Unit 1 Flashcards
(144 cards)
1
Q
What are proteins made of
A
Amino acids
2
Q
How are proteins joined together by
A
Peptide bonds
3
Q
What are the functions of proteins in cell
A
Speed up the rate of chemical reactions, & move cells
4
Q
How many different type of amino acids are there
A
20 types
5
Q
What are fatty acids made up of
A
Long chains of carbon bonded to one another & to hydrogen atoms
6
Q
What are triglycerides
A
Have 3 fatty acid chains attached to a glycerol molecule
7
Q
What are phospholipids
A
a lipid containing a phosphate group in its molecule
8
Q
What are carbohydrates made up of
A
Monosaccharides
9
Q
What do carbohydrates do
A
Act as energy storing molecules in many organisms
10
Q
What are monosaccharides
A
simple sugars
11
Q
What are complex carbohydrates
A
Monosaccharides bonded together
12
Q
What are the macromolecules
A
Sugars, fatty acids, amino acids, & nucleotides
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
14
Q
What is the central dogma; & what is the steps
A
DNA to protein
DNA to RNA to protein
15
Q
What is a gene
A
Portion of DNA that encodes info needed to synthesize a specific protein
16
Q
Transcribed
A
Changed into to
17
Q
Transcription
A
The first step of gene expression in which RNA is made
18
Q
Translation
A
Specific protein is synthesized from a code of the RNA transcript
19
Q
Having a codon, means having what
A
3 nucleotides
20
Q
Having 3 nucleotides means
A
Having a codon
21
Q
What does RNA have
A
Info to build a protein
22
Q
What is the RNA transcript divided into
A
3 base codons
23
Q
Where does the translation start
A
Start codon
24
Q
where does translation stop
A
Stop codon
25
What is the promoter & what does it do
The promoter is the Dna being ready to make the transcription happen but NOT the start codon
26
What does upstream mean
Before
27
What does downstream mean
After
28
What is RNA polymerase?
Transcription
29
What is the terminator
The stop site or stops the process of transcription
30
-ASE
Deals with enzymes
31
What do transcription factors do
Bind to protein & regulates DNA to mRNA
32
what are transcription factor binding sites
Proteins with DNA binding activity that are involved in the regulation of transcription
33
what does template strand mean?
The DNA sequence that can duplicate itself during mRNA synthesis
34
what does consensus sequence mean
A consensus sequence is a sequence of DNA, RNA, or protein that represents aligned, related sequences
35
What does it mean when a Transcription factors can be master regulators
a gene at the top of a gene regulation hierarchy, particularly in regulatory pathways related to cell fate and differentiation.
36
What are exons
Regions of the transcript that contain codons that code for protein
37
What are Intron
a segment of a DNA or RNA molecule which does not code for proteins and interrupts the sequence of genes.
38
BACTERIAS DONT HAVE WHAT
INTRONS BECAUSE THEY ARE GENES
39
What can be selectively removed & retained to increase the diversity of transcripts & what is the offical name for it
Introns
Alternative splicing
40
What is the start codon
AUG
41
If the mRNA transcript codons are shifted by one letter what would happen
Change the sequence & will go back to the original on the third shift
42
What are the stop codons
UAA, UAG, UGA
43
What does degrading protein mean
Remove protein cell
44
What can an inactive protein do
Change how a pathway is working
45
Protein are made of what
Amino acids
46
What binds amino acids
Peptide bond
47
N terminus
Beginning of polypeptide chain
48
C-terminus
End of polypeptide chain
49
What determines how the protein folds
R group
50
What is van deer walls attraction
Interaction between hydrophobic amino acids
51
What helps assist with protein folding
Chaperons
52
What are chaperones
Proteins that assist in protein folding
53
What are the two common protein folding pattern
Alpha Felix and beta sheet
54
When folding what does it contain
Alpha and beta patterns because of hydrogen bonding
55
How many steps are there in the protein structure
4
56
What are the 4 main protein structure; out of all of these which one is where a lot of important stuff happens
Primary protein
Secondary protein
Tertiary protein (Important, and chaperones are here)
Quaternary protein
57
-ase
Enzymes
58
What do enzyme do
Help speed or start chemical reaction
59
Where do enzymes bind
Substrate and active site
60
Kinase
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
Competitive inhibition
Competiting to bind and prevents reactions
62
Non-competitive inhibition
Inhibitor binds to an allsteric site altering the protein conformation, use to activate or deactivate
63
what determine which protein is selected for degradation?
Ubiquities-protea some system
64
Ubiquities-protea some system
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
proteasome
The trash can that proteins are disassembled
66
Glucose is used for what
ATP
67
What is a oligosaccharides
2-10 monosaccharides units
68
What are polysaccharides
Form hundreds or thousand of monosaccharides
69
Condensation reaction
One unit of OH and another react to each other
70
What is hydrolysis
Carbohydrate polymers can be broken
71
Condensation and hydrolysis are reversable? T or F
True
72
What happens in condensation
H2O is expelled and makes a chain
73
What happens in hydrolysis
Water is consumed and it breaks down chain
74
Glycosidic bond
Unit of glucose
75
Is hydrophilic head region reactive
Yes
76
Is hydrophobic tail region reactive
No
77
Saturated
Double bond
78
Unsaturated
Single bond
79
What do phospholipids make up
2 Cell membrane
80
What caused bending in the hydrophobic tail
Saturated bond
81
What does ATP stand for
Adenosine TriPhosphate
82
What do phosphoanhydride bonds produce
Lots of energy
83
How many parts is ATP divided into & what are they
Adenine, ribose, & phosphate
84
ATP hydrolysis yields?
ADP
85
ADP hydrolysis yields
AMP
86
What is the process of getting glycolysis & at the end what do you get
Polysaccharides -> simple sugars -> glucose -> GLYCOLYSIS -> pyruvate
87
Where does glycolysis occur
Cytoplasm
88
Result of glycolysis produces and what is the net gain?
2 ATP/ Pyrite
89
What happens when too much atp is produced
Negative feedback occurs & inhibits Hexokinase, Phosphofructokinase(PFK) & pyruvate kinase
90
What does PFK mean
Phosphofructokinase
91
What happens when too little ATP happens
Glycolytic enzymes active PFK & pyruvate kinase
92
PFK is dual regulated? T or F
True
93
What does allosterically mean?
Hydrophobic and Hydrophilic
94
What does the allosteric activator & inhibitor do
Repress & boost its
95
Once pyruvate gets converted to Acetyl-CoA and enters the mitochondria what is it called
Citric Acid cycle
96
what does NADH & FADH_2 do
Donate electrons
97
What does carnitine acyltransferase do
Modifies fatty acid (Oxidation)/ transfer channel
98
What is Beta- oxidation
Fatty acids to Acetyl CoA
99
After the fatty acid is modified it goes through a transporter channel called what
Carnitine acyltransferase 1 & 2
100
Where are the matrix, inner membrane, outer membrane, & intermembrane space located int he mitochondria
Matrix- gray space? open space :)
inner membrane- in between inner & outer membrane
outer- outside wall
inner- inside wall
101
What does dynamic mean
Changing
102
where is there high production of ATP
Intermembrane of mitochondria
103
Oxidative phosphorylation
Electron passing through
104
what does OXPHOS mean
Oxidative Phosphorylation
105
purpose of OXPHOS
Electron flow across complexes
106
Two stages to OXPHOS
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
How many complexes are there
4 for atp synthesis, they pass the electron over to the next till its to the goal or ATP
108
What is the endosymbiosis theory
Agent cells engulf a cell & became a mitochondria
109
What is hydrolyze ATP
reverse synthase & pump protons back into the intermembrane space
110
Compare & contrast Carbohydrates & Lipid (SODAS)
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
What is autophagy & how many membrane?
Self recycling of cellular material & compose of a double membrane
112
What is the largest organelle in the cell
Endoplasmic reticulum
113
Endoplasmic reticulum
Network of membrane enclosed tubules & sacs
114
Rough ER function
synthesis protein
115
Smooth ER function
Detoxify & lipid metabolism
116
Order of secretory pathway
ER -> Golgi apparatus -> secretory vesicles ->outside of cell(Secreation)
117
Do ER protein use a common set of ribosomes? T or F
True
118
Contranslational
Transportation to compartment as its getting translated
119
Order of docking the ribosome to the ER membrane
Er protein synthesis -> Er signal sequence(Info stored) -> Signal recognition particle (SRP) (NONMEMBRANE) -> SRP receptors (receives) -> Protein translator (Last step)
120
What does SRP
Signal recognition particle
121
Peptidase
PEPTIDE ENZYME
122
What does the signal peptidase do
Chopped off signal peptide because it is hydrophobic
123
endocytosis
Removal of plasma membrane components to be delieverd to internal structure
124
Exocytosis
Secretory pathways delivers protein, carbohydrates, or lipids to plasma
125
Lumen
Opening or Hole
126
What does it mean when a pathway has directionality
Vesicles have direction or go one way
127
Coated vesicles
Protein coat vesicles to give direction
128
What are the fuctions of coated vesicles
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
What are the three different coated vesicles
Clathrin-coated: Golgi -> Plasma membrane
COP1 coated vesicles: Golgi -> ER
COP2 coated vesicles: Er -> Golgi
130
How do coated proteins get added on or removed
Proteins called GTPases
131
What are GTPases
Enzymes that are for cell signaling (On or Off)
132
What happens when GTPases binds to GTP
hydrolyzes it & becomes GDP Nd is considered off
133
What happens when GTPases is bind to GDP
GDP make it turn off
134
What does GTPases regulate two proteins
GAP (GTPases activating Protein)
GEF ( Guanine Exchange Factor)
135
GAP binds to GTPase
Makes hydrolyzation happen to GDP, & GAP turns off GTPases
136
What does GEF do
It exchange the GDP of GTPases for GTP, turning on GTPases
137
What are the two main group
ARF GTPase & Sar1 GTPase
138
ARF GTPase
Regulates COP1 & clathrin coat assembly
139
SAR1 GTPase
Regulate COP2 coat assembly
140
COP2 vesicles bud from where & do what
ER membrane & regulated by the Sar1 GTPase
141
What is Sar1 GTPase involved in
Disassembling the COP2 vesciles & hydroluyes GTP to GDP
142
What is the area being curved in a membrane bending protein called
BAR domain
143
What is Dynamin
A type of GTPase & a lipid binding domain
144
How does the cell maintain?
Specific protein mediate this; teather needs to have a specific protein?????
