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Cell Structure and Function > Exam I > Flashcards

Exam I Flashcards

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
Q

Elongation factors - EUKS

A

EF1 and EF2

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26
Q

what do elongation factors do?

A

increase speed and accuracy of translation

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27
Q

Binding release factor

A

binds to UUA UAG and UGA (stop codons) to dissociate the ribosome

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28
Q

Nucleases

A

Can cleave phosphodiester bonds between nucleotides

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29
Q

Proteases

A

Enzymes breaking down protein

30
Q

Kinases

A

Enzymes that add phosphate groups to other molecules

31
Q

Phosphatases

A

Removes phosphate groups from protiens (opposite of kinase)

32
Q

ATPases

A

Hydrolyzes ATP
ATP-ADP

33
Q

GTPases

A

Hydrolyze GTP

34
Q

GEF

A

Swaps out GDP for GTP (facilitates GDP release)

35
Q

GAP function

A

Hydrolyzes GTP to GDP

36
Q

Phosphorylation of ser thr and tyr

A

drives forming of quaternary structure

37
Q

Palmitoylation on cys

A

Drives protein association with membranes

38
Q

Ubiquitine on Lys (mono)

A

Regulates transport of membrane proteins in vesicles

39
Q

Ubiquitin on lys (poly)

A

targets protein for degredation

40
Q

Profilin

A

encourages rapid binding of actin monomers to + end of actin filament, causing + end growth

41
Q

Thymosin

A

Actin-thymosin complexes cannot bind to the actin filament, halting growth

42
Q

Cofilin

A

Twists actin against its “grain” to encourage dissassembly

43
Q

ARP 2/3

A

Branching, mimics actin seed, forming a new filament at a 70° angle to original filament (pushing out)

44
Q

Formin

A

(dimer) Polymerizes actin by forming a ring around + end and grabbing monomers to add

45
Q

Capping protein

A

stabilizes ends of actin to prevent both growth and decay

46
Q

Fimbrin

A

Cross-linking monomer, forms close parallel bundles (not myosin friendly)

47
Q

Alpha-actinin

A

Cross-linking dimer, creates anti-parallel contractile bundles (myosin friendly)

48
Q

Filamin

A

Cross-linking dimer creates long, flexible connections, creates more of a supportive mesh

49
Q

Alpha actinin is found…

A

… anchored to ECM to act as a pulling cable

50
Q

Filamin is found….

A

… in the cell cortex as a supportive mesh

51
Q

ARP 2/3 is found….

A

…. in the lamellipodium to help with extending and grabbing

52
Q

Fimbrin and profilin are found…

A

… in the (stiff) filopodium to help reach and sense

53
Q

Function of myosin light chain kinase (MLCK)

A

phosphorylates light chains to cause spontaneous self assembly of myosin

54
Q

Titin

A

increases strength and stiffness of muscle contractions

55
Q

Thick filament /myosin bundle (Myosin II)

A

Muscle shit

56
Q

Myosin V

A

Cargo (longer light chains, shorter coiled coil, c-terminus chains for cargo binding)

57
Q

Microtubule subunits are…

A

dimers (alpha and beta)

58
Q

Centrosomes are

A

centrioles surrounded by pericentriolar material where microtubule. nucleating sites are embedded

59
Q

MAPs

A

Microtubule associated proteins

60
Q

Kinesin-13

A

Destabilizing - peels/bends protofilaments outward, causing breakage and catastrophe
microtubuel

61
Q

XMAP215

A

Stabilizing - straightens protofilaments, causing stability and growth

62
Q

Stathmin

A

Bends potential additional segments, preventing growth and depolymerization

63
Q

Katanin

A

Cuts microtubules in the middlw

64
Q

MAP2

A

90° grid

65
Q

tau

A

microtubule organization (not 90° grid)

66
Q

Kinesins

A

+ end directed motor proteins (brings things to edges of cell)

67
Q

Kinesin 1

A

Main vesicle transport

68
Q

Kinesins 5, 13, and 14

A

cell division

69
Q

Dyneins

A
  • oriented motor proteins (bring things towards center of cell)
70
Q

Kinesin ATP cycle

A

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
Q

Dynein movement

A

Inner and outer arms alternate in monkey bar movement

Cell Structure and Function (3 decks)

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