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Cell Physiology > Unit 1 > Flashcards

Unit 1 Flashcards

1
Q

What are proteins made of

A

Amino acids

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2
Q

How are proteins joined together by

A

Peptide bonds

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3
Q

What are the functions of proteins in cell

A

Speed up the rate of chemical reactions, & move cells

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4
Q

How many different type of amino acids are there

A

20 types

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5
Q

What are fatty acids made up of

A

Long chains of carbon bonded to one another & to hydrogen atoms

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6
Q

What are triglycerides

A

Have 3 fatty acid chains attached to a glycerol molecule

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7
Q

What are phospholipids

A

a lipid containing a phosphate group in its molecule

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8
Q

What are carbohydrates made up of

A

Monosaccharides

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9
Q

What do carbohydrates do

A

Act as energy storing molecules in many organisms

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10
Q

What are monosaccharides

A

simple sugars

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11
Q

What are complex carbohydrates

A

Monosaccharides bonded together

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12
Q

What are the macromolecules

A

Sugars, fatty acids, amino acids, & nucleotides

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13
Q

Small organic building blocks (sugar, fatty acids, etc.) build what

A

Large organic molecules of the cell such as polysaccharides glycogen & starch in plants, fats & membrane lipids, proteins & nucleic acids

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14
Q

What is the central dogma; & what is the steps

A

DNA to protein
DNA to RNA to protein

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15
Q

What is a gene

A

Portion of DNA that encodes info needed to synthesize a specific protein

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16
Q

Transcribed

A

Changed into to

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17
Q

Transcription

A

The first step of gene expression in which RNA is made

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18
Q

Translation

A

Specific protein is synthesized from a code of the RNA transcript

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19
Q

Having a codon, means having what

A

3 nucleotides

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20
Q

Having 3 nucleotides means

A

Having a codon

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21
Q

What does RNA have

A

Info to build a protein

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22
Q

What is the RNA transcript divided into

A

3 base codons

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23
Q

Where does the translation start

A

Start codon

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24
Q

where does translation stop

A

Stop codon

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25
Q

What is the promoter & what does it do

A

The promoter is the Dna being ready to make the transcription happen but NOT the start codon

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26
Q

What does upstream mean

A

Before

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27
Q

What does downstream mean

A

After

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28
Q

What is RNA polymerase?

A

Transcription

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29
Q

What is the terminator

A

The stop site or stops the process of transcription

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30
Q

-ASE

A

Deals with enzymes

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31
Q

What do transcription factors do

A

Bind to protein & regulates DNA to mRNA

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32
Q

what are transcription factor binding sites

A

Proteins with DNA binding activity that are involved in the regulation of transcription

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33
Q

what does template strand mean?

A

The DNA sequence that can duplicate itself during mRNA synthesis

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34
Q

what does consensus sequence mean

A

A consensus sequence is a sequence of DNA, RNA, or protein that represents aligned, related sequences

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35
Q

What does it mean when a Transcription factors can be master regulators

A

a gene at the top of a gene regulation hierarchy, particularly in regulatory pathways related to cell fate and differentiation.

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36
Q

What are exons

A

Regions of the transcript that contain codons that code for protein

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37
Q

What are Intron

A

a segment of a DNA or RNA molecule which does not code for proteins and interrupts the sequence of genes.

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38
Q

BACTERIAS DONT HAVE WHAT

A

INTRONS BECAUSE THEY ARE GENES

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39
Q

What can be selectively removed & retained to increase the diversity of transcripts & what is the offical name for it

A

Introns
Alternative splicing

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40
Q

What is the start codon

A

AUG

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41
Q

If the mRNA transcript codons are shifted by one letter what would happen

A

Change the sequence & will go back to the original on the third shift

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42
Q

What are the stop codons

A

UAA, UAG, UGA

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43
Q

What does degrading protein mean

A

Remove protein cell

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44
Q

What can an inactive protein do

A

Change how a pathway is working

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45
Q

Protein are made of what

A

Amino acids

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46
Q

What binds amino acids

A

Peptide bond

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47
Q

N terminus

A

Beginning of polypeptide chain

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48
Q

C-terminus

A

End of polypeptide chain

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49
Q

What determines how the protein folds

A

R group

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50
Q

What is van deer walls attraction

A

Interaction between hydrophobic amino acids

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51
Q

What helps assist with protein folding

A

Chaperons

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52
Q

What are chaperones

A

Proteins that assist in protein folding

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53
Q

What are the two common protein folding pattern

A

Alpha Felix and beta sheet

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54
Q

When folding what does it contain

A

Alpha and beta patterns because of hydrogen bonding

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55
Q

How many steps are there in the protein structure

A

4

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56
Q

What are the 4 main protein structure; out of all of these which one is where a lot of important stuff happens

A

Primary protein
Secondary protein
Tertiary protein (Important, and chaperones are here)
Quaternary protein

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57
Q

-ase

A

Enzymes

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58
Q

What do enzyme do

A

Help speed or start chemical reaction

59
Q

Where do enzymes bind

A

Substrate and active site

60
Q

Kinase

A

Enzyme that transfers a phosphate group from atp to another protein, changes the protein structure, turns it on or off, protein count stays the same and RNA as well

61
Q

Competitive inhibition

A

Competiting to bind and prevents reactions

62
Q

Non-competitive inhibition

A

Inhibitor binds to an allsteric site altering the protein conformation, use to activate or deactivate

63
Q

what determine which protein is selected for degradation?

A

Ubiquities-protea some system

64
Q

Ubiquities-protea some system

A

This enzyme puts on a protein that states that this needs to be degraded; it then goes to the trash so not all of them are taken out

65
Q

proteasome

A

The trash can that proteins are disassembled

66
Q

Glucose is used for what

A

ATP

67
Q

What is a oligosaccharides

A

2-10 monosaccharides units

68
Q

What are polysaccharides

A

Form hundreds or thousand of monosaccharides

69
Q

Condensation reaction

A

One unit of OH and another react to each other

70
Q

What is hydrolysis

A

Carbohydrate polymers can be broken

71
Q

Condensation and hydrolysis are reversable? T or F

A

True

72
Q

What happens in condensation

A

H2O is expelled and makes a chain

73
Q

What happens in hydrolysis

A

Water is consumed and it breaks down chain

74
Q

Glycosidic bond

A

Unit of glucose

75
Q

Is hydrophilic head region reactive

A

Yes

76
Q

Is hydrophobic tail region reactive

A

No

77
Q

Saturated

A

Double bond

78
Q

Unsaturated

A

Single bond

79
Q

What do phospholipids make up

A

2 Cell membrane

80
Q

What caused bending in the hydrophobic tail

A

Saturated bond

81
Q

What does ATP stand for

A

Adenosine TriPhosphate

82
Q

What do phosphoanhydride bonds produce

A

Lots of energy

83
Q

How many parts is ATP divided into & what are they

A

Adenine, ribose, & phosphate

84
Q

ATP hydrolysis yields?

A

ADP

85
Q

ADP hydrolysis yields

A

AMP

86
Q

What is the process of getting glycolysis & at the end what do you get

A

Polysaccharides -> simple sugars -> glucose -> GLYCOLYSIS -> pyruvate

87
Q

Where does glycolysis occur

A

Cytoplasm

88
Q

Result of glycolysis produces and what is the net gain?

A

2 ATP/ Pyrite

89
Q

What happens when too much atp is produced

A

Negative feedback occurs & inhibits Hexokinase, Phosphofructokinase(PFK) & pyruvate kinase

90
Q

What does PFK mean

A

Phosphofructokinase

91
Q

What happens when too little ATP happens

A

Glycolytic enzymes active PFK & pyruvate kinase

92
Q

PFK is dual regulated? T or F

A

True

93
Q

What does allosterically mean?

A

Hydrophobic and Hydrophilic

94
Q

What does the allosteric activator & inhibitor do

A

Repress & boost its

95
Q

Once pyruvate gets converted to Acetyl-CoA and enters the mitochondria what is it called

A

Citric Acid cycle

96
Q

what does NADH & FADH_2 do

A

Donate electrons

97
Q

What does carnitine acyltransferase do

A

Modifies fatty acid (Oxidation)/ transfer channel

98
Q

What is Beta- oxidation

A

Fatty acids to Acetyl CoA

99
Q

After the fatty acid is modified it goes through a transporter channel called what

A

Carnitine acyltransferase 1 & 2

100
Q

Where are the matrix, inner membrane, outer membrane, & intermembrane space located int he mitochondria

A

Matrix- gray space? open space :)
inner membrane- in between inner & outer membrane
outer- outside wall
inner- inside wall

101
Q

What does dynamic mean

A

Changing

102
Q

where is there high production of ATP

A

Intermembrane of mitochondria

103
Q

Oxidative phosphorylation

A

Electron passing through

104
Q

what does OXPHOS mean

A

Oxidative Phosphorylation

105
Q

purpose of OXPHOS

A

Electron flow across complexes

106
Q

Two stages to OXPHOS

A

1) Energy of electron transport is used to pump protons across membrane
2) ENERGY IN THE PROTON GRADIENT IS HARNESSED BY ATP SYNTHASE TO MAKE ATP

107
Q

How many complexes are there

A

4 for atp synthesis, they pass the electron over to the next till its to the goal or ATP

108
Q

What is the endosymbiosis theory

A

Agent cells engulf a cell & became a mitochondria

109
Q

What is hydrolyze ATP

A

reverse synthase & pump protons back into the intermembrane space

110
Q

Compare & contrast Carbohydrates & Lipid (SODAS)

A

C- short term storage L- Long term storage
C- More readily digested L- Less easily digested
C- Stores half as much ATP L- Stores twice as much ATP

111
Q

What is autophagy & how many membrane?

A

Self recycling of cellular material & compose of a double membrane

112
Q

What is the largest organelle in the cell

A

Endoplasmic reticulum

113
Q

Endoplasmic reticulum

A

Network of membrane enclosed tubules & sacs

114
Q

Rough ER function

A

synthesis protein

115
Q

Smooth ER function

A

Detoxify & lipid metabolism

116
Q

Order of secretory pathway

A

ER -> Golgi apparatus -> secretory vesicles ->outside of cell(Secreation)

117
Q

Do ER protein use a common set of ribosomes? T or F

A

True

118
Q

Contranslational

A

Transportation to compartment as its getting translated

119
Q

Order of docking the ribosome to the ER membrane

A

Er protein synthesis -> Er signal sequence(Info stored) -> Signal recognition particle (SRP) (NONMEMBRANE) -> SRP receptors (receives) -> Protein translator (Last step)

120
Q

What does SRP

A

Signal recognition particle

121
Q

Peptidase

A

PEPTIDE ENZYME

122
Q

What does the signal peptidase do

A

Chopped off signal peptide because it is hydrophobic

123
Q

endocytosis

A

Removal of plasma membrane components to be delieverd to internal structure

124
Q

Exocytosis

A

Secretory pathways delivers protein, carbohydrates, or lipids to plasma

125
Q

Lumen

A

Opening or Hole

126
Q

What does it mean when a pathway has directionality

A

Vesicles have direction or go one way

127
Q

Coated vesicles

A

Protein coat vesicles to give direction

128
Q

What are the fuctions of coated vesicles

A

Concentrates the cargo protein inside the vesicles (Concentrate/Max cargo protein)
Provides the shape to the vesicle by bending the membrane around (Give shape)

129
Q

What are the three different coated vesicles

A

Clathrin-coated: Golgi -> Plasma membrane
COP1 coated vesicles: Golgi -> ER
COP2 coated vesicles: Er -> Golgi

130
Q

How do coated proteins get added on or removed

A

Proteins called GTPases

131
Q

What are GTPases

A

Enzymes that are for cell signaling (On or Off)

132
Q

What happens when GTPases binds to GTP

A

hydrolyzes it & becomes GDP Nd is considered off

133
Q

What happens when GTPases is bind to GDP

A

GDP make it turn off

134
Q

What does GTPases regulate two proteins

A

GAP (GTPases activating Protein)
GEF ( Guanine Exchange Factor)

135
Q

GAP binds to GTPase

A

Makes hydrolyzation happen to GDP, & GAP turns off GTPases

136
Q

What does GEF do

A

It exchange the GDP of GTPases for GTP, turning on GTPases

137
Q

What are the two main group

A

ARF GTPase & Sar1 GTPase

138
Q

ARF GTPase

A

Regulates COP1 & clathrin coat assembly

139
Q

SAR1 GTPase

A

Regulate COP2 coat assembly

140
Q

COP2 vesicles bud from where & do what

A

ER membrane & regulated by the Sar1 GTPase

141
Q

What is Sar1 GTPase involved in

A

Disassembling the COP2 vesciles & hydroluyes GTP to GDP

142
Q

What is the area being curved in a membrane bending protein called

A

BAR domain

143
Q

What is Dynamin

A

A type of GTPase & a lipid binding domain

144
Q

How does the cell maintain?

A

Specific protein mediate this; teather needs to have a specific protein?????

Cell Physiology (1 decks)

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