BMS535 Proteins And Enzymes UITM Assignment Answer Malaysia
BMS535 Proteins and Enzymes” is an advanced biochemistry course offered at UITM (Universiti Teknologi MARA) in Malaysia. This comprehensive course covers various aspects of protein and enzyme biochemistry. Students will delve into topics such as protein structure and functions, protein synthesis and purification techniques, as well as enzyme structure, kinetics, and the mechanisms of enzyme activities. The course aims to provide a thorough understanding of the fundamental principles governing proteins and enzymes, and their vital roles in biological processes. Through lectures, practical exercises, and research, students will gain valuable insights into the fascinating world of proteins and enzymes, preparing them for further studies or careers in the field of biochemistry.
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Assignment Task 1 : Explain the mechanisms of protein synthesis, protein folding and conformation and how it relates to their functions.
Protein Synthesis:
Protein synthesis is the process by which cells build proteins using the information encoded in the DNA. It occurs in two main stages: transcription and translation.
- Transcription: In the cell nucleus, the DNA is transcribed into messenger RNA (mRNA) by the enzyme RNA polymerase. During this process, the DNA strand serves as a template, and complementary RNA nucleotides (adenine, uracil, guanine, and cytosine) are added to form the mRNA strand. The mRNA contains the genetic code for the specific protein.
- Translation: The mRNA leaves the nucleus and enters the cytoplasm, where it binds to ribosomes, the cellular machinery responsible for protein synthesis. Transfer RNA (tRNA) molecules bring specific amino acids to the ribosome, guided by the codons (three-nucleotide sequences) on the mRNA. The ribosome reads the codons and links the amino acids together in the correct order, forming a polypeptide chain, which folds into a functional protein.
Protein Folding:
Once a polypeptide chain is synthesized during translation, it undergoes a process called protein folding. Proteins must fold into their correct three-dimensional structures to be functional. The folding process is driven by the protein’s amino acid sequence and various cellular factors.
- Primary Structure: The linear sequence of amino acids in a polypeptide chain is called its primary structure. This sequence determines how the protein will fold.
- Secondary Structure: The primary structure forms secondary structures like alpha helices and beta sheets through hydrogen bonding between nearby amino acids.
- Tertiary Structure: The secondary structures further fold and interact, forming the unique three-dimensional shape of the protein. Various forces such as hydrogen bonds, disulfide bridges, hydrophobic interactions, and electrostatic attractions stabilize the tertiary structure.
Protein Conformation and Function:
The specific conformation (three-dimensional shape) of a protein is essential for its function. The conformation dictates the protein’s ability to interact with other molecules and perform its biological roles. If a protein misfolds or adopts the wrong conformation, it may become non-functional or even harmful.
Examples of Protein Functions and Conformations:
- Enzymes: Enzymes are proteins that act as biological catalysts, facilitating chemical reactions in cells. The active site of an enzyme has a specific conformation that allows it to bind with substrates and catalyze reactions.
- Structural Proteins: Proteins like collagen and keratin have unique conformations that provide strength and structure to tissues like skin, hair, and nails.
- Transport Proteins: Proteins like hemoglobin have specific conformations that enable them to bind with oxygen and transport it throughout the body.
- Receptor Proteins: Receptor proteins have specific conformations that allow them to recognize and bind with signaling molecules, triggering cellular responses.
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Assignment Task 2 : Perform basic laboratory experiments on enzyme kinetics and protein purification.
As this is a practical laboratory experiment, I’ll outline the general steps and procedures for enzyme kinetics and protein purification. Keep in mind that specific experimental details may vary based on the enzyme and protein being studied.
Enzyme Kinetics:
Enzyme kinetics investigates the rate of enzymatic reactions and the factors that influence them. A common experiment involves studying the reaction rate of an enzyme-catalyzed reaction at different substrate concentrations.
Experimental Setup:Â
- Prepare a buffer solution with the appropriate pH to maintain the enzyme’s activity.
- Set up a spectrophotometer to measure the changes in absorbance during the reaction.
Enzyme Assay:
- Mix the enzyme with varying concentrations of the substrate.Â
- Incubate the reaction mixture at a specific temperature.
- At regular intervals, measure the absorbance changes at the appropriate wavelength using the spectrophotometer.
Data Analysis:Â
- Plot the initial reaction rate against the substrate concentration.
- Â Determine kinetic parameters such as the maximum reaction rate (Vmax) and the Michaelis-Menten constant (Km) using appropriate equations.
Protein Purification:
Protein purification aims to isolate a specific protein from a complex mixture and obtain it in a highly pure form.
Cell Lysis:Â
- Harvest cells expressing the protein of interest.Â
- Lyse the cells to release their contents, including the protein.
Fractionation:Â
- Â Use techniques like centrifugation to separate the cellular components based on size and density.Â
- Â The protein of interest is often found in a specific fraction.
Chromatography:Â
- Apply the fraction containing the protein of interest to a chromatography column.
- The column matrix selectively interacts with the protein, separating it from other contaminants.
Elution and Collection:
- Use specific elution conditions to release the protein from the column.
- Collect the purified protein fractions.
Analysis and Confirmation:
- Â Analyze the collected fractions using techniques like SDS-PAGE to confirm protein purity.Â
- Concentrate the purified protein, if necessary, using ultrafiltration.
Assignment Task 3 : Illustrate the mechanisms related to enzyme function, kinetics and industrial applications.
Enzyme Function and Kinetics:
- Active Site: Enzymes have specific active sites where the substrate binds, leading to catalysis. The active site’s shape and chemical properties determine substrate specificity.
- Lock-and-Key Model: The lock-and-key model describes the specific fit between the enzyme’s active site (the lock) and the substrate (the key).
- Induced Fit Model: The induced fit model suggests that the enzyme’s active site undergoes conformational changes upon substrate binding to achieve an optimal fit.
- Enzyme Inhibition: Enzyme activity can be regulated through competitive, non-competitive, or uncompetitive inhibition, affecting the enzyme’s ability to bind with substrates.
Industrial Applications:
Enzymes find extensive use in various industrial applications due to their specificity and efficiency:
- Food Industry: Enzymes are used in food processing, such as converting starch to sugars, clarifying fruit juices, and improving bread texture.
- Detergent Industry: Protease enzymes are used in laundry detergents to remove protein-based stains.
- Pharmaceutical Industry: Enzymes are used in drug manufacturing, including the production of antibiotics and biopharmaceuticals.
- Biofuel Production: Enzymes are employed to convert biomass into biofuels like ethanol.
- Textile Industry: Enzymes are used for fabric softening and biostoning, giving a worn-out look to denim garments.
In conclusion, understanding the mechanisms of protein synthesis, folding, and conformation is crucial to comprehend how proteins acquire their functions. Enzyme kinetics and protein purification experiments provide valuable insights into enzyme behavior and are essential in both research and industrial applications. Enzymes’ diverse roles make them valuable tools in numerous industries, contributing to more sustainable and efficient processes.
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