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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
none competitive
Vmax, Km
Vmax, alphaKm
mixed non competitive
Vmax/ alpha' ,

Vmax/alpha', Km/alpha'
pure noncompetitive
Km, Vmax/ alpha
draw out mechanism for lysozyme reacting with sugar
p 468

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