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Biochemie Deel 1: hfdst. 3

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  • Course
  • Biochemie
  • Institution
  • Vrije Universiteit Brussel (VUB)

Dit document bevat de ppt presentaties van hoofdstuk 3 en de daarbij horende notities.

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Document information

  • March 28, 2016
  • 10
  • 2015/2016
  • Class notes
  • Unknown
  • Biochemie van de inspanning

Subjects

  • biochemie
  • barel

Written for

  • Vrije Universiteit Brussel (VUB)
  • Revalidatiewetenschappen en kinesitherapie
  • Biochemie
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Prof. Barel



Hoofdstuk 3. Hemoglobine voorbeeld van allosterisch eiwit

 Ruimtelijke structuur van Hemoglobine. Tetrameer. alfa 2 beta 2.
 Homologie in de sekwentie van de Myoglobine polypeptide keten en de alfa en
beta ketens.
 Sigmoïdale verzadigingskromme van Hemoglobine. Allosterisch effect.
 Invloed van pH en CO2 op de bindingskromme met O2
 Invloed van het Difosfoglycerolzuur DPG op de bindingskromme met O2.

 In de spieren kunnen er kleine veranderingen in PH gebeuren wanneer er veel
melkzuur wordt geproduceerd. Er moet zuurstof vrijkomen => Zuurstof komt vrij
wanneer ph daalt.

Structuur van Hemoglobine

 Hemoglobine is gevormd uit 2 alfa ketens ( 141 aminozuren) en 2 beta ketens
(146 aminozuren).
 De 4 ketens zijn georiënteerd zoals de 4 toppen van een tetraëder.
 Compacte structuur gevormd door de 4 polypeptide ketens. Holte in het midden
van de molecule.
 Wisselwerkingen tussen de alfa en de beta ketens.


Structuur van hemoglobine

 Roos: alfa
 Geel: beta




Homologie in de primaire structuur van Myoglobine en de alfa en beta ketens van
Hemoglobine

Als men de sekwenties van de 3 eiwitten vergelijkt observeert men dat:
 Op bepaalde plaatsen identische aminozuren ( His, Leu, enz..) voorkomen.
 Op talrijke plaatsen similaire aminozuren (vervanging van Leu door Ileu b.v.)
aanwezig zijn.



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