands in a double helix
- cytosine-guanine
- adenine-thymine

Tertiary structure: supercoil!

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39
Q

RNA structure

A

Primary structure: nucleotides connected by phosphodiester linkages

Secondary structure: spontaneously-formed hairpin shape with complementary base pairings on the same strand
- adenine-uracil
- cytosine-guanine

Tertiary structure: diverse!

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40
Q

Nucleic acid formation

A

Polymer composed of nucleotides bound by phosphodiester linkages, which form a backbone with nitrogenous bases sticking out and 5’ and 3’ on opposite ends

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41
Q

Phosphodiester linkage formation

A

Link between the phosphate group of one nucleotide and the sugar of another nucleotide

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42
Q

DNA characteristics

A
  • very stable
  • template for its own synthesis: double helix separates into two strands, free bases pair with complementary bases on the original (template) strand, ending with two new identical DNA helixes
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43
Q

RNA characteristics

A
  • template for its own synthesis
  • can be catalysts (like enzymes)
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44
Q

What do DNA and RNA have in common?

A
  • phosphodiester bonds
  • sugar-phosphate backbone
  • cytosine-guanine
  • forms template for own synthesis
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45
Q

How do DNA and RNA differ?

A

DNA:
- deoxyribose sugar
- antiparallel strands
- double helix
- adenine-thymine
- less reactive

RNA:
- ribose sugar
- base pairings on same strand
- hairpin
- adenine-uracil
- more reactive

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46
Q

Carbohydrates

A

Macromolecule sugars; monosaccharides or polysaccharides

47
Q

Carbohydrate structure

A

Carbonyl group (C-O), hydroxyl functional groups (-OH), and C-H bonds

Full formula: (CH2O)n

48
Q

Monosaccharies

A

Monomer/simple sugar

49
Q

Polysaccharides

A

Polymers made up of monosaccharides linked by glycosidic linkages; can be made up of the same or different monomers

50
Q

Monosaccharide structure

A

Diverse structure:
- number of carbons in backbone can vary from 3-7 (backbone forms a ring structure if there are more than 5 carbons)
- spatial arrangement of atoms varies
- location of the carbonyl group varies (this changes monosaccharide classification)

51
Q

Polysaccharides structure

A

Monosaccharides connected by glycosidic linkages between hydroxyl groups, where the location of the bond varies greatly

52
Q

Glycosidic linkages

A

Covalent bonds between hydroxyl groups (-OH) that produces H2O due to excess leftover atoms from bond

53
Q

Ring structures

A

Carbohydrates can be formed into ring structures when the oxygen atom from the 5-carbon bonds to the 1-carbon

For example: glucose can take the form of an alpha-glucose ring or a beta-glucose ring, where the only difference is the orientation of the 1-carbon and its hydroxyl group and C-H bond

54
Q

Carbohydrates in energy storage

A

Starch (plants) and glycogen (humans)

55
Q

Starch

A

Carbohydrate produced in chloroplasts of plants and stored in the roots and stem; composed of alpha-glucose monomers connected with glycosidic linkages to form helix-shaped polysaccharides

These polysaccharides take the form of either amylose (unbranched) or amylopectin (branched), which together make up starch

56
Q

Glycogen

A

Carbohydrate in animals stored in the liver and muscles; composed of alpha-glucose monomers connected with glycosidic linkages to form helix-shaped polysaccharides

Glycogen is made up of only amylopectin (branched) polysaccharides, which are much more highly branched than in starch

57
Q

Carbohydrates in cell structure

A

These carbohydrates are strong and elastic and resist cell decay; for example, cellulose in plants, chitin in animals, and peptidoglycan in bacteria

58
Q

Cellulose

A

Found in plants

Composed of beta-glucose monomers that form long horizontal strands bonded by glycosidic linkages where every other beta-glucose is flipped (upside down)

Horizontal strands are connected with hydrogen bonds on each beta-glucose to the adjacent strands

59
Q

Chitin

A

Found in animals; makes up exoskeletons

Organized in the same orientation as cellulose, but made up of N-acetyl-glucosamine monomers

Because of the N-acetyl groups, vertical bonds in chitin structure alternate between hydrogen bonds and N-acetyl bonding to adjacent monomer; horizontal bonds are still glycosidic linkages

60
Q

Peptidoglycan

A

Found in bacteria

Composed of N-acetyl-glucosamine and N-acetyl-muramic acid monomers; monomers alternate with each other in horizontal strands bonded by glycosidic linkages

Parallel strands are vertically bonded by alternating peptide bonds and N-acetyl bonds

61
Q

Carbohydrates in cell identification

A

Glycoproteins

62
Q

Glycoproteins

A

Carbohydrate covalently bonds to a protein embedded within the plasma membrane of a cell and sticks out from the surface of the membrane; glycoproteins are unique to each type of cell

63
Q

Lipids

A

Non-polar and hydrophobic molecules made up of carbon and hydrogen connected by covalent bonds

64
Q

Types of lipids

A

Different types defined by solubility
- steroids
- phospholipids
- fats

65
Q

Lipid structure

A

Lipids are only made up of hydrocarbons with structure varying very slightly between types

66
Q

Cell (plasma) membranes

A

Layer of molecules that surrounds the cell, separates the internal and external environments, and selectively regulates the passage of molecules and ions

Main functions:
- helps to regulate cell volume and function
- keeps inside and outside of cell different
- keeps all cell components together

67
Q

Membrane composition

A

Made up of lipids forming a bilayer

68
Q

Bilayer formation

A

Phospholipids organize themselves into two stable rows with their hydrophilic heads interacting with water on the outside (inside cell and outside cell) and their hydrophobic fatty acid tails on the inside interacting with each other

69
Q

Selective permeability

A

Some substances cross the plasma membrane more easily than others while some don’t cross at all; impacted by hydrophobic tails and depends on size and charge of molecule

70
Q

Membrane permeability per molecule

A

High permeability:
Hydrophobic molecules (O2, CO2, N2)

Small, uncharged, polar or nonpolar molecules (H2O, indole, glycerol)

Large, uncharged, polar molecules (glucose, sucrose)

Low permeability:
Ions (Cl-, K+, Na+)

71
Q

How do lipids alter permeability?

A

The degree of saturation of the lipids affects how permeable the membrane is

72
Q

Proteins in the bilayer

A

Proteins in the membrane can be peripheral (only on one side of the membrane) or integral (spans entire membrane; faces both internal and external fluids)

Can be ion channels, transporters, or pumps

73
Q

Ion channels

A

Pores in plasma membrane that make the membrane permeable to ions; each channel is selective to a given ion

Perform facilitated diffusion; the ion follows the concentration gradient but is facilitated by the channel

74
Q

Carrier proteins (transporters)

A

Another type of facilitated diffusion where the molecule is “carried” across the membrane by a transporter protein; involves a conformational change in the protein and is often a coupled transport (exchange)

75
Q

Pumps

A

Pumps transport molecules against the concentration gradient, which is a form of active movement and requires energy

76
Q

Fluid-mosaic model

A

Lipids and proteins in membrane are constantly in motion; dynamic, lateral movements

77
Q

Hypertonic

A

Lower concentration of solutes inside cell than outside; water moves out of cell to even concentration

78
Q

Hypotonic

A

Higher concentration of solutes inside cell than outside; water moves into cell to even concentration and potentially bursts the cell

79
Q

Isotonic

A

The concentration of solutes inside and outside the cell is the same; no water moves in or out

80
Q

Organism

A

A living entity made up of one or more cells

81
Q

Five characteristics of an organism

A
  1. Made up of cells
  2. Can replicate itself
  3. Product of evolution
  4. Hereditary/genetic info is encoded in genes
  5. Is able to acquire and use energy by a) acquiring chemical energy as ATP, and b) obtaining molecules from diet as building blocks
82
Q

Cell

A

A highly organized compartment bounded by a thin, flexible membrane and containing chemicals in an aqueous solution
- the smallest unit of life
- the structural and functional unit of organisms

83
Q

The three unifying theories of biology

A
  1. Cell theory
  2. Evolution by natural selection
  3. Chromosome theory of inheritance (and the central dogma)
84
Q

Tree of Life

A

A family tree of organisms, or phylogenetic tree, which depicts the evolutionary history and relationships between species

85
Q

Prokaryotes

A

Lack a true nucleus; all of Domains Bacteria and Archaea

86
Q

Eukaryotes

A

Have a true nucleus bound in a membrane; all of Domain Eukarya (plants, fungi, animals)

87
Q

Roles of protons, neutrons, and electrons

A

Protons: form nucleus with neutrons, help determine charge of atom alongside electrons, define atomic number, add to amount of neutrons to determine mass number of atom

Neutrons: form nucleus with protons, differing amounts cause isotopes, add to amount of protons to determine mass number of atom

Electrons: help determine charge of atom alongside protons, orbit nucleus, form bonds

88
Q

Electrons and orbitals

A

Electrons orbit the nucleus in paths called orbitals; atoms can have multiple orbitals where each orbital holds up to two electrons and are grouped into levels called electron shells

89
Q

Valence shell

A

The outermost electron shell where the number of orbitals depends on the element; an atom is most stable when the valence shell is full, and attempts to form chemical bonds when valence shell is not full

90
Q

Endergonic

A

Non-spontaneous chemical reactions that require energy input

91
Q

Exergonic

A

Spontaneous chemical reactions where the reactants have more potential energy than the products

92
Q

Why is water a good solvent?

A

Polarity of water molecules and their ability to create hydrogen bonds allow other charged or polar molecules to dissolve in water

93
Q

Cohesion

A

When like molecules bond together; for example, hydrogen bonds

94
Q

Hydrogen bonds

A

Weak interactions between H of one water molecule and O of another

95
Q

Adhesion

A

When unlike molecules bond together; for example, hydrogen bonds formed between water molecules and other substances that allow molecules to dissolve

96
Q

Hydrophilic molecules

A

“Water-loving” molecules that interact with water and easily dissolve; typically charged or polar

97
Q

Hydrophobic molecules

A

“Water-fearing” molecules that don’t dissolve in water; typically nonpolar and uncharged

98
Q

High specific heat of water

A

The energy required to raise one gram of water temperature by one degree C is high

99
Q

High surface tension of water

A

The surface of water forms an elastic membrane of tightly bound molecules due to high number of hydrogen bonds

100
Q

High heat of vaporization of water

A

The energy required to change one gram of water from liquid form to gas form is high

101
Q

Why is water denser as a liquid than as a solid?

A

Due to the latticed organization of water molecules in ice, there is more space and air between the molecules, causing the ice to float in water

102
Q

pH

A

The measurement of the concentration of excess (not bonded to anything) H+ ions there are in a solution

pH = -log [H+]

103
Q

How do hydrogen bonds play a role in pH?

A

H+ + OH- <–> H20

Water is unstable and is constantly dissociating and rebonding, resulting in unbonded H+ ions which indicate pH

104
Q

Proteins

A

Large polymer molecules made up of amino acid monomers; sometimes called peptides or polypeptides when they are made up of over 50 amino acids

105
Q

Ionized amino acid

A

In an ionized amino acid, the amino group is H3N+ and the carboxyl group is COO-

These charges contribute to chemical reactivity and bond forming, and help amino acids form hydrogen bonds and stay in solutions

106
Q

How is protein folding regulated?

A

Folding is directed by amino acids in their primary structure and regulated by molecular chaperones that can fold proteins, recognize mistakes, and fix unfolded proteins

107
Q

Steroids

A

Groups of 4-ringed hydrocarbons that differ based on which side groups are attached to the rings; for example, cholesterol

108
Q

Phospholipids

A

Three parts:
- phosphate (hydrophilic head)
- glycerol
- two hydrocarbon chains (hydrophobic tails)

Phospholipids are amphipathic (have both hydrophobic and hydrophilic parts)

109
Q

Fats

A

Two parts linked by ester linkage:
- glycerol
- hydrocarbon tails (can have three tails, making it a triglyceride)

110
Q

Saturated vs. unsaturated lipids

A

Saturated lipids have only single C-C bonds
Unsaturated lipids have at least one double C=C bond

Unsaturated tails have a kink; when many lipids are unsaturated, the bilayer leaves more space for molecules to cross through

111
Q

Cholesterol in the bilayer

A

Cholesterol is hydrophobic and interacts with the fatty acid tails in the bilayer; fills the spaces and increases the density and stiffness of the membrane, which decreases fluidity and permeability

112
Q

Diffusion

A

When particles move from areas of high concentration to low concentration; is passive and spontaneous

113
Q

Osmosis

A

When water moves from areas of low solute to high solute; is passive and spontaneous

Bio 110 (4 decks)

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