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and Function
Proteins
• Make up about 15% of the cell
• Have many functions in the cell
Enzymes
Structural
Transport
Motor
Storage
Signaling
Receptors
Gene regulation
Special functions
Shape = Amino Acid Sequence
Hydrophilic Hydrophobic
Protein Folding
•Primary structure
• Amino acid sequence of the protein
•Secondary structure
• H bonds in the peptide chain backbone
• -helix and -sheets
•Tertiary structure
• Non-covalent interactions between the R
groups within the protein
•Quanternary structure
• Interaction between 2 polypeptide chains
Protein Structure
Domains
•Hemoglobin
•2 globin
subunits
•2 globin
subunits
Protein Assemblies
E + S ES EP E + P
• Step 1 – binding of the substrate
• Limiting step depending on [S] and/or [E]
• Vmax – maximum rate of the reaction
• Turnover number determines how fast the substrate
can be processed = rate of rxn [E]
• Step 2 – stabilize the transition state
• State of substrate prior to becoming product
• Enzymes lowers the energy of transition state and
therefore accelerates the reaction
Reaction Rates
• Regulation of enzymatic
pathways prevent the
deletion of substrate
• Regulation happens at
the level of the enzyme in
a pathway
• Feedback inhibition is
when the end product
regulates the enzyme
early in the pathway
Feedback Regulation
• Negative feedback –
pathway is inhibited by
accumulation of final
product
• Positive feedback – a
regulatory molecule
stimulates the activity of
the enzyme, usually
between 2 pathways
• ADP levels cause the
activation of the glycolysis
pathway to make more
ATP
Allostery
• Conformational coupling of 2 widely
separated binding sites must be responsible
for regulation – active site recognizes
substrate and 2nd site recognizes the
regulatory molecule
• Protein regulated this way undergoes
allosteric transition or a conformational
change
• Protein regulated in this manner is an
allosteric protein
Allosteric Regulation