Protein Therapeutics Exam
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Protein Therapeutics Exam

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Questions and Answers

What is the mechanism of enzyme regulation involving the attachment of a phosphate group to an enzyme?

Phosphorylation

What is the term for the process by which an enzyme is broken down?

Degradation

What is the change in free energy (ΔG) associated with a favourable chemical reaction?

A drop in free energy

What type of molecule can compete with substrates for binding to an enzyme active site?

<p>Small molecules</p> Signup and view all the answers

What is the term for the process by which an enzyme is synthesized?

<p>Synthesis</p> Signup and view all the answers

What is the function of DNA polymerase in genome replication?

<p>To create a copy of the genome</p> Signup and view all the answers

What is the term for the process by which an enzyme is modified after translation, such as through the addition of a phosphate group?

<p>Posttranslational modification</p> Signup and view all the answers

What is the function of the spliceosome in gene expression?

<p>To remove introns and join exons</p> Signup and view all the answers

What is the term for the high-energy state that reactants pass through during a chemical reaction?

<p>Transition state</p> Signup and view all the answers

What is the function of the ribosome in protein translation?

<p>To synthesize polypeptide chains</p> Signup and view all the answers

Study Notes

Protein Therapeutics

  • Proteins can be developed and produced to serve specific therapeutic functions, such as treating metabolic disorders, resisting infections, and arresting the spread of cancer.
  • Protein-based drugs can be grouped into four categories based on their pharmacological activity:
    • Group 1: therapeutics with enzymatic or regulatory activity
    • Group 2: therapeutics with special targeting activity
    • Group 3: vaccines
    • Group 4: diagnostic agents
  • Protein therapeutics have several advantages over small-molecule drugs, including:
    • highly specific and complex functions that cannot be mimicked by simple chemical compounds
    • less potential for interference with normal biological processes and adverse effects
    • well-tolerated and less likely to elicit immune responses
    • effective replacement treatment for diseases with mutated or deleted genes
    • faster clinical development and FDA approval time
    • unique form and function, allowing for far-reaching patent protection
  • The first recombinant protein used in therapy was insulin, which was purified from bovine pancreas in 1922 and later produced through genetic engineering in E. coli bacteria in 1978.

Challenges of Recombinant Proteins

  • Storage, distribution, and understanding of protein properties (solubility, ability to enter the body, stability)
  • Degradation of proteins through lysosome, proteosome, or protease action
  • Immune response, which can neutralize the effect of the introduced protein or cause severe effects
  • Administration of active protein/enzyme in active conformation, considering post-translational modifications
  • Cost and time-consuming process of producing recombinant proteins
  • Ethical issues in investing in research for rare diseases versus widely distributed diseases

Enzymatic Catalysis

  • Enzymes are biological catalysts made of proteins that accelerate chemical reactions without heating.
  • Enzymes are:
    • efficient, with acceleration rates of up to 17 orders of magnitude
    • substrate-specific, with active sites that complement the substrate geometrically and electrostatically
    • reaction-specific, catalyzing a single reaction
  • There are six classes of enzymes:
    • Oxidation-reduction class (catalyzes oxidoreduction reaction)
    • Group transfer class (catalyzes transfer of a chemical group from one molecule to another)
    • Hydrolysis class (catalyzes reaction in which a molecule is broken down using a water molecule)
    • Water-independent lysis class (catalyzes reaction hydrolysis of a molecule without a water molecule)
    • Isomerisation class (catalyzes isomerization of a chemical group or double bond)
    • Ligation class (catalyzes binding of two molecules, often coupled with energy consumption by hydrolysing ATP)
  • Enzymes can be classified using the Enzyme Classification (E.C) system, which assigns a 4-digit number indicating the class, reaction, and specific information.
  • Enzymes can:
    • couple energy-demanding reactions to ATP hydrolysis
    • be regulated through means such as small molecules, phosphorylation, degradation, synthesis, and post-translational modifications
    • create large molecular machines for carrying out complex tasks

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Description

This exam assesses knowledge on protein therapeutics, including their development, production, and functions in treating various diseases and disorders. It may include multiple-choice and open-ended questions, as well as lab experience and drawing of amino acid residues.

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