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BIO 110 > Exam 1 > Flashcards

Exam 1 Flashcards

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Biology 101 flashcards
1
Q

Comparative Experiment

A

use data from the outside world, would not be possible as a controlled experiment

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2
Q

Independent Variable

A

the variable manipulated

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3
Q

Dependent Variable

A

the variable being measure, changes in response to IV

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4
Q

Negative control

A

no phenomenon is expected

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5
Q

Positive Control

A

a group where the phenomenon is expected

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6
Q

Null Hypothesis

A

there is no relationship between the two variables. Any difference is the result of random chance

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7
Q

Hypothesis

A

A hypothesis can not be proven. If it is supported by evidence, we reject the null hypothesis. If it is not supported by evidence, we fail to disprove the null hypothesis

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8
Q

Structure of Water

A

Water is a bent molecule with electrons unequally shared (different electronegativity). Oxygen is more electronegative than the hydrogens, so it pulls on the shared electrons more. Resulting in the oxygen having a slight negative charge and hydrogen having a slight positive charge.

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9
Q

Hydrogen Bonding

A

Hydrogen bonds explain the high melting and boiling points of water.Water can form hydrogen bonds with up to 4 other water molecules

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10
Q

Polarity of Water

A

Water pulls apart ionic compounds (salts) due to its polarity

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11
Q

Hydrophobic Effect

A

The dipole nature of water creates the hydrophobic effect (entropically driven exclusion from water).
Hydrophobic effect: tendency for hydrophobic molecules to clump together in polar solutions.
When nonpolar molecules are apart, it takes more energy than if all of the molecules were together. Since it requires less energy when the molecules are clumped, they proceed to the state that is thermodynamically favorable

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12
Q

Water Uses

A

Water is an important part of most biomolecules and can be crucial for the structure and function of an active site of an enzyme.
Water is often used to make and break covalent bonds
Hydrolysis: Water is used to break a bond
Condensation: water is produced as a result of a bond forming

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13
Q

weak interactions hold together complex biological molecules

A

covalent bonds
Hydrogen bonds: sharing of H atom (between polar molecules)
ionic bonds: attraction of opposite charges, charges are full
hydrophobic interactions: interaction of nonpolar substances in the presence of polar substances
van der Waals forces: interaction of electrons of non polar substances. Electrons are constantly moving, causing negative and positive regions (unequal distribution of electrons)

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14
Q

Energy

A

Endergonic: requires energy to occur (activation energy), Ereactants< Eproducts
Exergonic: releases energy, Ereactants> Eproducts
Free energy (ΔG) = [Energy]products - [Energy]reactants
energy in living systems is found in many forms (covalent bonds, electron carriers, proton
gradients, ATP)
ATP is the energetically rich energetic currency used by many reactions within a cell
the hydrolysis of ATP (a favorable reaction) is coupled with unfavorable reactions to push them forward

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15
Q

Structure of Carbohydrates, Lipids, Fatty Acids, and Triglycerol

A

Carbohydrates: made of carbon and hydrogens. Cn(H2O)n. Chain of carbons connected by single bonds, if there are more than 5 carbons carbon rings form.
Lipids: nonpolar molecules
Fatty acids: long nonpolar hydrocarbon chain with a terminal polar carboxyl functional group
Triacylglycerol: Simple lipid. 1 glycerol group and 3 fatty acid tails (hydrocarbon+acid on tp)

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16
Q

Carboydrates VS Lipids

A

Energetic differences between carbohydrates and lipids
Lipids are more efficient at storing energy than carbohydrates. More energy per carbon (less oxidized). They take up less space per carbon (water doesn’t bind to lipids)

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17
Q

Saturated versus unsaturated fatty acids

A

Saturated fatty acids: all carbon bonds are single bonds. Packs efficiently, solid at room temperature
Unsaturated fatty acids: some carbons have double bonds, causing kinks in the chain. Liquid at room temperature, can not pack efficiently. Causes membranes to be more fluid

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18
Q

Amino Acids: why these 20?

A

Because amino acids were present before life existed on earth, so life chose the 20 simplest and most common amino acids to synthesize proteins with. Only 20 amino acids are used because they have enough diversity.

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19
Q

Amino Acids: why one isoform? Why L?

A

Amino acids are almost exclusively the L isoform because their structures have to be consistent so that the proteins made folds the correct way.

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20
Q

What are the unique properties of each?

A

Nonpolar, uncharged: hydrophobic, tend to cluster together
Polar, uncharged: hydrophilic, can form hydrogen bonds
Aromatic group: nonpolar, can participate in hydrophobic interactions, made of carbon rings
Positively charged: hydrophilic
Negatively charged: hydrophilic

more carbon = more phobic

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21
Q

Protein Folding

A

Peptides are polymerized amino acids, usually synthesized at the ribosome.
All the information necessary to properly fold a protein is contained in primary sequence
If denature agents are removed, structure and function are restored

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22
Q

Primary Structure

A

The linear sequence of amino acids in a peptide

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23
Q

Secondary structure

A

Interactions between nearby amino acids give rise to regular repeating structures called secondary structure.
Secondary structure is maintained by hydrogen bonding.
α-helix by intramolecular H-bonds. For spiral regions. Full revolution every 3.6 residues, hydrogen every 4 residues.
β-sheet by intermolecular H-bonds. Form pleated sheets

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24
Q

Tertiary structure

A

the 3D structure of a folded peptide
Non-covalent forces (H bonds, hydrophobic effect, ionic interactions, Van der Waals) and disulfide bonds stabilize both Tertiary and Quaternary structures.

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25
Q

Quaternary structure

A

the 3D structure of a protein composed of more than one polypeptide.
Non-covalent forces (H bonds, hydrophobic effect, ionic interactions, Van der Waals) and disulfide bonds stabilize both Tertiary and Quaternary structures.

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26
Q

Antifreeze Proteins

A

Evenly spaced hydroxyl groups on the flat side allows for H bonds with water crystals. This makes it thermodynamically unfavorable for water molecules to add to the ice layer. This prevents the ice layer from growing too large

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27
Q

Mucins

A

Large, relatively unfolded glycoproteins. Consisting of about 80% carbohydrates, carbohydrates bind to water, causing the protein to take up a lot of space. Mucins bind to each other via dimerization domains and disulfide bridges. Hydrophobic alpha helix at the end embeds them into membranes

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28
Q

Enzymes

A

Enzymes are proteins that catalyze reactions, increase the rate of reactions

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29
Q

Coenzymes

A

molecules that bind to enzymes and put them in their functional form

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30
Q

Induced Fit Model

A

when a substrate binds to the active site, there is a conformational change in the enzyme, along with the substrate (catalysis)

31
Q

Enzymes Facts

A

Enzymes do not change the equilibrium of a reaction, they only allow the reaction to go faster
Enzyme activity can be regulate be binding something to change the shape of the active site or blocking the active site

32
Q

T.H.Morgan

A

Recognized that the inheritance of the sex chromosomes in Drosophilia closely followed the inheritance of the white-eye phenotype. Concluded genes are on chromosomes

33
Q

Oswald Avery

A

Information necessary for causing virulence survived heat treatment and was able to transform non-deadly virus strand. Concluded DNA, not proteins, are the material of heredity.

34
Q

Hershey Chase

A

Bacter was radioactive with 32P, so the bacteriophage injected bacteria with DNA. Concluded DNA is the material of heredity.

35
Q

Chargaff’s Rule

A

The number of adenosine residues is equal to the number of thymidine residues (A=T). The number of guanine residues is equal to the number of cytidine residues (G=C).
Purines: adenosine and guanosine
Pyrimidines: Cytidine and thymidine

36
Q

Watson & Crick

A

Hydrophilic sugar phosphate backbone are antiparallel strands. Run from 5’ to 3’. Hydrogen bonds between complementary bases (A-T 2, G-C 3). 10 bases/full rotations
Nucleotide=sugar+phosphate+base

37
Q

Dickerson Dodecamer

A

3D structure of DNA varies with sequence. Differences in twist, roll, propeller twist, displacements (different in many minor features). Departure from B form DNA
so important because need to locate specific sequences in our genomes in order to regulate genes (every DNA sequence is a different ligand (the specific thing a protein binds to))

38
Q

Prediction

A

If ___, then ___

39
Q

Osmotic Effect

A

high concentration water goes to low concentration water

40
Q

sugars

A

carbon:water (1:2)
more connected = less soluble
remove water to form bond, add water to break

41
Q

join 2 sugars

A

formed by a condensation reaction, splitting of water

42
Q

branching

A

more branches = more efficiency with adding and subtracting glucose

43
Q

lipid functions

A

energy storage (more energy per carbon in lipids because of how oxidized carbon is, and no water needed so better than carbohydrates)
basic structural unit of cellular membranes

44
Q

triglycerides

A

glycerol attached to 3 fatty acids
energy storage and insulation
when connect no more OH groups, and becomes hydrophobic
(and destroys part of the fatty acid that is hydrophilic)

45
Q

cis fats vs trans fats

A

natural, artificial

46
Q

membrane lipids

A

need hydrophobic and hydrophilic parts
remove 1 fatty acid add in something hydrophilic

47
Q

amino acids

A

hydrogen, amino group, carboxyl group, and r group attached alpha carbon
building blocks of proteins
neurotransmitters
energy source

48
Q

protein where is the hydrophilic and hydrophobic parts?

A

hydrophobic inside
hydrophilic outside

49
Q

proteins (primary structure)

A

linear sequence of amino acids (encoded in DNA)
determines fold and therefor function

50
Q

proteins (secondary structure)

A

hydrogen bonds between amino acids form alpha helices and beta sheets

51
Q

proteins (tertiary structure)

A

heme picket helps carry oxygen throughout the body

52
Q

proteins (quaternary structure)

A

2+ polypeptide chains form one functional molecule with subunits

53
Q

protein shape and function

A

defense (protect body from disease by recognizing and binding to foreign molecules)
structure (collagen forms strong triple helix for structural support throughout body)
communication (insulin can easily maintain its shape while traveling through the blood and helps regulate blood and sugar levels)
transport (calcium pump moves ions across cell membranes)
enzymes
storage

54
Q

protein structure

A

protein structure determined by protein structure
protein structure determined by amino acid sequence

55
Q

how do proteins know how to fold?

A

hydrophobic effect
hydrogen bonds, ionic bonds, vander waals, disulfide bonds
all of these forces help stabilize the 3d structure of proteins
bonds depend on each other

56
Q

cooperativity of folding

A

changing one part of the protein changes the other parts of the protein
change by binding something to the protein

57
Q

alpha helix

A

a repeated structure in proteins caused by hydrogen bonds between different elements of the backbone
every 3.6 residues
stable because of the hydrogen bond between the C and O of one amino acid and the N and H of another
one side very positive, other is very negative

58
Q

antifreeze proteins

A

prevent death by freezing
prevent ice from expanding
without –> keeps small
common features: bind to ice (flat regular side)
evenly spaced OH groups on the flat side allows for H bonds with water crystals
humans don’t have antifreeze proteins

59
Q

mucins

A

binds to and traps foreign things
protective layer heavy with proteins
sequence is very repetitive (largely unfolded)
extracellular glycoproteins
both membrane bound and secreted mucins share many common features. Both are highly glycosylated consisting of 80% carbohydrates

60
Q

sodium potassium pump

A

uses ATP
protein found in cell membranes, used to generate a gradient of ions
sodium out, potassium in
for each ATP that is broken down, 3 sodium out, 2 potassium in (removal of phosphate group + bind to protein which causes a structural change)

61
Q

Lock and Key Model

A

explains specificity of the enzyme but does not explain the stability of the transition state for it would require more energy to reach the transition state complex, and is more rigid

62
Q

Induced Fit Model

A

enzymes put strain on substrate, catalysts, begin reaction
causes conformational change and structural adaptation that makes this binding site more complementary and lighter
molecules mold into precise formation so that there is an induced fit where the enzyme can perform maximum catalytic function

63
Q

what do enzymes do?

A

bond between the enzyme and substrate creates energy that can be used to reduce activation energy in order to make reactions more likely to occur)

64
Q

how do you regulate enzyme activity?

A

change the structure, change function
covalent modification (another enzyme do the work)
allosteric modulators (activator or repressor, non-covalent, cells prefer because not using ATP)
more regulated = more important

65
Q

Gregor Mendel

A

provides first evidence for a heredity material

66
Q

T.H.Morgan

A

provides evidence that chromosomes are the material of heredity
sex determination related to the inheritance of x or y chromosome
inheritance of sex chromosome similar to inheritance of white-eye phenotype
alleles for the red/white eyes are carries on x chromosome

67
Q

Griffiths, and Avery

A

MICE
smooth vs rough (live or die)

68
Q

Watson & Crick

A

DNA structure

69
Q

Gene

A

the functional unit of hereity

70
Q

allele

A

a specific form of a gene at a given location on a chromosome, among multiple possible forms

71
Q

denaturing of a protein

A

hydrogen bond is broken, protein back to primary structure, when rebinds together not native shape
if remove denaturing agent, can get back to original shape

72
Q

A and G are what?

A

purines (two rings)

73
Q

T and C are what?

A

pyrimidines (one ring)

74
Q

Structure of DNA

A

Base-Sugar —- Phosphate over and over again
bases bind together via H-bonds

BIO 110 (1 decks)

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