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Medicinsk Biokemi & Cellbiologi > 2 Livets Kemi > Flashcards

2 Livets Kemi Flashcards

1
Q

Cytoskelett

A

Ger stadga/ form

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2
Q

Lysosom

A

Nedbrytning

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3
Q

Endosom

A

Innehåller endocyterat material och sorterar det

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4
Q

Peroxisom

A

Nedbrytning/ metabolism

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5
Q

Cellmembran

A

Skyddar cellen/ avgräsning/ transport

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6
Q

Golgi

A

Bearbetning och sortering från ER samt modifiering

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7
Q

Ribosomer

A

Binder aminosyror till protein

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8
Q

ER

A

Producerar protein

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9
Q

Kromatin

A

Genetiska materialet

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10
Q

Mitokondrie

A

Energiproduktion av ATP

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11
Q

Nukleus

A

Innehåller det genetiska materialet

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12
Q

Heterokromatin

A

Saknar replikation

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13
Q

Eukromatin

A

Det mindre kondenserade kromatinet med replikerande förmåga

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14
Q

Puriner

A

Adenin och Guanin

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15
Q

Pyrimidiner

A

Tymin och Cytosin

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16
Q

Primär struktur

A

Aminosyra sekvensen

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17
Q

Sekundär struktur

A

α helix och β lamell

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18
Q

Tertiär struktur

A

Folding in 3 dimensions

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19
Q

Kvartär struktur

A

Två eller fleravpeptid bindningar binds tillsammans till dimer till stora komplex

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20
Q

Peptidbindning

A

Bindning mellan karboxyl och amino gruppen. Hydrolys (en H2O försvinner)

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21
Q

φ och ψ

A

Bestämmer sekundära strukturen.

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22
Q

Ramachandran plot

A

Backbone conformation.

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23
Q

α helix

A

Cylinder. Side chains pekar ut från helixen och avgör hydro-fob/fil egenskap.

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24
Q

β lamell

A

Kan vara parallel/ anti- parallel eller mixed.

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25
Q

β turn

A

Loop mellan β sheets. Styv.

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26
Q

Hydrophobic effect

A

Hydrophobic side chaims are hidden in the hydrophobic core that stabilizes the tertiary structure

27
Q

Isoelectric point, (pI)

A

The pH at which the protein has no net charge.

28
Q

pH < pI

A

Protein has net positive charge

29
Q

pH > pI

A

Protein has net negative charge

30
Q

TIM barrel fold

A

Parallel β sheet, closed. Connected by α helixes.

31
Q

Kofaktor

A

Prostetisk grupp. Kovalent bunden till proteinet.

32
Q

Native structure

A

Functional in vivo structure

33
Q

Active site

A

Part of protein where functional amino acids are arranged

34
Q

Coil

A

Unstructured part of folded protein

35
Q

Coiled coil

A

Special tertiary structure of a protein

36
Q

Random coil

A

Unfolded state of a protein

37
Q

Domain

A

Protein that folds independentely

38
Q

Family

A

Proteins related in evolution, similiar sequence/structure; can have structural or functional meaning.

39
Q

Fold

A

3D arrangement of secondsry structures.

40
Q

Globular structure

A

Ball like structure of soluble proteins.

41
Q

Residue

A

Amino acid in protein

42
Q

Subunit

A

Part of quarternary structure.

43
Q

Turn

A

Protein part connecting secondary structure elements.

44
Q

Levinthal paradox

A

Folding is not a random process

45
Q

Folding path.

A

Nucleation: One secondary structure element forms first, rest attaches to it.
Diffusion/ collision: Secondary structure forms first -> 3’
Hydrophobic collapse: Protein becomes compact first, them secondary structures form.

46
Q

Chaperones

A

Help proteins that don’t fold fast enough to their folded state fold.

Bind unfolded states snd prevent them from precipitating.

Can unfold missfolded proteins using energy.

47
Q

Apoenzym

A

Enzym utan kofaktor

48
Q

Holoenzym

A

Enzym med kofaktor

49
Q

[S] = KM

A

Enzymet jobbar med halva maxhastigheten

50
Q

Vmax

A

Enzymet är mättat med Substratet

51
Q

kcat

A

Maxhastighet per molekyl. dvs. Hur många molekyler (P) ett enzym maximalt kan producera varje sekund.

52
Q

Högt KM

A

Lätt dissociation = svag bindning

53
Q

Lågt KM

A

Svår dissocistion = stark bindning

54
Q

KM och kcat betydelse

A 
KM = hur starkt enzymet binder substratet 
kcat = hur snabbt enzymet kan arbeta
55
Q

Reglering av enzymaktivitet

A
  1. Tillgång på S
  2. Tillgång på E
  3. Aktiviteten hos E (Kovalent reglering & Alloster reglering)
  4. pH/temperatur
  5. Inhibering av aktivitet
56
Q

Kovalent reglering

A

•Kemisk modifiering av aminosyror, fosforylering: överföring av fosfatgrupp från ATP till sidokedjor av serin, treonin, tyrosin.

E + ATP —> (kinase) —> E-P + ADP
reaktion mot vänster (fosfatas)

•Proteolytisk reglering: E kan bildas som inaktivt förstadie. Aktiveras nör det klyvs av proteas.

57
Q

Alloster reglering

A

Bindning av effektormolekyl till alloster yta kan antingen aktivera eller hämma enzymet. Strukturen på aktuva ytan ändras av alloster bindning.

58
Q

Kooperativitet

A

Kräver multimert enzymkomplex.

Bindning av S till active site i en subenhet => andra subenhetens active site binder lättare substrat.

59
Q

Inhibitor

A

Molekyl som sänker eller helt slår av ett enzyms aktivitet

60
Q

Irreversibel inhibitor

A

Binder kovalent till E => slår av E permanent

61
Q

Reversibel inhibitor

A

Hämmar E när bunden, men kan lossna igen.

62
Q

Kompetitiv inhibitor

A

Reversibel inhibitor som tävlsr med S om bindning till E.

63
Q

Enzymklasser

A 
Oxidoreduktader
Transferaser
Hydrolaser
Lyaser
Isomeraser
Ligaser

Medicinsk Biokemi & Cellbiologi (7 decks)

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