Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

biochem > exam 1 > Flashcards

exam 1 Flashcards

1
Q

enthalpy

A

total heat content

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

entropy

A

level of disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

exothermic

A

(-), release of heat, 1 structure breaking into multiple parts, spontaneous, exergonic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

endothermic

A

(+), multiple parts joining into 1 structure, non-spontaneous, endergonic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

ONLY animals cells have

A

lysosomes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

ONLY plant cells have

A

chloroplasts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

ONLY bacterial cells have

A

zero membrane-bound organelles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

plant and bacterial cells have

A

cell walls

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

animal and bacterial cells have

A

flagella

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

animal and plants cells have

A

golgi, rough/smooth ER, mitochondria, nucleus, similar in size + both eukaryotic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

animal, plant and bacterial cells have

A

cell membrane, ribosomes, DNA, cytoplasm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

prokaryotic cells don’t have a

A

nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

cell membrane

A

barrier that protects cell; semipermeable, in pro and euk cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

ribosomes function

A

protein synthesis; in euk and pro cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

mitochondria

A

responsible for cell respiration that creates ATP; in euk cells only

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

nucleus

A

encloses genetic info and site of replication; euk cells only

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

DNA

A

contains instructions for reporduction/proteins; in both euk and pro cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

cell wall

A

controls water intake and prevents osmotic lysis

in both euk (PLANT ONLY) and pro cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

rough ER

A

has ribosomes, makes proteins that leave the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

smooth ER

A

no ribosomes, produces lipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

chloroplasts

A

IN PLANTS ONLY; site of photosynthesis in euk plant cells only

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

golgi apparatus

A

“shipping” center for materials; modifies, pack/ships and transports proteins/lipids/etc in euk cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

functional groups in proteins

A

amine group and carboxylic acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

functional group containing phosphate found in DNA

A

phosphoric acid ester

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

symbol for change in enthalpy

A

delta H

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

change in entropy

A

delta S

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

correlation between level of organization in molecules and change in entropy

A

exothermic enthalpy: increase in entropy means MORE randomness in product
endothermic enthalpy: decrease in entropy means MORE disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

does human beings/organisms violate the second law of thermodynamics?

A

no–we exchange energy with our environment, staying in compliance with the second law

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

difference between exothermic and exergonic?

A

exothermic: releases HEAT
exergonic: releases ENERGY

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

equation for pH of any aqueous solution

A

[H+] [OH-] = 1.0 x 10^-14 M

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

equation for H+ and pH

A

pH = -log10 [H+]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Ka represents

A

acid disassociation constant which describes the strength of an acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Ka =

A

[H+] [A-] / HA

where HA is the weak acid and A- is the conjugate base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

pka is used for

A

strong acids mainly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

pka =

A

-log(Ka)

36
Q

Henderson-Hasselbach equation is used to calculate

A

the pH of a buffering system

37
Q

native conformation

A

major conformation of proteins considered protein’s “native conformation”

38
Q

levels of protein structure

A

primary, 2ndary, tertiary, quarternary

39
Q

primary structure is the…

A

sequence of amino acids in a polypeptide chain, read from N terminus to C terminus

40
Q

tertiary structure is the…

A

3D arrangement of all atoms

41
Q

changes in one AA in the primary sequence can…

A

alter biological function

42
Q

secondary structure is the

A

H-bonded arrangement of protein’s backbones
includes alpha helix and beta pleated sheet

43
Q

each AA residue has 2 bonds with reasonably free rotation

A

alpha carbon and amino nitrogen

alpha-carbon and carboxyl carbon

44
Q

alpha helix has peptide bonds and each are

A

trans and planar

45
Q

carboxyl and amino H bonds are parallel..

A

to helical axis which allows stability of H bond

46
Q

all R groups point

A

outward from the helix

47
Q

direction of alpha helix coil?

A

clockwise or right handed

48
Q

what can disrupt an alpha-helix?

A

proline created a bend
electrostatic repulsion caused by proximity of side chains of like charge (Lys +, Arg +, Glu -, Asp -)
steric crowding caused by proximity of bulky side chains (Val, Ile, Thr)

49
Q

each peptide bond in beta pleated sheets is…

A

trans and planar
may be parallel or antiparallel

50
Q

polypeptide chains lie

A

adjacent to one another

51
Q

beta-pleated sheet’s R groups

A

alternate (first above and then below plane)

52
Q

carboxyl and amino H bonds are b/w adjacent sheets and…

A

perpendicular to the direction of the sheet

53
Q

structures of reverse turns involves…

A

protein folding that needs polypeptide changes in direction
spatial/steric reasons - glycine common in reverse turns
proline also encountered in reverse turns

54
Q

forces stabilizing tertiary structure

A

noncovalent interactions and covalent interactions

55
Q

noncovalent interactions

A

H bonds b/w polar side chains (Ser and Thr)
hydrophobic interaction of non-polar (Val, Ile)
electrostatic attraction of charge (Lys +, Glu -)
electrostatic repulsion (Lys/Arg +, Glu/Asp -)

56
Q

covalent interactions

A

disulfide bonds between side chains of cysteines

57
Q

quarternary structure is the association of…

A

polypeptide monomers into multisubunit proteins (dimers, trimers, tetramers)

58
Q

hydrophobic interactions are major factors in

A

protein folding

59
Q

hydrophobic interactions help proteins

A

fold so that nonpolar side chains are on inside away from water

hydrophobic interactions are spontaneous

60
Q

protein folding chaperones

A

aid in correct and timely folding of many proteins; exist in organisms from prokaryotes and humans

61
Q

denaturation is the

A

loss of structure order that controls assignment of biological activity of each protein structure

62
Q

causes of denaturation

A

heat, changes in pH, detergents (disrupts hydrophobic interactions), urea (disrupts H bonding), mercaptoethanol (reduces disulfide bonds)

63
Q

what atoms does carboxyl group give up in a hydrolysis rxn?

A

Oxygen

64
Q

what atoms are lost from the amino group in a hydrolysis

A

2 hydrogen

65
Q

direction of peptides?

A

N-terminus (amino group) to C-terminus (carboxylic acid)

66
Q

what bonds stabilize the alpha-helix?

A

h bonds + alpha-helix is part of 2ndary structure

67
Q

h bonds direction…

A

parallel to helix axis

68
Q

which way do R groups point?

A

outwards from helix b/c they are too big to fit in the coil of the helix

69
Q

what bonds stabilize the beta sheet?

A

h bonds

70
Q

h bonds in a beta sheet are between the carboxyl of…

A

one AA to amine group of another AA

71
Q

h bonds in a beta sheet lie…

A

perpendicular to the beta pleated sheet

72
Q

r groups point above or below plane of the sheet?

A

alternate above and below plane

73
Q

in antiparallel beta-sheets, chain runs..

A

in alternating directions (N–C and C—N)

74
Q

in parallel sheets..

A

N===C N===C

75
Q

why does proline disrupt alpha-helix and beta sheet?

A

proline’s R group is bonded to the backbone amine group

76
Q

where is proline found in either alpha-helices and beta-pleated sheets?

A

beginning

77
Q

which ‘small’ AA might accommodate the tight turns of reverse turns observed in beta-pleated sheets?

A

glycine (R group is just H)

78
Q

why do hydrophobic interactions among subunit R groups take place?

A

b/c of aqueous outside environment, R groups that are nonpolar orient towards inside, away from water

79
Q

R groups are involved in..

A

nonpolar/hydrophobic interactions b/c they’re hydrophobic

80
Q

what interactions among subunit R group help stabilize tertiary and quarternary structures?

A

h bonds
hydrophobic interactions
electrostatic attraction
electrostatic repulsion
disulfide bonds

81
Q

how can pH denature proteins?

A

could affect h bonds or electrostatic attraction/repulsion
can deprotonate/protonate molecules

82
Q

how can detergents denature proteins?

A

they disrupt hydrophobic interactions

83
Q

how can urea denature proteins?

A

disrupts h bonds and electrostatic interactions

84
Q

mercaptoethanol: how can it denature proteins?

A

disrupts S-S bonds (disulfide bridge)

85
Q

how can heat denature proteins?

A

usually can disrupt all bonds seen in secondary, tertiary and quarternary structures

extreme heat will disrupt primary (covalent bonds)

biochem (11 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions