Proteins Flashcards
Subunits
Amino Acids
Amino Acids general structure
Amino group, variable side chain, carboxyl group
How many different amino acids are there
@0
What elemnts do Amnio Acids contain
Carbon Hydrogen Oxygen Nitrogen and sometimes Sulfur
2 amino acids make a
dipeptide
Bond in a dipeptide
peptide bond
Structures of a protein
Primary
Secondary
Tertiary
Quaternary
Primary structure
Sequence of amino acids in the polypeptide chain
Primary structure bonds
Peptide bonds
Secondary structure
Initial folding of a polypeptide chain
Alpha helix and Beta pleated sheets
Secondray structure bonds
Hydrogen bonds
Tertiary structure
Further folding to give the fianl 3D form
Tertiary structure bonds
Hydrogen bonds
Disulphide bonds
Ionic bonds
Hydrophobi/hydrophilic interactions
Quaternary structure
Many polypeptide chains in tertiary structure together
Prostectic group
Some proteins have non proteins groups attached
Fibrous proteins
Long fibres/sheets
Insoluble in proteins
Structural role
Globular proteins
Spherical/globe like
Soluble in water
Biomedical functions (enzymes)
metabolic function
Denaturation
Permanent change in shape
Temperature
weak bonds are broken
alters tertiary structure so unable to carry out function
pH
disrupt hydrogen and ionic bonds
alters tertairy structure
unable to cary out functions
Enzymers Are Proteins
Enzymers Are Proteins
Enzymes
Biologicalcatalysts
increase rate of reaction
Activation Energy
minimum amount of energy required for a reaction to occur
How do enzymes affect Activation Energy
enzymes lower the activation energy
allows reactions to take place in the body
Lock and Key
Substrate is completly complementary in shape to the enzymes active site
Perfect fit
No change in shape
Induced Fit
Substrate and Active site are complementary but not completly
Not an exact match
Slight change in shape
pH of a solution
Measure of its hydrogen ion concentration
Calculating pH
pH = -log10[H+]
[H+] = 10^-pH
Measure enzyme activity
Formation of products
or
disappearance of substrate
Enzyme-Substate Complexes
Enzyme-Substate Complexes
Rate
change / time
change in y / change in x
For a reaction to occur
Must be contacts between sunstarte and active site of enzyme
Increase Contact
increase temperature
increase concentration of substrate
increase concentration of enzyme
Competative Inhibitor
Different molecule with the same shape
binds to active site instead of substare
stops formation of enzyme-substate complexes
Non Competative Inhibitor
Molecule binds to enzyme at the allosteric site
changes active site shape
substrate can no longer fir and bind
stops formation of enzyme-substrate complexes
Enzyme Activation
molecule can bind as an inhitior but instead of stopping the formation of enzyme-substrae complexes
it allows binding and actiavtes the enzyme for enzyme-substare completes to form
