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DAT > Chapter 1 bio > Flashcards

Chapter 1 bio Flashcards

1
Q

Matter

A

anything that takes up space and has mass

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2
Q

Element

A

A pure substance that has specific physical/chemical properties and can’t be broken down into a simpler substance

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3
Q

Atom

A

the smallest unit of matter that still retains the chemical properties of the element

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4
Q

Molecule

A

two or more atoms joined together

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5
Q

Intramolecular forces

A

attractive forces that act on atoms within a molecule

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6
Q

Intermolecular forces

A

forces that exist between molecules and affect physical properties of the substance

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7
Q

Monomers

A

single molecules that can polymerize, or bond with one another

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8
Q

Polymers

A

substance made up of many monomers joined together in chains

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9
Q

Dehydration (condensation) reaction

A

creates a covalent bond between monomers and releases water

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10
Q

Hydrolysis

A

a reaction that breaks a covalent bond using water

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11
Q

Carbohydrates

A
  • used as fuel and structural support
  • they contain carbon, hydrogen, and oxygen atoms (CHO)
  • they can come in the form of monosaccharides, disaccharides, and polysaccharides
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12
Q

Monosaccharides

A

carbohydrate monomers

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13
Q

Ribose

A

a 5 carbon monosaccharide

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14
Q

Fructose

A

a 6 carbon monosaccharide

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15
Q

Glucose

A

a 6 carbon monosaccharide

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16
Q

What is an example of 2 carbohydrate isomers?

A

glucose and fructose (different arrangement of atoms)

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17
Q

Disaccharides

A
  • contain 2 monosaccharides joined together by a glycosidic bond
  • the result of a dehydration reaction
  • Ex: sucrose, lactose, and maltose
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18
Q

Glycosidic bond

A

a covalent bond that joins a carbohydrate molecule to another group

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19
Q

Polysaccharides

A

contain multiple monosaccharides connected by glycosidic bonds to form long polymers (Ex: starch and glycogen)

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20
Q

Starch

A

form of energy storage for plants

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21
Q

Glycogen

A

form of energy storage in animals

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22
Q

Proteins

A
  • contain carbon, hydrogen, oxygen, and nitrogen atoms (CHON)
  • these atoms combine to form amino acids, which link together to build polypeptides (or proteins)
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23
Q

Amino acids

A
  • are monomers of proteins
  • have an amino, carboxy;, and R-group side chain
  • there are 20 different kinds of amino acids, each with a different R-group
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24
Q

Polypeptides

A
  • are polymers of amino acids and are joined by peptide bonds through dehydration reactions
  • Hydrolysis reactions break peptide bonds
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25
Q

Primary structure of protein

A

Sequence of amino acids connected through peptide bonds

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26
Q

Secondary structure of protein

A
  • intermolecular forces between the polypeptide backbone (not R-groups) due to hydrogen bonding
  • forms a-helices and B-pleated sheets
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27
Q

Tertiary structure of protein

A
  • 3-dimensional structure due to interactions between R-groups
  • can create hydrophobic interactions based on the R-groups
  • Disulfide bonds are created by covalent bonding between the R-groups of two cysteine amino acids
  • hydrogen bonding and ionic bonding between R groups also hold together the tertiary structure
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28
Q

Protein denaturation

A
  • describes the loss of protein function and higher order structure
  • only the primary structure is unaffected
  • proteins will denature as a result of high or low temperatures, pH changes, and salt concentrations
  • Ex: cooking an egg in high heat will disrupt the intermolecular forces in the egg’s proteins, causing it to coagulate
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28
Q

Quaternary structure of protein

A

multiple polypeptide chains come together to form one protein

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29
Q

What are examples of protein function?

A

Storage, hormones, receptors, structure, immunity, and enzymes

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30
Q

Catalysts

A
  • increase reaction rates by lowering the activation energy of a reaction
  • transition state is the unstable conformation between the reactants and the products
  • they reduce the energy of the transition state
  • they do not shift a chemical reaction or affect spontaneity
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31
Q

Enzymes

A
  • act as biological catalysts by binding to substrates (reactants) and converting them into products
  • enzymes bind to substrates at an active site, which is specific for the substrate that it acts upon
  • most enzymes are proteins
  • protein enzymes are susceptible to denaturation
  • they require optimal temperatures and pH for function
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32
Q

Induced fit theory

A

describes how the active site molds itself and changes shape to fit the substrate when it binds

33
Q

ribozyme

A

an RNA molecule that can act as an enzyme (a non-protein enzyme)

34
Q

Cofactor

A

a non-protein molecule that helps enzymes perform reactions

35
Q

Coenzyme

A

an organic cofactor (i.e., vitamins), inorganic cofactors are usually metal ions

36
Q

How do enzymes catalyze reactions?

A
  • conformational changes that bring reactive groups closer
  • the presence of acidic or basic groups
  • induced fit of the enzyme-substrate complex
  • electrostatic attractions between the enzyme and substrate
37
Q

Phosphatase

A

cleave a phosphate group off of a substrate molecule

38
Q

Phosphorylase

A

directly adds a phosphate group to a substrate molecule by breaking bonds within a substrate molecule

39
Q

Kinase

A
  • indirectly adds a phosphate group to a substrate molecule by transferring a phosphate group from an ATP molecule
  • these enzymes do not break bonds to add the phosphate group
40
Q

Feedback regulation of enzymes

A

occurs when the end product of an enzyme-catalyzed reaction inhibits the enzyme’s activity by binding to an allosteric site

41
Q

Competitive inhibition

A
  • occurs when the competitive inhibitor competes directly with the substrate for active site binding
  • can be outcompeted by adding more substrate
42
Q

Noncompetitive inhibition

A
  • occurs when the noncompetitive inhibitor binds to an allosteric site that modifies the active site
  • cannot be outcompeted by adding more substrate
43
Q

Allosteric site

A

a location on an enzyme that is different from the active site

44
Q

Enzyme kinetics plot

A

can be used to visualize how inhibitors affect enzymes

45
Q

Michaelis Constant (Km)

A

is the substate concentration [X] at which the velocity (V) is 50% of the maximum reaction velocity (Vmax)

46
Q

Saturation

A

occurs when all active sites are occupied, so the rate of reaction does not increase anymore despite increasing substrate concentration (causes graph plateaus)

47
Q

How does competitive inhibition compare to normal enzyme on enzyme kinetics plot?

A

Vmax stays the same while Km increases

48
Q

How does noncompetitive inhibition compare to normal enzyme on enzyme kinetics plot?

A

Vmax decreases while Km stays the same

49
Q

Lipids

A
  • contain carbons, hydrogen, and oxygen atoms (CHO), like carbohydrates
  • they have long hydrocarbon tails that make them very hydrophobic
50
Q

Triacylglycerol (triglyceride)

A
  • is a lipid molecule with a glycerol backbone (3 carbons and 3 hydroxyl groups) and 3 fatty acids (long hydrocarbon tails)
  • glycerol and the 3 fatty acids are connected by ester linkages
51
Q

Saturated fatty acids

A

have no double bonds and as a result pack tightly (solid at room temperature)

52
Q

Unsaturated fatty acids

A
  • have double bonds
  • double bonds create kinks in the fatty acid chain, preventing tight packing and increasing membrane fluidity
53
Q

Phospholipids

A
  • are lipid molecules that have a glycerol backbone, one phosphate group, and 2 fatty acid tails
  • the phosphate group is polar, while the fatty acids are nonpolar
  • as a result, they are amphipathic (both hydrophobic and hydrophilic)
  • they spontaneously assemble to form lipid bilayers
54
Q

Cholesterol

A
  • an amphipathic lipid molecule that is a component of the cell membranes
  • it is the precursor to steroid hormones (lipids with 4 hydrocarbon rings)
  • it is the starting material for vitamin D and bile acids
55
Q

Lipoproteins

A

allow the transport of lipid molecules in the bloodstream due to an outer coat of phospholipids, cholesterol, and proteins

56
Q

Waxes

A

are simple lipids with long fatty acid chains connected to alcohols

57
Q

Carotenoids

A

are lipid derivatives containing long carbon chains with double bonds and function mainly as pigments

58
Q

Sphingolipids

A
  • have a backbone with aliphatic (non-aromatic) amino alcohols and have important functions in structural support, signal transduction, and cell recognition
59
Q

Glycolipids

A
  • are lipids found in the cell membrane with a carbohydrate group attached instead of a phosphate group in phospholipids
  • like phospholipids, they are amphipathic and contain a polar head and a fatty acid chain
60
Q

Nucleic acids

A
  • contain nucleotide monomers that build into DNA (deoxyribonucleic acid) and RNA (ribonucleic acid) polymers
61
Q

Nucleosides

A

contain a 5 carbon sugar and a nitrogenous base

62
Q

Nucleotides

A

contain a 5 carbon sugar, a nitrogenous base, and a phosphate group

63
Q

Deoxyribose vs ribose

A

Deoxyribose sugars have a hydrogen at the 2’ carbon while ribose have a hydroxyl group at the 2’ carbon

64
Q

Phosphodiester bonds

A
  • are formed through a condensation reaction where the phosphate group of one nucleotide (at the 5’ carbons) connects to the hydroxyl group of another nucleotide (at the 3’ carbon) and release a water molecule as a by-product
  • a series of phosphodiester bonds create the sugar-phosphate backbone, with a 5’ end (free phosphate) and a 3’ end (free hydroxyl)
65
Q

Nucleic acid polymerization

A

proceeds as nucleoside triphosphates are added to the 3’ end of the sugar-phosphate backbone

66
Q

DNA

A
  • is an antiparallel double helix, in which two complementary strands with opposite directionalities (positioning of 5’ ends and 3’ ends) twist around each other
67
Q

miRNA (microRNA)

A

small RNA molecules that can silence gene expression by base pairing to complementary sequences in mRNA

68
Q

mRNA

A

is single-stranded after being copied from DNA during transcription

69
Q

rRNA (ribosomal RNA)

A

it is formed in the nucleolus of the cell and helps ribosomes translate mRNA

70
Q

dsRNA (double stranded RNA)

A
  • some viruses carry their code as double stranded RNA
  • dsRNA must pair its nucleotide, so it must have equal amounts of A/U, and C/G
71
Q

tRNA (transfer RNA)

A

small RNA molecule that participates in protein synthesis

72
Q

How old is the universe?

A

approximately 13.8 billion years old

73
Q

When did the first cells appear on Earth?

A

3.5 billion years ago

74
Q

Primordial Earth

A
  • Earth’s primordial atmosphere was comprised of inorganic compounds and was a reducing environment (little O2 gas)
  • as Earth cooled, gases condensed, forming the primordial sea
  • simple compounds evolved into more complex organic compounds
  • organic monomers linked into polymers
  • protobionts emerged as precursors to cells
  • heterotrophic, obligate anaerobic prokaryotes developed
  • autotrophic prokaryotes, such as cyanobacteria capable of photosynthesis, formed. This led to oxygen production and accumulation, creating an oxidizing environment (high O2 gas)
  • Primitive eukaryotes emerged, supporting the endosymbiotic theory where membrane bound organelles (mitochondria, chloroplasts), originally free-living, were engulfed by other prokaryotes, leading to a symbiotic relationship
  • more complex eukaryotes and multicellular organisms began to evolve
75
Q

Modern Cell Theory

A
  • all lifeforms have one or more cells
  • the cell is the basic structural, functional, and organizational unit of life
  • all cells come from other cells (cell division)
  • genetic information is stored and passed down through DNA
  • an organism’s activity is dependent on the total activity of its independent cells
  • metabolism and biochemistry (energy flow) occurs within cells
  • all cells have the same chemical composition within organisms of similar species
76
Q

Central dogma of genetics

A
  • states that information is passed from DNA->RNA->proteins
  • there are a few exceptions (reverse transcriptase and prions)
77
Q

RNA world hypothesis

A

the theory that early life forms relied on self-replicating RNA both to store genetic information and to catalyze chemical reactions before the evolution of DNA and proteins

78
Q

What happens because RNA is reactive and unstable?

A
  • DNA replaced RNA in how genetic information is stored
  • proteins largely replaced RNA in catalyzing reactions (ribozymes being a notable exception)
79
Q

Endosymbiotic theory

A

states that eukaryotes developed when aerobic bacteria were internalized as mitochondria while the photosynthetic bacteria became chloroplasts

80
Q
A
81
Q
A

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