enzymes and proteins
- Created by: Emilyburkee
- Created on: 19-04-21 13:37
View mindmap
- protein structure and enzymes
- structure
- primary
- sequece of amino acids joined by a peptide bond
- determines 2+3 structure at parts of the chain
- sequece of amino acids joined by a peptide bond
- secondary
- h bonding forming simple structures eg alpha helix or beta sheet
- tertiary
- 3D folding, interactions between groups - depends where R groups are to where bonds form
- specific structure forms function
- -disulphide bridges -ionic bond. -hydrogen bonds -hydrophobic interactions
- 3D folding, interactions between groups - depends where R groups are to where bonds form
- quaternary
- more than one polypeptide chains
- primary
- enzymes
- have specific tertiary structure meaning it has a specific active site which is complemtarty to its substrate
- forms enzyme-substrate complex - stresses bonds
- induced fit modle
- enzyme changes shape slightly to better fit substrate which stresses bonds
- conditions
- ph -can stress hydrogen bonds ect changing tertary structure - decreasing E-S complexes
- ror- increases until optimum
- temp- increased tem= increased Ke therefore more succeful collisons - more e-s complexes
- moles vibrates and breaks bonds
- substrate concerntration- more avalible to bind and form e-s complexs
- sub = more than enzyme - rate = constant
- ph -can stress hydrogen bonds ect changing tertary structure - decreasing E-S complexes
- inhibitors
- bind to enzyems and prevent formation of enzyme-substrate complexes
- competive - binds to active site
- non-competive binds to enzyme and changes tertary struture of (A~S) no longer complemtary
- structure
Comments
No comments have yet been made