BI208 Protein Structure and Function NUIG assignment sample Ireland

BI208 is a protein structure and function course offered at many colleges and universities. The course covers the structure and function of proteins, enzymes, and other biomolecules important to living systems. Students learn how proteins are put together and how they work in enzymatic reactions, cell signaling, cell motility, and other processes. Complex problems are posed throughout the term to give students practice in using basic knowledge to solve real-world scenarios.

This protein structure and function course are usually taught as a junior-level undergraduate course, but some schools may offer it as part of a graduate program. The prerequisites for this course include one semester each of organic chemistry, biochemistry, or cell biology (or the equivalent courses).

Proteins are composed of amino acids, which are the building blocks of proteins. There are 20 different amino acids that can be found in proteins. Each amino acid has a unique structure that determines its function. The sequence of amino acids in a protein determines the protein’s three-dimensional structure.

Get Individual Assignment samples for BI208 Protein Structure and Function Course

In this course, there are many types of assignments given to students like individual assignments, group-based assignments, reports, case studies, final year projects, skills demonstrations, learner records, and other solutions given by us. We also provide Group Project Presentations for Irish students.

In this section, we are describing some briefs. These are:

Assignment Brief 1: Describe fully the general molecular structure and function of proteins.

Proteins are large, complex molecules that perform a variety of tasks in the body. They are made up of smaller units called amino acids, which are linked together in long chains. The order of the amino acids determines the structure and function of the protein. Proteins can be found in all cells and tissues, and they play a vital role in cell structure and function.

Proteins are composed of amino acids, which are small organic molecules that contain both an amine group (–NH2) and a carboxyl group (–COOH). There are 20 different amino acids that can be used to make proteins, and each one has a unique chemical structure. Amino acids are joined together by peptide bonds, and the sequence of amino acids in a protein determines the protein’s three-dimensional structure.

Assignment Brief 2: Demonstrate the role of enzymes as nature’s own biocatalysis at the molecular level from studies of kinetics and molecular structure.

Enzymes are proteins that catalyze biochemical reactions. As nature’s own biocatalysts, enzymes are essential to the proper functioning of all life forms. Their role in the molecular structure is to lower the activation energy of a reaction, thus speeding up the process.

Studies of kinetics reveal that enzymes obey first-order kinetics, meaning that the rate at which a reaction proceeds is proportional to the concentration of enzyme present. The molecular structure of an enzyme reveals a hydrophobic core with several charged residues on the surface. These charged residues form an electrostatic interaction with the substrate, and it is this interaction that facilitates catalysis.

In proteins, the primary structure is the sequence of amino acids, which are held together by peptide bonds. The secondary structure is the way in which the polypeptide chain folds up. There are two main types of secondary structure, both of which involve hydrogen bonding:

1) Alpha helix

2) Beta pleated sheet

The tertiary structure is the three-dimensional shape that the protein assumes. This is determined by the primary and secondary structures, as well as by the interactions between different parts of the protein molecule. The quaternary structure is the way in which several polypeptide chains are bound together to form a complex protein molecule.

Assignment Brief 3: Develop an understanding of the main experimental approaches and concepts for biomolecule analysis.

There are many experimental approaches and concepts for biomolecule analysis. Some of the most common include chromatography, electrophoresis, and spectroscopy. Each of these techniques has its own advantages and disadvantages, which can be best suited for certain types of biomolecules or analysis applications.

Chromatography is a separation technique that uses a mobile phase (liquid or gas) to move a sample mixture through a stationary phase (a column). This technique can be used to separate complex mixtures into their individual components. Electrophoresis is a separation technique that uses an electric field to move charged molecules through a gel or liquid. This technique can be used to separate proteins by their net charge, nucleic acids by their size, and carbohydrates by their structure. Spectroscopy is the study of the interaction of light with matter. This technique can be used to identify biomolecules by their absorption or emission spectra.

Assignment Brief 4: Manipulate biochemical reagents and perform biochemical assays.

There are many different ways to manipulate biochemical reagents and perform biochemical assays. The specific method you use will depend on the reagents and assays you are working with. However, some general tips that may be helpful include:

• Make sure your work area is clean and well-organized. This will help you avoid contamination and errors.
• Take care when handling reagents, especially those that are volatile or dangerous.
• Following protocols carefully. Again, this will help you avoid errors and produce consistent results.
• Keep good records of your work. This will be valuable if you need to replicate your results or troubleshoot any problems that occur.
• As always, practice safe lab practices. Biochemical reagents can be hazardous if not handled properly.

Assignment Brief 5: Perform core techniques for measuring properties and quantities of the four main classes of biomolecules, including proteins.

There are four main classes of biomolecules: proteins, carbohydrates, lipids, and nucleic acids. Each class of biomolecule has unique properties that can be measured using a variety of techniques.

Proteins are the largest and most complex class of biomolecules. They are composed of amino acids arranged in a specific sequence, which gives them their unique structure and function. Proteins can be measured using techniques such as mass spectrometry, nuclear magnetic resonance spectroscopy, and X-ray crystallography.

Carbohydrates are composed of simple sugar units linked together by glycosidic bonds. They play important roles in cellular energy storage and metabolism, as well as cell-cell recognition. Carbohydrates can be measured using techniques such as gas chromatography and high-performance liquid chromatography.

Lipids are a diverse class of molecules that include fats, oils, waxes, and sterols. They are important components of cell membranes and play a variety of roles in cellular function. Lipids can be measured using techniques such as thin-layer chromatography and mass spectrometry.

Nucleic acids are the largest and most complex molecules in cells. They are composed of nucleotides, which are arranged in a specific sequence. Nucleic acids play important roles in cellular function, including DNA replication and gene expression. Nucleic acids can be measured using techniques such as gel electrophoresis and nuclear magnetic resonance spectroscopy.

Assignment Brief 6: Demonstrate an ability to present and interpret scientific results.

Scientists have long known that calorie restriction is associated with a host of health benefits, including longer lifespans. But the underlying mechanisms were not well understood.

New research published in Cell Metabolism sheds light on the cellular processes responsible for the life-extending effects of calorie restriction. The study found that calorie restriction reduces insulin signaling pathways, which leads to increased levels of waste products that accumulate within cells and cause aging.

The findings provide new insight into the link between diet, metabolism, and aging, and suggest that strategies aimed at reducing insulin signaling may be beneficial for increasing lifespan.

The study’s authors say the findings could have implications for developing new therapies to treat age-related diseases.

When presenting scientific results, it is important to be clear and concise. It is also important to be able to interpret the data in a way that is meaningful to non-scientists.

Assignment Brief 7: Draw scientifically grounded conclusions from observations and explain these in writing.

When scientists observe something in nature, they often try to come up with a hypothesis to explain what they have seen. A hypothesis is a proposed explanation for an observed phenomenon that can be tested by further observation and experimentation.

Once a scientist has formulated a hypothesis, they must then test it to see if it is correct. If the data support the hypothesis, then the scientist can draw scientifically grounded conclusions from the data. If the data does not support the hypothesis, then the scientist must come up with a new hypothesis.

Scientific conclusions must be based on evidence, and scientists must always be willing to change their conclusions in the face of new evidence.

When writing about scientific findings, it is important to be clear and concise. It is also important to explain the findings in a way that is meaningful to non-scientists.

Assignment Brief 8: Explain the main units of biochemical measurements and perform the basic calculations used in biochemistry.

The main units of biochemical measurements are mass (g), volume (mL), and concentration (M). Molarity (M) is defined as the number of moles of solute per liter of solution, and it is the most commonly used unit of concentration in biochemistry.

To calculate the concentration of a solution, you divide the mass of the solute by the volume of the solution. For example, if you have a 0.5 M NaCl solution, that means there are 0.5 moles of NaCl per liter of solution. To calculate the amount of solute in a given volume, you multiply the concentration by the volume. So if you wanted to know how many grams are in 10 mL of a 0.5 M NaCl solution, you would multiply 0.5 x 10 to get 5 g.

The other units of concentration that are sometimes used in biochemistry are mole fraction (X) and morality (m). Mole fraction is defined as the number of moles of solute per mole of the solution, and it is usually expressed as a decimal. Morality is defined as the number of moles of solute per kilogram of solvent, and it is usually expressed as a percentage.

These are the basic units and calculations used in biochemistry. It is important to be able to understand and use these concepts when working with biochemical data.

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