1) How does alanine differ from glycine?
2) Protein shape can be changed by heat. Egg white is rich in the protein albumin. What happens to egg white when an egg is cooked, and why?
3) Is the shortage of tyrosine the cause of albinism? Explain.
4)Through recumbinant DNA techniques, bacteria have been engineered that are capable of making human insulin, human growth hormone, and a hepatitis B vaccine. These substances are proteins. Why is this significant for medical technology?
5) Bacteria used in recombinant DNA technology are specialized strains that cannot survive outside of a laboratory. Explain why this is important..
ok i understand 1 2 and 3 i just don't get 4 and 5
4) What benefit would that have for diabetics, abnormally short people and people in danger of getting hepatitis B?
5) If it cannot survive outside the laboratory, how can it be effectively used?
I hope this helps a little more.
1) Alanine and glycine are both amino acids, which are the building blocks of proteins. However, they differ in their chemical structure. Alanine is a non-polar amino acid, meaning it contains a hydrocarbon side chain, while glycine is the simplest amino acid with just a hydrogen atom as its side chain. This makes glycine more flexible compared to alanine, as it lacks a bulky side chain. Moreover, alanine is considered an essential amino acid, meaning it needs to be obtained from the diet, whereas glycine is classified as a non-essential amino acid, as our bodies can synthesize it.
To determine how alanine differs from glycine, you can compare their chemical structures and side chains. Alanine has the chemical formula C3H7NO2, and its side chain is a methyl group (-CH3) attached to the carbon atom of the amino group. On the other hand, glycine has the chemical formula C2H5NO2, and its side chain consists of just a hydrogen atom. Comparing these structures will visually illustrate their differences.
2) When egg white, which is rich in the protein albumin, is cooked, it undergoes a structural change due to heat. This change is often observable as the egg white transitions from a translucent, gel-like state to an opaque and solid form. The heating process disrupts the weak bonds holding the protein's structure together, such as hydrogen bonds and hydrophobic interactions. As a result, the protein molecules unfold and aggregate, forming a solid mass with a denser texture.
The unfolding and aggregation of proteins in egg white are driven by the denaturation process induced by heat. Denaturation involves breaking the secondary, tertiary, and quaternary protein structures, but it does not break the primary structure (the linear amino acid sequence). The heat causes the protein molecules to lose their three-dimensional shape and interact with each other, forming a network of intermolecular bonds. This network is responsible for the solidification of the egg white and the change in its texture.
3) No, the shortage of tyrosine is not the cause of albinism. Albinism is a genetic disorder caused by mutations in genes responsible for the production of melanin, the pigment that gives color to the skin, hair, and eyes. Tyrosine is an amino acid involved in the synthesis of melanin, but its shortage alone does not lead to albinism.
In albinism, mutations affect enzymes such as tyrosinase, which converts the amino acid tyrosine into melanin precursors. Without functional tyrosinase or related enzymes, melanin production is significantly reduced or completely halted, resulting in a lack of pigmentation in various tissues. It is a complex genetic condition that can vary in severity depending on the specific gene mutations affecting melanin production. Therefore, while tyrosine is a necessary component for melanin synthesis, the shortage of this amino acid alone does not cause albinism.
4) The ability to engineer bacteria to produce human insulin, human growth hormone, and vaccines like Hepatitis B using recombinant DNA technology is significant for medical technology for several reasons:
a) Availability: The production of these substances in bacteria allows for large-scale manufacturing of therapeutic proteins. Bacteria can be grown in bioreactors, which allows for cost-effective production on a much larger scale compared to traditional methods.
b) Purity and Safety: By using recombinant DNA techniques, the manufactured proteins can be produced in a highly purified form, reducing the risk of impurities or contaminants. This ensures the safety and efficacy of the therapeutic products.
c) Customization: Recombinant technology enables scientists to modify the genetic sequences of the proteins, making them more compatible with the human body. This customization allows for improved functionality, decreased side effects, and increased overall effectiveness of the therapeutic proteins.
d) Accessibility: The ability to produce these proteins in bacteria allows for easier access to essential medical treatments for patients worldwide. This technology has helped increase the availability of important drugs like insulin, making them more accessible to those in need.
Overall, the use of recombinant DNA technology in bacteria has revolutionized the production of therapeutic proteins, leading to advancements in medical technology that benefit patients globally.
5) Bacteria used in recombinant DNA technology are often genetically modified to carry specific traits, such as the ability to produce a protein of interest or replicate DNA fragments. These specialized strains are engineered to be deficient in essential nutrients, rendering them unable to survive outside of a laboratory environment. This characteristic is crucial for several reasons:
a) Safety: Engineered bacteria may contain genetic modifications that make them potentially harmful if released into the environment. By designing them to be unable to survive outside of a controlled laboratory setting, the risk of accidental release or unintended ecological consequences is minimized.
b) Contamination Prevention: The specialized strains used in recombinant DNA technology are often carefully selected to prevent contamination of natural ecosystems or other production processes. Their inability to survive outside of a controlled environment ensures that they do not interfere with other organisms or impact natural microbiota.
c) Regulatory Compliance: The containment of genetically modified organisms (GMOs) is an important aspect of biosafety regulations. Designing bacteria to be non-viable outside of a laboratory facilitates compliance with regulatory requirements, ensuring responsible and ethical usage of genetically modified strains.
d) Process Control: Limiting the survival of engineered bacteria to a controlled laboratory environment allows for better control and optimization of the production processes. By confining them to controlled settings, scientists can maintain consistent conditions, monitor growth rates, and prevent unwanted genetic spread or mutations.
In summary, the limitations placed on engineered bacteria to survive exclusively in a laboratory environment are crucial for the safety, containment, and effective utilization of recombinant DNA technology.