Brainscape's Knowledge GenomeTM

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


See full index

AAA BIO107: Cell and Molecular Biology > 2. Biomolecules and Enzymes > Flashcards

2. Biomolecules and Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

made of long
unbranched chain of
these amino acids

A

proteins

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

repeating sequence of
atoms along the core of
the polypeptide chains

A

polypeptide backbone

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

give amino acids its unique properties

A

side chains

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

bonds of protein foldings

A

hydrogen bonds,
electrostatic attractions, and van der Waals

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

assist in protein folding

A

molecular chaperones

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

generated when a single
polypeptide chain twists around
on itself to form a rigid cylinder

A

a helix

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

form from neighboring segments of the polypeptide backbone that run in the same orientation

A

parallel chains

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

hydrogen bonding of the peptide
backbone; helices and β sheet

A

secondary structure

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

from a polypeptide backbone that folds back and forth upon itself, with each section of the chain running in the direction opposite of that of its immediate neighbors

A

antiparallel chains

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

formed from two or
more have most of their nonpolar
side chains on one side

A

coiled-coil

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

amino acid sequence

A

primary structure

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

full 3D organization of a polypeptide chain

A

tertiary structure

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

readily recognized when the genome of any organism is sequence

A

protein families

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

protein molecule formed as a complex of more than one polypeptide chain

A

quaternary structure

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

human genome have how many coding genes

A

21,000 protein-coding genes

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

tests to be undergone for protein sequence viewing

A

x-ray crystallography and nuclear
magnetic resonance (NMR)

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

the basic units of proteins that can fold, function, and evolve
independently

A

protein domains

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

process of creating new combination of gene functional domains

A

domain shuffling

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

during vertebrate evolution has given rise to many novel
combinations of protein
domains

A

domain shuffling

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

the subset of protein domains, mobile during evolution

A

protein modules

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

recognition domain – only in
humans

A

Major Histocompatibility
Complex (MHC) antigen

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

any region of a protein’s
surface that can interact with another molecule

A

binding site

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

forming a symmetric complex of two protein subunits (dimer)

A

head to head arrangement

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

ropelike structures;
important component of the cytoskeleton

A

intermediate filaments

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

two identical α-globin
subunits and two identical β-globin subunits, symmetrically arranged

A

hemoglobin

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

why is a helix a common
structure in biology?

A

all subunits are identical, they
can only fit together in one
way – rarely straight line
resulting in a helix

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

intrinsically disordered regions of
proteins are frequent in nature,
WHY?

A

to form specific binding sies for
other protein molecules that
are of high specificity

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

abundant outside the cell; main component of the gel-like extracellular matrix

A

fibrous proteins

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

main component in long
lived structures

A

keratin filaments

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

a dimer of two identical subunits

A

a-keratin

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

elongated three-dimensional
structure

A

fibrous protein

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

___ can spontaneously assemble into the final structure under the appropriate condition

A

purified subunits

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

another abundant
protein in ecm; highly
disordered polypeptide

A

elastin

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

4 process of disoerdered polypeptide chain

A

binding
signaling
tethering
diffusion barrier

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

consists of three long
polypeptide chains, each containing that nonpolar
amino acid glycine at every 3rd position

A

collagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

2 examples of prion diseases

A

scrapie in sheep,
Creutzfeldt-Jakob disease (CJD) in
humans
Kuru in humans
bovine spongiform encephalopathy (BSE) in
cattle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

guide construction but take no part in the final assembled structure

A

assembly factors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Can Form from
Many Proteins; self
propagating, stable β-sheet
aggregates

A

amyloid fibrils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

example of capable of self
assembly from its component parts

A

tobacco mosaic virus (TMV)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

consist of amyloid fibrils – acts like a vesicle containing peptide
and hormones

A

secretory granules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

the substance that is bound by the protein

A

ligand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

each protein molecule can usually bind just one or a few molecules out of many thousands

A

specificity

43
Q

secretes proteins
that form long amyloid fibrils
projecting from the cell
exterior that help to bind
bacterial neighbors to biofilms

A

in bacteria, secretory granules

44
Q

Proteins aggregates may be released from dead cells and accumulate as

A

amyloid

45
Q

Which disease can produce amyloid

A

Prion diseases

46
Q

The ability of a protein to bind selectively and with high affinity to a ligand depends on the formation of a set of _____

A

weak noncovalent bonds

47
Q

4 weak noncovalent bonds

A

hydrogen bonds
electrostatic attractions
van der Waals attractions
favorable hydrophobic interactions

48
Q

the region of protein that associates with a ligand

A

Binding site

49
Q

the interaction of neighboring parts of the polypeptide chain may _____

A

restrict the access of water molecules to that protein’s ligand binding sites

50
Q

the clustering of neighboring polar amino acid chains can _______

A

alter their reactivity

51
Q

3 types of interface

A
  • surface-string interaction
  • helix-helix
  • surface-surface
52
Q

binds tightly to a particular target molecule (antigen), inactivating directly or making it for destruction

A

Antibody or immunoglobulins

53
Q

complementary to a small portion of the surface of the antigen molecule

A

Y-shaped molecules with two identical binding sites

54
Q

cause the chemical transformations that make and break covalent bonds in cells

A

Enzymes

55
Q

Enzymes + substrates 

A

Products

56
Q

Speeds up reactions, act as catalysts

A

Enzymes

57
Q

Enzymes that hydrolytic cleavage reaction

A

Hydrolases

58
Q

Break down nucleic acids by hydrolyzing bonds

A

Nucleases

59
Q

Breaks down protein

A

Proteases

60
Q

Synthesize molecules

A

Synthases

61
Q

Joins together two molecules

A

Ligases

62
Q

Catalyze the rearrangement of bonds

A

Isomerases

63
Q

Catalyze polymerization reactions

A

Polymerases

64
Q

Adds phosphate group

A

Kinases

65
Q

Catalyze the hydrolytic removal of phosphate group

A

Phosphatases

66
Q

Oxidized and redox

A

Oxido-reductases

67
Q

Hydrolyze ATP

A

ATPases

68
Q

Hydrolyze GTP

A

GTPases

69
Q

Formula of enzyme substrate complex

A

E + S → ES → EP → E + P

70
Q

the maximum rate of reaction divided by the enzyme concentration

A

Turnover number

71
Q

enzymes achieve ______ of chemical reactions

A

extremely high rates

72
Q

enzymes greatly increase the local concentration of both these ____ at the _____

A

substrate molecule at the catalytic site

73
Q

unstable intermediate state

A

Transition state

74
Q

the free energy required to attain the transition state

A

Activation energy

75
Q

adds a molecule of water to a single bod bet. two adjacent sugar groups in the polysaccharide chain, thereby causing the bond to break

A

Hydrolysis

76
Q

catalyzes the cutting of polysaccharide chains in the cell walls of bacteria.

A

Lysozyme

77
Q

assisting the hydrolysis reaction. In other enzymes, a small organic molecule serves a similar purpose. Such organic molecules are often referred to as

A

Coenzyme

78
Q

a large protein assembly; allows the product of enzyme A to be passed directly to enzyme B, and so on

A

Multienzyme complex

79
Q

controls how many molecules of each enzyme it makes by ____

A

regulating the expression of the gene that encodes that enzyme

80
Q

controls enzymatic activities by confining sets of?

A

enzymes to particular compartments

81
Q

a product produced late in a reaction pathways inhibits an enzyme that acts earlier in the pathway

A

Feedback inhibition

82
Q

prevent an enzyme from acting

A

Negative regulation

83
Q

regulatory molecule stimulates the enzyme’s activity rather than shutting the enzyme down

A

Positive regulation

84
Q

Greek words ___ meaning “other” and _____ meaning “solid or 3d”

A

Allos, stereo

85
Q

Enzyme having two binding sites – active and regulatory site

A

Allosteric enzymes

86
Q

Recognizes the substrates

A

Active site

87
Q

Recognizes a regulatory molecule

A

Regulatory site

88
Q

Interaction between separated sites on a protein

A

Conformational change

89
Q

positive regulation caused by ____ between two separate binding sites

A

conformational coupling

90
Q

if the shift of a protein to a conformation that binds glucose best also causes the binding site for X to fit X better, then the protein will bind glucose more tightly when X is present than when X is absent

A

Positive regulation caused by conformational coupling between two separate binding sites

91
Q

if a shape change caused by glucose binding decreases the affinity of a protein for molecule X, the binding of X must also decrease the protein’s affinity for glucose

A

Negative regulation caused by conformational coupling between two separate binding sites

92
Q

can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site

A

Cooperative allosteric transition

93
Q

transfer of the terminal phosphate group of an ATP molecule to the hydroxyl group

A

Protein phosphorylation

94
Q

Phosphorylates

A

Protein kinase

95
Q

phosphate removal, dephosphorylate

A

Protein phosphatase

96
Q

phosphate is part of guanine nucleotide GTP; addition and removal of phosphate

A

GTP-binding proteins (GTPases)

97
Q

What happens when a tightly bound GTP is hydrolyzed by the GTP-binding protein to GDP,

A

Conformational change then inactivated

98
Q

They generate forces responsible for muscle contraction and the crawling and swimming of cells; a series of conformational changes

A

Motor proteins

99
Q

they help to move chromosomes to opposite ends of the cell during mitosis

A

Motor proteins

100
Q

coupling one of the conformational changes to the hydrolysis of an ATP molecule that is tightly bound to the protein

A

unidirectional conformation changes

101
Q

Membrane bound transporters with function to export hydrophobic molecules from the cytoplasm

A

ABC Transporters (ATP-binding cassette)

102
Q

proteins binding sites for multiple other proteins

A

Scaffold proteins

103
Q

they serve both to link together specific sets of interacting proteins and to position them at specific locations inside a cell

A

Scaffold proteins

AAA BIO107: Cell and Molecular Biology (5 decks)

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