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BME361 Advanced Experimental Biomedical Laboratory Proficiency SUSS Assignment Sample Singapore

This course will equip you with the necessary skills to experimentally study proteins in real life situations. You’ll learn how to express them and analyze their expression patterns using up-to-date technology, as well as submitting a research paper.

The experimental skills course that continues from BME261, Advanced Experimental Biomedical Laboratory Proficiency will teach you all about expression and induction analysis of a researcher’s work in biomedical engineering. The practical problems are real-life healthcare related tasks which equip students with necessary thinking abilities for research papers they submit to publishable journals!

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Get Solved Assignment Sample For BME361 Advanced Experimental Biomedical Laboratory Proficiency SUSS Singapore

This is an assignment sample for BME361 Advanced Experimental Biomedical Laboratory Proficiency. The goal of this course, as its name suggests, entails a deep understanding and application in the lab settings based on research findings from biomedical disciplines such as physiology or genetics which can help us better understand human health problems like diabetes among others things!

Assignment Brief 1: Illustrate protein refolding, protein structure and bioinformatics analysis

Protein refolding is the process by which a protein molecule is denatured and then renatured into its original three-dimensional conformation. This occurs when a protein is exposed to an environment that is different from the one in which it was created, such as extreme heat, acidity, or salinity. The protein structure is maintained by the hydrophobic interactions between the amino acids that make up the backbone of the molecule.

Bioinformatics analysis is a means of studying and understanding the structure and function of proteins through their genetic code. This type of analysis relies on sophisticated computer programs that can decipher the sequence of codons in DNA and translate them into amino acids. The process of creating these amino acids is called translation, and the resulting protein molecule is a product of this translation.

Bioinformatics analysis can be used to determine whether or not a protein will have the same structure in every environment it encounters. Incorrect folding due to changes in temperature, acidity, or salinity can lead to serious complications, including the development of fatal diseases.

The translation process is a step-by-step method for converting genetic information into proteins that can function in a cell. The codons on a DNA strand are copied three at a time during this process, and these triplets are assigned to specific amino acids by the messenger RNA (mRNA). Each protein has a unique sequence of amino acids, and this is what determines its three-dimensional structure.

The primary determinant factor for protein folding is the hydrophobic effect. This type of interaction occurs when nonpolar molecules are brought into an aqueous environment, such as water.

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Assignment Brief 2: Analyze SDS PAGE

SDS PAGE is a technique used in molecular biology to separate proteins by their size. SDS stands for sodium dodecyl sulfate, a detergent that dissolves proteins and causes them to unfold. When proteins unfold, they lose their 3-dimensional structure and become single strands of amino acids called polypeptides.

The polypeptides are then run through a gel, which separates them according to their size. Larger polypeptides move more slowly through the gel than smaller ones, and so they are separated into bands that can be seen with an ultraviolet light microscope.

Theoretically, there are at least 10000 different proteins in a given cell. In practice this number is under 1000 because most proteins have a similar size and so cannot be readily differentiated from each other.

This technique was successfully used by James D. Watson and Francis Crick to determine the structure of DNA. By 1953, they had collected X-ray diffraction data suggesting that DNA has a repeated structure and they proposed helical and double-helical structures to account for the repeating pattern.

Assignment Brief 3: Examine the basics of protein-protein interaction

Protein-protein interactions (PPIs) are the physical and chemical contacts between proteins. The contact can be direct, as in a close contact between two protein molecules, or indirect, as mediated by other molecules such as water or ions. PPIs play important roles in many cellular processes, including protein folding, enzyme catalysis, DNA replication and transcription.

The strength of a PPI is determined by the number of hydrogen bonds and salt bridges that form between the interacting proteins. Hydrogen bonding is the strongest type of interaction and salt bridging is the weakest. The stability of a PPI is also affected by its solvent environment. Proteins that interact with each other in an aqueous environment are more stable than those that interact in an organic solvent.

The potential for a PPI is dictated by the structure of its components, as PPIs are often mediated by protein residues that form or interact with a particular secondary or tertiary structure within the protein complex. Some examples include:

In addition to residue-level interactions, PPIs can occur at different levels of protein structure, which are determined by the degree of folding of a protein complex. The most common types are antiparallel structures, parallel α-helical structure and

The various levels at which PPIs can occur are often referred to as “interactome” or “protein-protein interactome”, terms that were first introduced by Edward Marcotte and Lawrence Rawlings and originally referred to the structure and interactions of a single, two-component protein complex. The term “protein interactome” has recently been extended to include all PPIs within a cellular environment, especially when there is more than one interacting protein complex.

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Assignment Brief 4: Prepare protein purification using affinity chromatography, basic cell culture, passaging, countring, typsinization, cryopreservation, sonication and extraction of prokaryotic inclusion bodies

Protein purification is a process by which a protein molecule is isolated from a complex mixture, often called its “cellular environment”. The protein of interest may be purified from natural sources, or produced through recombinant DNA technology.

The first step in protein purification is to break open the cells that contain the desired protein. This is accomplished using a variety of methods, including sonication and mechanical shearing. Once the cells have been disrupted, the proteins are released and can be separated from each other using centrifugation.

The next step in protein purification is to select an appropriate chromatography column. The column will depend on the properties of the desired protein molecule. For example, if the molecule has an affinity for a particular buffer, it will be best purified using chromatography in that buffer. 

The process of purifying a protein typically involves at least two distinct steps:

  • Breaking open cells 
  • Using chromatography to separate proteins from different sources.

In the first step, cells containing the target protein are broken open, releasing many other intracellular molecules that can co-purify with the desired molecule. The target molecule is often surrounded by other molecules that help stabilize it, in addition to proteins involved in cell structure. For example, membranes can be split in the process of breaking open cells, causing membrane proteins to co-purify with the desired protein. 

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Assignment Brief 5: Set up cell culture for thawing, counting, seeding and express proteins in bacteria

There are a few things to keep in mind when setting up a cell culture for thawing, counting, seeding, and expressing proteins. First and foremost, it is important to make sure that all of the equipment is sterile and that you are working in a clean environment. It is also important to use the correct media and supplements for your cells and to follow the manufacturer’s instructions closely.

In order to thaw your cells, you will need to warm them slowly over a period of several hours. Once they have reached room temperature, you can begin counting them using a hemocytometer or other counting device. Be sure to gently mix the cells before counting them in order to get an accurate count.

Next, you will want to seed your cells at an appropriate density in a tissue culture dish. This will vary depending on the type of cell and manufacturer’s instructions, but it is often recommended that you seed them at a concentration of 1-5 x 10^6 cells/mL. Once your cells have been seeded, incubate them in a 37 degree Celsius tissue culture incubator. It is important to make sure that the cells are kept warm and moist during this time, as they will need to express proteins in order for you to harvest them.

Last but not least, before expressing your protein it is important to activate your cells with a serum or growth factor of some sort. Typically this is done using a solution of bovine serum albumin (BSA), although it may vary depending on the type of cell you are working with.

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Assignment Brief 6: Discuss results and prepare good manuscripts and reports

The process of writing a scientific manuscript or report may seem daunting, but with careful preparation and organization, it can be a relatively straightforward process. The first step is to gather all of the data that you will need to include in your paper. Once all of the data is collected, the next step is to organize them into a logical and coherent order.

The next step is to write the Introduction section, which should provide a brief overview of your study and its purpose. The Results section should then follow, and this is where you will present your data in a concise and easy-to-read format.

The Discussion section should interpret your results and explain what they mean in relation to other published studies on the same topic. Finally, the Conclusion section should be included last as it serves as a final statement of how your study contributes to the existing body of literature on the subject.

Writing a good paper requires proper planning, organization and attention to detail. It is important for student researchers not only to explain their results clearly to others but also to learn how to interpret them correctly themselves. A well-written paper will describe the methods used in detail, but it is not necessary to include all of the raw data collected in the results section. The Results and Discussion sections should be organized so that they flow smoothly from one topic to the next, with each succeeding paragraph building on previous ideas.

If you follow these simple steps when writing your laboratory report, you will soon be able to create a well-organized and informative manuscript that will help you earn the highest grades in your science classes.

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