BIOL112 EXAM 1 CARDS (has lectures 1-10)

0.0(0)
Studied by 11 people
call kaiCall Kai
Locked
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/138

flashcard set

Earn XP

Description and Tags

BIOL112 EXAM 1 CARDS (has lectures 1-10)

Last updated 11:46 PM on 9/20/26
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai
Chat

No analytics yet

Send a link to your students to track their progress

139 Terms

1
New cards

What domains are prokaryotes?

Bacteria and Archaea

2
New cards

protists are…

eukaryotes

3
New cards

What is a true nucleus found in?

eukaryotes

4
New cards

Which cells are more complex, eukaryotes or prokaryotes?

eukaryotes

5
New cards

What percentage of the atmosphere is N2N_2 gas?

78%

6
New cards

What makes a covalent bond nonpolar?

equal sharing of electrons

7
New cards

What type of bond holds the two NN atoms together in N2N_2?

A triple covalent bond.

8
New cards

Why is atmospheric N2N_2 difficult for most organisms to use?

The N≡NN \equiv N triple bond is extremely strong, so atmospheric N2N_2 is unusable to all but a few organisms.

9
New cards

What percentage of the atmosphere is O2O_2 gas?

21%21\%

10
New cards

Where does most of the O2O_2 in the atmosphere come from?

Photosynthesis.

11
New cards

What is ozone?

O3O_3, a molecule made of three oxygen atoms.

12
New cards

How does the ozone layer protect terrestrial life?

It blocks UVC and UVB radiation, which can damage living organisms.

13
New cards

What is the greenhouse effect?

When gases in the atmosphere trap heat from Earth, warming the planet

14
New cards

What are greenhouse gases?

Gases in the atmosphere that trap heat, such as CO2 and CH4

15
New cards

Is atmospheric CO2CO_2 currently at its highest level in Earth's history?

No.

16
New cards

When was atmospheric CO2CO_2 higher according to the lecture?

Paleocene-Eocene Thermal Maximum (PETM)

17
New cards

What happened during the PETM when CO2CO_2 was very high?

There were mass extinctions and major sea-level rise.

18
New cards

What is the electronegativity ranking of HH, CC, NN, and OO from lowest to highest?

H<C<N<O

19
New cards

What does electronegativity mean?

How strongly an atom pulls on shared electrons

20
New cards

What makes a covalent bond polar?

Unequal sharing of electrons

21
New cards

What is starch?

A polymer of glucose that plants use to store glucose.

22
New cards

What is cellulose?

A carb that is insoluble in water and acts as insoluble fiber in humans

23
New cards

Which atoms are more likely to form polar covalent bonds with each other?

Atoms with different electronegativities, because they will pull on the shared electrons unequally.

24
New cards

What is a hydrogen bond?

Partially pos/neg bond between H with N,O,F

25
New cards

What is ionic bonding?

Attraction between positive and negative charges

26
New cards

What is a hydrophobic interaction?

Nonpolar molecules come together in water

27
New cards

What are Van der Waals forces?

Weak attractions between molecules caused by temporary dipoles

28
New cards

Which four noncovalent bonds/interactions do you need to recognize?

Hydrogen bonds, Ionic bonds, Hydrophobic interactions, van der Waals forces

29
New cards

What is an acid?

A substance that releases H+ into solution.

30
New cards

What is a weak acid?

An acid that only partially dissociates and releases H+

31
New cards

What is a base?

A substance that takes in an H+, therefore reducing H+ in the entire solution

32
New cards

What is a weak base?

A base that is only partially dissociated and has a weak tendency to accept H+

33
New cards

What is protonation?

When a molecule gains an H+

34
New cards

What is deprotonation?

When a molecules looses/gives away an H+

35
New cards

After an acid deprotonates, what charge does it have?

-

36
New cards

After a base protonates, what charge does it have?

+

37
New cards

carbs feel…

sticky

38
New cards

lipids feel…

slippery

39
New cards

Low pH means what?

High acidity and high H+

40
New cards

High pH means what?

Low acidity, low H+ (alkaline)

41
New cards

As pH increases, what happens to [H+][H^+]?

H+ decreases.

42
New cards

A solution with pH 33 has how many times more H+H^+ than a solution with pH 66?

1000 times more

43
New cards

What is ocean acidification?

the ocean becomes more acidic because it absorbs extra CO2 (therefore more H+) from the atmosphere

44
New cards

What is the equation for CO2CO_2 reacting with water?

CO2 + H2O → H+ + H2O

45
New cards

What happens to ocean pH when atmospheric CO2CO_2 increases?

Ocean pH decreases.

46
New cards

What is the basic formula for carbohydrates?

(CH2O)n

47
New cards

Are carbohydrates water-soluble or lipid-soluble?

Watersoluble

48
New cards

Are carbohydrates hydrophilic or hydrophobic?

Hydrophilic.

49
New cards

What is the exception to carbohydrates generally being water-soluble?

Cellulose is insoluble in water and is insoluble fiber in humans.

50
New cards

What is the basic formula for lipids?

(CH2)n

51
New cards

Are lipids hydrophilic or hydrophobic?

Hydrophobic.

52
New cards

What is glycogen?

stored glucose/energy in animals

53
New cards

How much glycogen does the human liver store?

Enough to maintain blood sugar for about 11 hours11\,\text{hours} of fasting.

54
New cards

Why don't we store huge amounts of glycogen?

Because glycogen holds onto a lot of water, making it heavy

55
New cards

What is chitin?

Carb polymer found in arthropod exoskeletons and fungal cell walls.

56
New cards

What does protein folding mean?

The protein folds into its functional 3D shape

57
New cards

What is one of the strongest/most important forces in protein folding according to the lecture?

Hydrophobicity (hydrophobic interactions).

58
New cards

How are alpha-helices and beta-sheets stabilized?

By hydrogen bonds between the protein backbone's O and N atoms.

59
New cards

What four interactions can help stabilize a protein's shape?

Hydrophobic interactions, hydrogen bonding, ionic bonds, disulfide bridges

60
New cards

Which protein-folding interaction is the only covalent bond?

The disulfide bridge.

61
New cards

Where are disulfide bridges found?

In extracellular proteins.

62
New cards

What amino acid forms disulfide bridges?

Cysteine.

63
New cards

Where are hydrophobic R-groups usually found when a protein folds?

On the inside of the protein, away from water.

64
New cards

What is the exception to hydrophobic R-groups being on the inside?

An alpha-helix that spans a lipid bilayer.

65
New cards

Where are the hydrophobic R-groups located in a membrane-spanning alpha-helix?

On the outside of the protein, where they contact the nonpolar lipid bilayer.

66
New cards

Why do they face outward in a membrane-spanning alpha-helix?

Nonpolar–nonpolar contact with the lipid bilayer is the most stable arrangement.

67
New cards

What do some proteins need in order to fold correctly?

Molecular chaperones.

68
New cards

What are intrinsically disordered proteins (IDPs)?

Proteins that do not have a distinct, fixed 3D shape

69
New cards

What is a ligand?

A molecule that binds to a protein and induces a response/reaction

70
New cards

Where does a ligand bind?

At a binding site/active site

71
New cards

What makes a ligand able to bind to a protein/receptor?

Complementary shape and electrostatic contour

72
New cards

Do the amino acids that make up a protein's binding site have to be next to each other in the amino acid chain?

No. Proper folding can bring amino acids from different parts of the chain together to form the binding site.

73
New cards

What is denaturation?

when a protein loses its shape and stops working properly

74
New cards

What can cause protein denaturation?

Changes in temperature, pH, ion concentration, or certain chemicals.

75
New cards

Is protein denaturation always irreversible?

No it can be reversible

76
New cards

Are shape changes that are part of a protein's normal function reversible?

Yes.

77
New cards

Conformational change

a protein changes shape temporarily to do its job

78
New cards

What is the difference between denaturation and a normal conformational change?

Denaturation is when the protein loses its normal shape and function, usually because of a disruptive condition. Conformational change is when a protein changes shape temporarily to do its job, then can return to its original shape

79
New cards

What are the three parts of a nucleotide?

Base, sugar, phosphate

80
New cards

nucleoside

base and sugar

81
New cards

is ATP a nucleotide?

yes

82
New cards

DNA is a ____ strand while RNA is a ____ strand

double, single

83
New cards

What are the two types of nitrogenous bases?

Pyrimidines and Purines

84
New cards

Which bases are pyrimidines?

T U and C (TUC the pyramid)

85
New cards

Which bases are purines?

A and G (Pure As Gold)

86
New cards

How can you recognize a pyrimidine vs. a purine structurally?

Pyrimidine has 1 ring and purine has 2 rings

87
New cards

What sugar is found in RNA?

Ribose

<p>Ribose</p>
88
New cards

What sugar is found in DNA?

Deoxyribose

<p>Deoxyribose</p>
89
New cards

What is the 5' carbon associated with?

it forms a covalent bond with the phosphate group

90
New cards

At which carbon do the sugars in DNA and RNA differ?

They differ at the 2' carbon

91
New cards

What makes up the backbone of DNA or RNA?

Sugars + phosphates.

92
New cards

What is the charge of the DNA/RNA backbone?

Highly negative

93
New cards

 

Starch is a _______ of glucose and it is how plants store glucose.

polymer

94
New cards

Nucleic acids are built in the ______ direction.

5’ to 3’

95
New cards

The DNA backbone is highly negative because of the ______

phosphates

96
New cards

Nucleotides are connected by…

Phosphodiester bonds

97
New cards

DNA replication requires an enormous amount of _____ & ______.

nitrogen and phosphorus

98
New cards

What holds the two DNA strands together?

H bonds

99
New cards

What are DNA and RNA?

polymers of nucleotides joined together

100
New cards

What is protein folding?

process where a protein folds into its proper 3D shape