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Protein Function

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Function: To carry small molecules and ions. Example: hemoglobin ... Example: rhodopsin. Motor Proteins. Function: To generate movement in cells and tissues. ... – PowerPoint PPT presentation

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Title: Protein Function


1
Protein Function
2
Enzymatic Proteins
  • Function To catalyze covalent bond breakage or
    formation.
  • Example trypsin

3
Transport Proteins
  • Function To carry small molecules and ions.
  • Example hemoglobin

4
Structural Proteins
  • Function To provide mechanical support to cells
    and tissues.
  • Example keratin

5
Storage Proteins
  • Function To store small molecules or ions.
  • Example ovalbumin

6
Signal Proteins
  • Function To carry signals from cell to cell.
  • Example insulin

7
Receptor Proteins
  • Function To detect extracellular signals and
    transmit them to the cells response machinery
    inside.
  • Example rhodopsin

8
Motor Proteins
  • Function To generate movement in cells and
    tissues.
  • Example myosin

9
Defensive Proteins
  • Function To protect the cell against diseases.
  • Example antibodies

10
Gene Regulatory Proteins
  • Function To bind DNA in order to switch genes
    on and off.
  • Example lac repressor

11
Special Purpose Proteins
  • Function variable
  • Example green fluorescent protein

12
Enzymes
13
Enzyme Catalysis
  • What is an enzyme?
  • What is catalysis?
  • Why is enzyme catalysis important?
  • Many cellular functions require speed
  • Examples DNA replication, amino acid synthesis,
    protein modification

14
Molecule Associations
  • When a protein molecule binds to a second
    molecule, the second molecule is referred to as a
    ligand.

The region of the protein that associates with
the ligand is referred to as the binding site or
active site.
15
Molecule Associations and Catalysis
  • The protein molecule is the enzyme E
  • The ligand is called the substrate S
  • The product resulting from the action the E has
    on S is referred to as P

E S
ES
E P
16
Molecule Associations and Catalysis
  • What does E S look like?

E
S
17
Measuring the Catalytic Properties of Enzymes
  • Kd Dissociation constant ES/ES
  • Ka Association constant ES/ES

Ka
E S
ES
E P
Kd
18
Measuring the Catalytic Properties of Enzymes
E S
ES
E P
  • There is a limit to the amount of substrate a
    single enzyme molecule can process in a given
    time.
  • An increase in substrate concentration results in
    an increase in product formation up to a maximum
    value.

19
Maximum Rate of the Reaction
  • The maximum rate of the reaction or Vmax is
    reached when substrate concentration exceeds
    enzyme concentration by some amount.

20
Michaelis-Menten Equation
VmaxS
Vo
KM S
  • This equation describes the rate of a reaction.

21
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26
Serine Proteases
27
Serine Proteases
  • Definition A general class of enzymes that
    cleaves covalent peptide bonds.
  • They are called serine proteases because serine
    is the most prominent functional group in the
    active site of the enzyme.

28
Substrate Specificity
  • Cleave adjacent to positively charged amino acids.

29
Laboratory Trypsin Digest
  • Partial trypsin digestion of bovine serum albumin
    (BSA)
  • Digestion products separated by gel
    electrophoresis and then visualized.
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