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Samenvatting Protein Structure and Dynamics NL $5.45   Add to cart

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Samenvatting Protein Structure and Dynamics NL

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De samenvatting is gebaseerd op de hoorcolleges aangevuld met de literatuur.

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  • November 7, 2021
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  • 2019/2020
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Maandag 9 september 2019
Protein Structure & Dynamics
Lill, H

2.1 Amino Acids

- The general structural properties of amino acids
- Chirality of amino acids
- The chemical classes of amino acids, their determining features, and which amino
acids belongs to which class

Structuur is bepalend voor functie.

Aminozuren
- Aminegroep (belangrijk in de oplossing)
- Zuurgroep (carboxylgroep, belangrijk in de oplossing)
- aC-atoom (centraal)
- Zijketen (bepaalt de chemische eigenschappen van het aminozuur)

Zwitter-ion: zowel positieve als negatieve ladingen (fysiologisch pH)

Chiraal koolstofatoom: 4 verschillende groepen

Klassen: onderscheiding in zijketen!
- Negatief geladen aminozuren: zijketen met carboxylgroep: COO-
- Positief geladen aminozuren: zijketen met aminegroep: NH 2 kan proton opnemen >
NH3+)
- Niet geladen (wel polaire) aminozuren: zijketen met hydroxyl groep -OH
- Hydrofobe (niet polaire) aminozuren: zijketen zit alleen C en H

2.2 Protein structure

- How amino acids polymerize to build peptides
- The four niveaus of protein structure and their characterizing features
- What motifs and domains are

Prionen: eiwitten die hun structuur kwijtraken, worden meestal afgebroken op opgeruimd in
het lichaam. Bij prionen worden gezonde eiwitten ook ‘besmet’ met de verkeerde structuur
> celdood.

Voobeeld: Alzheimer’s, Kanker (eiwit: P53), Cystis fibrosis.
P53 checkt de eiwitten in ons lichaam. Fout > ruimt foute cel op. Als P53 zelf muteert, doet
die het niet meer. De controle is uitgeschakeld. De mutatie zelf leidt niet voor kanker, maar
wel als de controleur gemuteerd wordt.

- Primaire structuur: sequentie van aminozuren die een polypeptide (macromolecuul)
vormen. Aminozuren zijn verbonden door peptidebindingen (condensatiereactie), er

1

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