Category: Biochemistry

I need help with an amino acid and buffering capacity lab report. I can share with you my results, and the instructions. Please follow that and make a lab report. Please plot graphs in ms excel and all the required info in MS word. please follow the instructions completely and ask any questions if you need. please keep me updated.

Draw the full chemical structure of an optically INACTIVE tryglycerol that yields 2 moles of 18:0 fatty acid and 1 mole of 18:2🔺️⁹’¹² fatty acid.[6 Marks

Final Project – Part 3
Your final project will consist of three parts that will aid you in completing a research paper and creating an educational brochure that integrates what you have learned about genetic predisposition and how to make the public more aware of the issue you have chosen.
In Part 3 of the final project, you will:
Construct an educational brochure based on the topic you previously chose in Part 1 of the final project.
Provide three credible references to support your topic of choice.
Educational Brochure:
For the third and last part of this project you will create an educational brochure for a public audience that integrates what you have learned about the genetic condition of your choice. This is your chance to help the public learn more and be more prepared if they have to deal with this disease state. You will use the same information and research that you compiled in Part 2 of this project. You will need to introduce the specific condition or disease along with information about how individuals can have a genetic predisposition for this disease. In addition, you will need to highlight important parts of the biochemical process that are influenced or changed in this condition. You need to include the most important points from your research on the following requirements:
Explain the genetic consequences of the observed trait or conditions. Compare and contrast the normal and disease state of the condition and the genetic differences that result in protein dysfunction or dysregulation.
Describe how the condition is inherited and the population genetics related to the condition. Explain the relationship between genetic information transfer and the structure of nucleic acids.
Include a biochemistry review that focuses on the medically applicable concepts and techniques that form the underpinnings of the diagnosis, prognosis, and treatment of medical conditions.
Define any genetic testing currently available.
How to format your brochure:
Develop your brochure with the idea that the reader knows nothing about the patient’s disease or condition.
All sections must include appropriate text and headers to include the facets of your research. All images and graphs should be accompanied by an explanation and proper references. Correct grammar, professional language, and punctuation are required
The brochure you submit must be your own work. If you borrow ideas from printed sources or from people you have spoken to or heard speak, note that it should not be more than 10% of your text, and be certain to cite the sources of those ideas, even when paraphrasing. Include a separate reference section that is formatted as per APA guidelines. At least three professional references must be included in your brochure.
Be sure to include a separate small section at the beginning that has the following information:Title of Paper, Your Name, SC335, Section #, Final Project – Part 3, University Name, Date
Create a trifold, double-sided brochure using the Unit 9 Final Project Template.
The disease that was chosen was hunginton disease

Need: Abstract,Introduction,Materials and Methods,Results and Discussion. any information that you use beside the lab protocol please site. going to attach lab protocol and data.

Are there any challenges associated with the validation of liquid chromatography tandem mass spectrometry (LC-MS/MS) for voriconazole therapeutic drug monitoring (TDM) in urine samples?
Please write a research proposal regarding voriconazole therapeutic drug monitoring in urine sample by LC-MS/MS comparing to analysis this drug in serum samples which is the common used and applied method in most of the laboratories. Start with introduction then literature review, Relevance of the Research, Research Question, hypothesis, aims, methodology, and references.

I want someone to send me 3 research papers that are scientifically proven. I need them to be about estimating sugar content quantitatively in pasta, white bread and, macaroni. I want to use them to make my discussion.

I want someone to send me 3 research papers that are scientifically proven. I need them to be about estimating sugar content quantitatively in pasta, white bread and, macaroni. I want to use them to make my discussion.

I want someone to send me 3 research papers that are scientifically proven. I need them to be about estimating sugar content quantitatively in pasta, white bread and, macaroni. I want to use them to make my discussion.

I want someone to send me 3 research papers that are scientifically proven. I need them to be about estimating sugar content quantitatively in pasta, white bread and, macaroni. I want to use them to make my discussion.

PDB: 2PX6
The assignment should contain at least three figures: one (1) highlighting the secondary structure and two (2) active site images. Each Figure must have a caption for the active site images, be sure to describe the types of interactions you are showing in the image, and refer to any specific amino acid residues (involved in catalysis or inhibitor binding) by their amino acid number. I included an example on the file for how the assignment should look like. The three images need to be created using PyMOL for PDB: 2PX6 and using the white background.
Active site and enzyme-drug interactions
A. Include an image of the chemical structure of your drug molecule.
B. Create at least two PyMOL figures zoomed in on just the active site of your
enzyme. List the catalytic residues (e.g., Ser261, His342). Clearly show these
residues. Highlight other molecules in the structure that are involved in the reaction
catalyzed by your enzyme (substrates, products, cofactors, coenzymes, etc.). You
may hide the bound drug/inhibitor, or use a secondary, unbound structure to create
this image.
C. Zoom in on the drug bound to your enzyme (note that it may be in the active site, or
bound to another part of the protein, depending on the inhibitor type). Illustrate all
noncovalent interactions with measurements between this molecule and the
enzyme using at least one PyMOL figure. Include all hydrogen bonds and salt
bridges, clearly distinguishing these types of interactions. Also, show one nonpolar
interaction (3.3-4.0 Angstrom range).
D. Describe all of the interactions, referencing the specific amino acid side chain that is
involved in the interaction by its three-letter code and residue number and describing
the type of interaction with the drug. To save space, you may group them by type of
interaction.
VII. Figure Captions
For each figure, include a caption or description that helps the viewer understand
what they are seeing. A good figure caption briefly describes:
1. The figure content
2. Any coloring/labeling schemes to help the viewer interpret the image.