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Samenvatting biochemie 1e jaar BMWtem H5
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Samenvatting biochemie tem h5 1e jaar BMW prof. Johan Van Lint
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Inhoud1. Biomoleculen ................................................................................................................................... 4
I. Basiseigenschappen aminozuren ................................................................................................ 4
Non-polair met alifatische R-groepen ............................................................................................. 4
Aromatische R-groepen................................................................................................................... 4
Negatieve R-groepen ....................................................................................................................... 5
Polaire ongeladen R-groepen .......................................................................................................... 5
Positieve R-groepen ........................................................................................................................ 6
II. Basiseigenschappen suikers ........................................................................................................ 7
Mono- en disachariden ................................................................................................................... 7
Suikerderivaten ............................................................................................................................... 8
Polysachariden ................................................................................................................................ 8
Glycoconjugaten ............................................................................................................................ 10
Lectines .......................................................................................................................................... 10
III. Basiseigenschappen lipiden................................................................................................... 11
Vetzuren ........................................................................................................................................ 11
Triglyceriden .................................................................................................................................. 12
Glycerofosfolipiden ....................................................................................................................... 12
Sfingolipiden .................................................................................................................................. 12
Sterolen ......................................................................................................................................... 13
Lipiden enkel een structurele rol? ................................................................................................. 13
2. Basisbegrippen van de bio-energetica .......................................................................................... 14
I. Welk soort arbeid moeten cellen verrichten ............................................................................ 14
II. Welke energieomzettingen en moleculaire omzettingen gebeuren er in een cel om arbeid te
verrichten? ........................................................................................................................................ 14
III. Energie tijdelijk opslaan..................................................................................................... 14
IV. Hoe kunnen ongunstige reacties toch doorgaan? ................................................................ 15
V. Hoe spontane reacties met hoge activeringsenergie sneller laten verlopen? .......................... 15
VI. Welk thermodynamisch systeem hoort bij een levend organisme? ..................................... 16
VII. Nut van ‘vrije energie’ voor redeneringen over levende organismen .................................. 16
Waarom ATP zo energierijk ........................................................................................................... 17
VIII. Hoge-energieverbindingen ........................................................................................................ 17
1. Wat zijn hoge-energieverbindingen .......................................................................................... 17
2. Waarom is ATP een hoge-energieverbinding............................................................................ 17
3. Wat is de rol van verbindingen met nog hogere energie dan ATP............................................ 17
1
,IX. Waarom en hoe oxideren wij voedingsmoleculen .................................................................... 18
1. Waarom onttrekken wij elektronen aan voedingsmoleculen ................................................... 18
2. Welke moleculen kunnen optreden als elektronencarriers ...................................................... 18
3. Eiwitten.......................................................................................................................................... 19
I. Wat zijn de vier niveaus van eiwitstructuur .............................................................................. 19
Primaire structuur ......................................................................................................................... 19
Secundaire structuur ..................................................................................................................... 19
....................................................................................................................................................... 22
Tertiaire structuur ......................................................................................................................... 22
Quaternaire structuur ................................................................................................................... 24
II. Hoe vouwen eiwitten op? ......................................................................................................... 24
Proteïnedenaturatie-renaturatie-experimenten van Anfinsen..................................................... 25
Door welke krachten wordt het vouwen van eiwitten bepaald? .................................................. 25
Kunnen eiwitten altijd spontaan vouwen? ................................................................................... 26
Foutief vouwen van eiwitten kan ziekten veroorzaken ................................................................ 28
IV. Hoe werken eiwitten ....................................................................................................... 29
* Eiwitten werken door binding aan liganden ......................................................................... 29
Eiwitwerking door binding aan andere moleculen ....................................................................... 30
Antistoffen – binding door doorgedreven complimentariteit ...................................................... 31
Proteïne-interacties gemoduleerd door chemische energie ........................................................ 32
....................................................................................................................................................... 32
5. Enzymen ............................................................................................ Error! Bookmark not defined.
I. Wat is een enzym ...................................................................................................................... 33
Wat doet een enzym ..................................................................................................................... 33
Hoe is een enzym opgebouwd ...................................................................................................... 33
Hoe worden enzymen geclassificeerd? ......................................................................................... 34
II. Hoe bevorder je enzymreacties? ............................................................................................... 34
Via optimale binding aan het substraat in zijn transitietoestand ................................................. 34
Via zuur-base effecten................................................................................................................... 35
Via vorming covalente intermediairen .......................................................................................... 35
Via elektrostatische effecten ......................................................................................................... 35
Via gebruik van metalen ................................................................................................................ 36
III. Hoe kun je de werking van enzymen kwantificeren?............................................................ 36
Welke factoren bepalen de snelheid van gekatalyseerde reacties ............................................... 36
Michaelis-Mentenvergelijking ....................................................................................................... 36
Hoe kinetische parameters gebruiken om effect van enzyminhibitoren te kwantificeren .......... 37
2
,IV. Hoe kan de werking van een enzym geregeld worden ......................................................... 38
Allosterische regeling .................................................................................................................... 38
Regeling door fosforylatie ............................................................................................................. 38
Regeling door proteolyse .............................................................................................................. 38
Interactie met G-proteïnen ........................................................................................................... 39
Regeling door beïnvloeding van expressie van enzym of benodigde subeenheden .................... 40
Regeling via compartimentalisatie ................................................................................................ 40
Regeling via de vorming van multi-enzymcomplexen ................................................................... 41
V. Klinisch belang enzymen ........................................................................................................... 41
Diagnostische belang ..................................................................................................................... 41
Therapeutisch belang .................................................................................................................... 41
Pathofysiologisch belang ............................................................................................................... 42
3
, 1. Biomoleculen
I. Basiseigenschappen aminozuren
Non-polair met alifatische R-groepen
Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu)
o Non polair o Non polair
o Niet -asymmetrisch o Inerte alifatische zijketen
o Kleinst o Hydroob
o Conformationele o Zijketens willen samenclusteren -> stabieler
flexibiliteit -> geen
zijketen
Isoleucine (Ile) Methionine (Met)
Aromatische R-groepen
Fenylalanine (Phe) Tyrosine (Tyr) Tryptophan (Trp)
o Apolair o Intermediair polair (-OH) o Intermediair polair (N)
o Niet reactief o -OH: H-bruggen, o Zeldzaam
o ++ hydrofoob enzymen, fosforylatie o Grootste zijketen
voor signaaltransductie
Spectrofotometrie -> absorptie UV-licht
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