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