Practicum: biochemie en biotechnologie (J000496A)
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Pymol
Eiwitten = macromoleculen
Opgebouwd uit AZ
o Linker: peptidebindingen
o Centrale C, aminogroep, carboxylgroep + R-groep
o Bepalen hoe eiwit zich gaan opvormen
o Onderverdeling: niet-polaire, polaire en geladen AZ
o Niet-polaire AZ
Hydrofoob
Na opvouwing aan binnenkant eiwit
Hydrofobe deel v. eiwit vormen dat interageert
met lipidemembranen
Vaak betrokken bij hydrofobe, VdW interacties
o Polaire AZ
Hydrofiel
Na opvouwing aan opp. eiwit zitten
In contact komen met waterige extracellulaire of
intracellulaire compartimenten
Betrokken in waterverbindingen
Cysteïne vormt covalente disulfidebruggen + stabiliseert sec. structuur en
vouwing v. eiwitten
o Basische en zure AZ
Meestal pos. of neg. geladen bij fysiologische pH
Betrokken bij elektrostatische interacties
Hydrofiel
Niet-covalente en covalente interacties bepalen structuur en vouwing vd. eiwitten
o Niet-covalent: hydrofoob, hydrofiel & geladen
o Covalent: disulfidebruggen
Functies
o Transport + opslag kleine moleculen (bv. O2)
o Structurele componenten v. cellen en weefsels
o Rol bij spiercontractie
o Rol in immuunresponsen
o Rol bij bloedstolling
o Enzymen = biologische katalysatoren
Manier eiwitten worden opgevouwen, bepaalt hun
functie
o Verkeerd gevouwen eiwitten ziektes
Eiwitstructuur
o Primaire structuur
Opeenvolging van AZ
o Secundaire structuur
Conformatie vd. ruggengraat
Lokale opvouwing in herhalende
eenheden
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