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Adv H Biology > Unit 1 > Flashcards

Unit 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

proteomics is

A

study of the proteome

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2
Q

proteome is

A

entire set of proteins expressed by genome

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3
Q

what is larger proteome or genome and why

A

proteome because of alternative splicing and post translational modification

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4
Q

types of RNA

A

rRNA mRNA tRNA non coding RNA

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5
Q

transcriptome

A

all mRNA molecules produced by genome

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6
Q

how to find out transcriptome

A

microarray analysis

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7
Q

amino acids are made of

A

carboxyl group, hydrogen, carbon, amine group, R group

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8
Q

environmental factors that affect protein shape and function

A

ph and temperature

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9
Q

binding of proteins cause a ____ change which can consequently change the function. this can/cannot be reversible

A

conformational , can

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10
Q

when binding, shapes must be ______

A

complementary

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11
Q

primary structure

A

order in which amino acids are synthesised into amine polypeptides

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12
Q

types of secondary structure

A

alpha helix, beta sheets, turns, hydrogen bonds between atoms of same chain

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13
Q

alpha helix

A

spiral, r groups sticking out

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14
Q

beta sheets

A

running alongside each other, can be antiparallel or parallel

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15
Q

what determines whether beta sheet is parallel or antiparallel

A

N and C terminus. if they are at opposite termini then they are parallel

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16
Q

turns

A

reverse the direction of the polypeptide chain

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17
Q

tertiary structure

A

R GROUPS. folding and shape depends on these. bonding can influence folding- ionic, disulphide, hydrogen, van Der Waals, add prosthetic group eg haem

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18
Q

quartenary structure

A

links subunits (polypeptide chains) together

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19
Q

ionic bonds are

A

electrostatic

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20
Q

hydrogen bonds are

A

electromagnetic

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21
Q

disulphide bonds are

A

covalent

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22
Q

folding can hide the ____ R groups and have the _____ R groups on the outside

A

hydrophobic, hydrophilic

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23
Q

how are peripheral proteins held in place

A

charged or polar amino acids or hydrophobic interactions

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24
Q

how are integral proteins held in place

A

hydrophobic interactions

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25
Q

integral proteins

A

some transmembrane- channels, transporters, some not

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26
Q

fluid mosaic model is

A

membrane. phospholipid bilayer- moves around a lot, mosaic because of integral proteins, peripheral proteins

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27
Q

phospholipid bilayer has

A

hydrophilic polar head, hydrophobic non polar tail

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28
Q

ligands are

A

substances that can bind to a protein

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29
Q

what allows substances to bind to proteins

A

R groups and complementary binding sites

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30
Q

DNA binds to proteins a lot. Name one protein it binds to

A

histones

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31
Q

what part of DNA binds to protein

A

sugar phosphate backbone because negatively charged

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32
Q

DNA wraps around histones to form

A

nucleosomes

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33
Q

what environmental factors affect ligands

A

ph and temp

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34
Q

cooperativity

A

binding increases affinity of remaining sites

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35
Q

allosteric enzymes

A

modulators bind at secondary site, changing affinity of active site (increase or decrease)

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36
Q

phosphorylation

A

addition or removal of phosphate from R groups which causes a reversible conformational change

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37
Q

phosphorylation is a type of ___ _______ ______

A

post translation modification

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38
Q

phosphorylation regulates ____/_____ activity

A

enzyme/ receptor

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39
Q

which enzyme catalyses dephosphorylation

A

phosphatase

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40
Q

which enzyme catalyses phosphorylation

A

kinase

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41
Q

what enzyme uses ATP for phosphorylation

A

ATPases

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42
Q

water channels

A

aquaporins

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43
Q

facilitated transport

A

involves conformational change. does not require energy

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44
Q

transmembrane proteins function

A

control the concentration of ions and other molecules within the cell

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45
Q

voltage gated channels

A

controlled by changes in ion concentration.

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46
Q

ligand gated channels

A

neurotransmitters required to open binds to receptor site

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47
Q

active transport

A

conformational change requires energy from hydrolysis of ATP

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48
Q

sodium potassium pump

A

3 Na out 2 K in. phosphorylation of ADP + Pi uses active transport

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49
Q

glucose uses ____ to transport

A

facilitated transport

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50
Q

signal transductions

A

receptor proteins convert extracellular chemical signals to specific intracellular response

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51
Q

signal transductions can (3)

A

activate proteins that regulate gene transcription, rearrange cytoskeleton, change uptake/secretion of molecules

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52
Q

G proteins

A

transmits signals from outside to inside the cell

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53
Q

G proteins are active by

A

GTP

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54
Q

G proteins are inactivated by

A

GDP

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55
Q

sodium potassium pump is used for (4)

A

maintaining osmotic balance, glucose symport, resting potential neurons, ion gradient for kidney tubules

56
Q

glucose symport

A

sodium and glucose in. glucose against conc gradient so need energy from sodium going down gradient

57
Q

membrane potential

A

electrical potential difference (voltage) across plasma membrane

58
Q

resting potential value

A

-70mV

59
Q

minus sign for voltage means

A

inside of cell is negative relative to outside

60
Q

the resting potential is generated and maintained by

A

sodium potassium pump

61
Q

nerve transmission is

A

a wave of depolarisation of resting potential

62
Q

depolarisation is stimulated by

A

neurotransmitter opening ligand gated ion channels, causing resting potential to increase and action potential to begin

63
Q

order of action potential

A

neurotransmitters act as ligand and open ligand gated channel, allows ions to enter and voltage increases, voltage gated channels open, wave of depolarisation, wave passes, channels close, restore resting potential

64
Q

depolarised value

A

40mV

65
Q

polarised

A

more K+ inside. negative membrane potential

66
Q

graded potential

A

small change

67
Q

action potential

A

big change

68
Q

graph of action potential

A

depolarisation, repolarisation, hyperpolarisation

69
Q

refractory period

A

axon can’t respond to any other stimulus

70
Q

rod cells

A

changes due to light intensity, longer than cones, very sensitive to light

71
Q

cone cells

A

less sensitive to light, absorb different wavelengths of light, colours

72
Q

rhodopsin

A

combination of retinal and opsin

73
Q

photoreceptor proteins are

A

light sensitive and sense and respond to light

74
Q

how rhodopsin reacts to photon of light

A

becomes excited, nerve impulse generated, G protein activated, enzymes activated, ion channels close, sodium leak inward, membrane potential increases, hyper polarisation stimulates nerve impulse

75
Q

communication between cells caused by

A

extracellular signalling molecules, receptors and responses

76
Q

receptor molecules are

A

on target cells and have binding site for signalling molecule,

77
Q

the signals are s____

A

specific for specific receptors

78
Q

signal transduction occurs when

A

signalling molecules bind to and activates specific receptor which is on surface or within cell

79
Q

hydrophobic signalling molecules can/cannot pass through membrane

A

can

80
Q

examples of hydrophobic signalling molecules

A

steroid hormones eg oestrogen and testosterone and thyroxine

81
Q

hydrophilic signalling molecules can/cannot pass through membrane

A

cannot but signal can be transduced

82
Q

the binding of insulin triggers

A

GLUT4 glucose transporters to cell membrane of fat and muscle cells and this facilitates uptake of glucose into cells

83
Q

type 1 diabetes

A

due to lack of insulin production

84
Q

type 2 diabetes

A

due to loss of insulin receptor proteins. exercise triggers GLUt4 too so can help

85
Q

Cytoskeleton is made of

A

Proteins. Microfilaments, microtubules, intermediate filaments

86
Q

Cytoskeleton is

A

Network of proteins extending throughout cytoplasm constantly breaking down and reforming

87
Q

Function of cytoskeleton

A

Provide mechanical support
Provide anchorage for organelles
Enable whole cell to move
Enable organelles within cell to move

88
Q

Microtubules are

A

Hollow, straight cylinders made of tubulins

89
Q

Types of tubulin

A

Alpha and beta

90
Q

Tubulin governs…

A

Location and movement of membrane bound organelles

91
Q

Microtubules originate from

A

Microtubules organising centre MTOC in centrosome

92
Q

Spindle fibres are formed by

A

Microtubules

93
Q

Cell cycle order

A

M
G1
S
G2

94
Q

Decreasing rate of cell cycle causes

A

Degenerative diseases

95
Q

G1 phase

A

Growth phase where proteins are synthesised

96
Q

S phase

A

Cell continues to grow and copies chromosomes in preparation for mitosis

97
Q

G2

A

Growth phase where proteins are synthesised

98
Q

M phase

A

2 part- mitosis and cytokinesis

99
Q

Parts of mitosis

A 
PMAT 
prophase
Metaphase
Anaphase
Telophase
100
Q

First part of cell cycle is collectively called

A

Interphase

101
Q

Spindle fibres join to ____ to pull apart chromatids

A

Kinetochore

102
Q

Cytokinesis

A

Separation of cytoplasm into daughter cells

103
Q

G1 checkpoint

A

Occurs at end of G1 and checks for sufficient growth and other conditions satisfied

104
Q

If don’t pass G1

A

G0 phase which is non dividing phase

105
Q

S phase checkpoint

A

None

106
Q

G2 checkpoint

A

Occurs at end of G2 DNA replication must be completed

107
Q

M phase checkpoint

A

Occurs during metaphase and controls entry to anaphase. Checks chromosomes are aligned correctly and ensure each daughter cell receive correct number of chromosomes

108
Q

CDKs are

A

Cyclin dependant kinases. Cause phosphorylation of proteins that stimulate cell cycle if enough phosphorylation is reached, can proceed

109
Q

Types of regulatory proteins

A

Retinoblastoma Rb and P53

110
Q

Retinoblastoma

A

If non phosphorylation then restricts progression from G1 to S phase. Phosphorylation inhibits Rb activity so it can no longer bind to transcription factor so transcription factor is released and genes are trans opted for S phase to begin

111
Q

P53

A

Repairs, arrests or causes cell death.

Is there if DNA damage or cell damage

112
Q

If mutation in p53

A

Cancer

113
Q

Apoptosis is

A

Destruction of cells. Programmed cell death

114
Q

Death signals results in activation of enzymes called

A

DNAases and Proteinases (caspases)

115
Q

DNAases

A

Catalyse breakdown of DNA

116
Q

proteinases

A

Bring about degradation of cellular proteins

117
Q

Fragments at end of apoptosis are

A

Engulfed by phagocytes

118
Q

Extrinsic death signals

A

Lymphocytes can express death activator ligand called Fas which activated protein cascade that introduces caspases and causes apoptosis

119
Q

Intrinsic death signal

A

DNA damage

120
Q

Receptor proteins for steroid hormones

A

Transcription factors

121
Q

What happens to receptor protein when a signal molecule binds

A

G protein activation
Enzyme activation
Ion channels close

122
Q

Role of ligand gated ion channels in transmission of nerve impulses

A

Neurotransmitter triggers opening of ligand gated ion channels, if sufficient ion movement occurs then voltage gated ion channels open and this triggers sequence of voltage gated channels to open and a wave of depolarisation.

123
Q

Intracellular responses as a result of signal transduction

A

Activation of enzyme
Activation of G protein
Change in uptake or secretion of molecules
Rearrangement of cytoskeleton

124
Q

Steroid hormones are hydrophobic/hydrophilic

A

Hydrophobic

125
Q

Insulin is hydrophilic/hydrophobic and steroid/ peptide

A

Hydrophilic and peptide

126
Q

Tubulin is integral/ globular

A

Globular

127
Q

types of amino acid

A

acidic, basic, polar, hydrophobic

128
Q

r group of acidic amino acid

A

carboxylic acid COOH

129
Q

r group of basic amino acid

A

amine group NH2

130
Q

r group of polar amino acid

A

hydroxide group OH

131
Q

r group of hydrophobic amino acid

A

hydrocarbon CH (benzene ring)

132
Q

acidic amino acids are what charge

A

negatively

133
Q

basic amino acids are what charge

A

positive

134
Q

polar amino acids are what charge

A

slightly charged and hydrophilic

135
Q

hydrophobic amino acids are what

A

non polar

136
Q

peptide bonds are formed by what reaction

A

condensation H20 is removed

137
Q

what does peptide bond look like

A

N-H- C=0

Adv H Biology (12 decks)

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