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Cell Structure and Function > Exam I > Flashcards

Exam I Flashcards

(71 cards)

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1
Q

Prokaryote

A

No nucleus, no membrane bound organelles

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2
Q

Eukaryote

A

Nucleus and membrane bound organelles

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3
Q

Atoms that cells are made of

A

H,B,C,N,O,F,Si
Na,Mg,K,Ca,P,S,Cl
V,Cr,Mn,Fe,Co,Ni,Cu,Zn,Mo,Se,I

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4
Q

Cells are made of… (percentages of macromolecules)

A

70% H20, 30% chemicals. Chemicals are: 2% polysaccharide, 15% protein, 6% RNA, 1% DNA, 2% phospholipid, 3% small molecules, 1% inorganic ions

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5
Q

List the bond strengths from strongest to weakest

A

Covalent, Ionic, hydrogen, Van der Waals

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6
Q

Nucleotide structure

A

pentose sugar (ribose in RNA, deoxyribose in DNA), phosphate group, and nitrogen base

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7
Q

Central Dogma

A

DNA is transcribed into RNA which is translated into proteins

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8
Q

mRNA

A

messenger RNA, transcription of DNA

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9
Q

tRNA

A

Transfer RNA, allows for polymerization of amino acids in order dictated by mRNA

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10
Q

rRNA

A

Ribosomal RNA, creates ribosomes

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11
Q

Negatively charged (acidic) amino acid side chains

A

Asp, Glu

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12
Q

Positively charged (basic) amino acid side chains

A

Arg, Lys, His

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13
Q

polar noncharged amino acid side chains

A

Asn, Gln, Ser, Thr, Tyr

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14
Q

Non-polar amino acids

A

Met,Ala,Gly,Ile,Cys,Leu,Pro,Phe,Trp,Val

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15
Q

Alpha helices

A

Hydrogen bonds form all in the same orientation, causing the secondary structure of a protein to form a helix

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16
Q

Beta sheets

A

Hydrogen bonds form in alternating directions, pleating the secondary structure of the protein back and forth

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17
Q

Homodimer vs heterodimer

A

same parts vs different parts

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18
Q

dimer vs trimer etc

A

dimer is two, trimer is three

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19
Q

Disulfide bonds

A

The only covalent bonds formed by amino acids, between the sulfides in cytesine. pretty strong

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20
Q

Homologue

A

A double of a DNA sequence (gene duplication)

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21
Q

Orthologue

A

Two species each with one of the genes that arose from gene duplication

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22
Q

Paralogue

A

Two differing genes within ONE organism that both arose from gene duplication of one gene

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23
Q

Translation

A

Forming a polypeptide by following mRNA

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24
Q

Elongation factors - bacteria

A

EF-tu:Elongation factor thermal unstable Tu (EF-Tu) is a G protein that catalyzes the binding of aminoacyl-tRNA to the A-site of the ribosome inside living cells., EF-G:Elongation factor G (EF-G) uses energy stored in GTP to catalyze movement of transfer RNAs and messenger RNA in the ribosome during the translocation step of prokaryotic protein synthesis.

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25
Elongation factors - EUKS
EF1 and EF2
26
what do elongation factors do?
increase speed and accuracy of translation
27
Binding release factor
binds to UUA UAG and UGA (stop codons) to dissociate the ribosome
28
Nucleases
Can cleave phosphodiester bonds between nucleotides
29
Proteases
Enzymes breaking down protein
30
Kinases
Enzymes that add phosphate groups to other molecules
31
Phosphatases
Removes phosphate groups from protiens (opposite of kinase)
32
ATPases
Hydrolyzes ATP ATP-ADP
33
GTPases
Hydrolyze GTP
34
GEF
Swaps out GDP for GTP (facilitates GDP release)
35
GAP function
Hydrolyzes GTP to GDP
36
Phosphorylation of ser thr and tyr
drives forming of quaternary structure
37
Palmitoylation on cys
Drives protein association with membranes
38
Ubiquitine on Lys (mono)
Regulates transport of membrane proteins in vesicles
39
Ubiquitin on lys (poly)
targets protein for degredation
40
Profilin
encourages rapid binding of actin monomers to + end of actin filament, causing + end growth
41
Thymosin
Actin-thymosin complexes cannot bind to the actin filament, halting growth
42
Cofilin
Twists actin against its "grain" to encourage dissassembly
43
ARP 2/3
Branching, mimics actin seed, forming a new filament at a 70° angle to original filament (pushing out)
44
Formin
(dimer) Polymerizes actin by forming a ring around + end and grabbing monomers to add
45
Capping protein
stabilizes ends of actin to prevent both growth and decay
46
Fimbrin
Cross-linking monomer, forms close parallel bundles (not myosin friendly)
47
Alpha-actinin
Cross-linking dimer, creates anti-parallel contractile bundles (myosin friendly)
48
Filamin
Cross-linking dimer creates long, flexible connections, creates more of a supportive mesh
49
Alpha actinin is found...
... anchored to ECM to act as a pulling cable
50
Filamin is found....
... in the cell cortex as a supportive mesh
51
ARP 2/3 is found....
.... in the lamellipodium to help with extending and grabbing
52
Fimbrin and profilin are found...
... in the (stiff) filopodium to help reach and sense
53
Function of myosin light chain kinase (MLCK)
phosphorylates light chains to cause spontaneous self assembly of myosin
54
Titin
increases strength and stiffness of muscle contractions
55
Thick filament /myosin bundle (Myosin II)
Muscle shit
56
Myosin V
Cargo (longer light chains, shorter coiled coil, c-terminus chains for cargo binding)
57
Microtubule subunits are...
dimers (alpha and beta)
58
Centrosomes are
centrioles surrounded by pericentriolar material where microtubule. nucleating sites are embedded
59
MAPs
Microtubule associated proteins
60
Kinesin-13
Destabilizing - peels/bends protofilaments outward, causing breakage and catastrophe microtubuel
61
XMAP215
Stabilizing - straightens protofilaments, causing stability and growth
62
Stathmin
Bends potential additional segments, preventing growth and depolymerization
63
Katanin
Cuts microtubules in the middlw
64
MAP2
90° grid
65
tau
microtubule organization (not 90° grid)
66
Kinesins
+ end directed motor proteins (brings things to edges of cell)
67
Kinesin 1
Main vesicle transport
68
Kinesins 5, 13, and 14
cell division
69
Dyneins
- oriented motor proteins (bring things towards center of cell)
70
Kinesin ATP cycle
Leading head ADP bound, lagging ATP bound. ATP hydrolysis, lagging launches into leading position, while leading simultaneously exchanges ADP for ATP and becomes new lagging
71
Dynein movement
Inner and outer arms alternate in monkey bar movement

Cell Structure and Function (3 decks)

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