2 Livets Kemi Flashcards

(63 cards)

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
β turn
Loop mellan β sheets. Styv.
26
Hydrophobic effect
Hydrophobic side chaims are hidden in the hydrophobic core that stabilizes the tertiary structure
27
Isoelectric point, (pI)
The pH at which the protein has no net charge.
28
pH < pI
Protein has net positive charge
29
pH > pI
Protein has net negative charge
30
TIM barrel fold
Parallel β sheet, closed. Connected by α helixes.
31
Kofaktor
Prostetisk grupp. Kovalent bunden till proteinet.
32
Native structure
Functional in vivo structure
33
Active site
Part of protein where functional amino acids are arranged
34
Coil
Unstructured part of folded protein
35
Coiled coil
Special tertiary structure of a protein
36
Random coil
Unfolded state of a protein
37
Domain
Protein that folds independentely
38
Family
Proteins related in evolution, similiar sequence/structure; can have structural or functional meaning.
39
Fold
3D arrangement of secondsry structures.
40
Globular structure
Ball like structure of soluble proteins.
41
Residue
Amino acid in protein
42
Subunit
Part of quarternary structure.
43
Turn
Protein part connecting secondary structure elements.
44
Levinthal paradox
Folding is not a random process
45
Folding path.
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
Chaperones
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
Apoenzym
Enzym utan kofaktor
48
Holoenzym
Enzym med kofaktor
49
[S] = KM
Enzymet jobbar med halva maxhastigheten
50
Vmax
Enzymet är mättat med Substratet
51
kcat
Maxhastighet per molekyl. dvs. Hur många molekyler (P) ett enzym maximalt kan producera varje sekund.
52
Högt KM
Lätt dissociation = svag bindning
53
Lågt KM
Svår dissocistion = stark bindning
54
KM och kcat betydelse
``` KM = hur starkt enzymet binder substratet kcat = hur snabbt enzymet kan arbeta ```
55
Reglering av enzymaktivitet
1. Tillgång på S 2. Tillgång på E 3. Aktiviteten hos E (Kovalent reglering & Alloster reglering) 4. pH/temperatur 5. Inhibering av aktivitet
56
Kovalent reglering
•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
Alloster reglering
Bindning av effektormolekyl till alloster yta kan antingen aktivera eller hämma enzymet. Strukturen på aktuva ytan ändras av alloster bindning.
58
Kooperativitet
Kräver multimert enzymkomplex. | Bindning av S till active site i en subenhet => andra subenhetens active site binder lättare substrat.
59
Inhibitor
Molekyl som sänker eller helt slår av ett enzyms aktivitet
60
Irreversibel inhibitor
Binder kovalent till E => slår av E permanent
61
Reversibel inhibitor
Hämmar E när bunden, men kan lossna igen.
62
Kompetitiv inhibitor
Reversibel inhibitor som tävlsr med S om bindning till E.
63
Enzymklasser
``` Oxidoreduktader Transferaser Hydrolaser Lyaser Isomeraser Ligaser ```