biochem test 4 Gallivan
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- what influences how protein folds?
-
1) thermodynamics- determines if it is energetically favored
2) kinetics - determines how fast follding happens
3) protein fold is not random - what is a molten globule
- when molecule has folded into discrete secondary regions.
- what is the name of strucutre after it folds into tertiary structure
- native structure
- what is Ks equal to
- k-1/ k1
- what two ways can an enzyme promote a rxn
-
1) can destabalize the substrate
2) can bind to transition state and lower energy/ stabalize them - Does Vmax change in competitive inhibition?
- no because u can add enough substrate to outcompete the inhibitor.
- draw graph for what changing concentration of inhibitor in competitive inhibition affects teh line Weaver Burke graph
- p 422
- In what type of inhibition is Vmax not affected by [I]?
- competitive p422
- if Ki does not equal Ki' what type of inhibition is that
- mixed non competitive
- what amino acids does chymotripsin cleave after
- aromatic ones- phenylalanine, tyrosine, trptophan.
- what methods to enzymes use to drive foward reaction
-
1) proximetry
2) electrostatics - chymotripsin
3) covalent bonding-bacterial cell wall
4) acid/ base - chymotripsin - what do proteases do?
- hydrolize proteins
- what type of protease uses a metal ion in order to make a protein reactive?
- metallo protesase p452
- what type of enzyme is HIV protease and what are the two amino acids in its active site
- asparteal protease (homodimer)/ aspartic acids
- what are the 6 ways that enzymes are regulated
-
1) product inhibition- product of reaction builds up
2) substrate avaliability
3) genetic mechanisms
4) covalent modification- phosphorylation
5) zymogen- enzyme synthasized in inactive form
6) allosteric regulation- product in pathway will affect an earlier enzyme- pos/ neg feedback - what is the region of RNA where product can interact with it and cut off the expression
- riboswitches
- none competitive
- Vmax, Km
- competitive
- Vmax, alphaKm
- mixed non competitive
-
Vmax/ alpha' ,
(alphaKm)/alpha' - uncompetetive
- Vmax/alpha', Km/alpha'
- pure noncompetitive
- Km, Vmax/ alpha
- draw out mechanism for lysozyme reacting with sugar
- p 468