Introduction Recombinant proteins first came to light in 1970’s. The method was initially proposed by a graduate student called Peter Lobban. It was then acknowledged by two scientists called Stanley...

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Introduction


Recombinant proteins first came to light in 1970’s. The method was initially proposed by a


graduate student called Peter Lobban. It was then acknowledged by two scientists called


Stanley Norman Cohen and Herbert Boyer, who went on to publicize their work. Herbert


Boyer then went on to use this recombinant technology to create the first recombinant drug,


a biosynthetic human insulin product (Berg and Mertz, 2010).


These proteins are coded for by a recombinant DNA sequence. This technology allows us to


cut different fragments of DNA from different sources so that they could later be combined to


create a recombinant DNA strand. These new DNA strands could be used in a multitude of


ways and changed how scientists could
analyse
and manipulate biological molecules. The



revelation of this technology led to many breakthroughs and discoveries, some of which I will


cover later




Essay BMS3092 Title ‘Recombinant proteins are important in the 21st century?” Grading This assignment is worth (25% of your overall course grade). Please see the grading rubrics to see how you will be evaluated on this assignment. Requirements • An essay of 2500 words in length not including the Bibliography or Figures that addresses the question ‘Are recombinant proteins important in the 21st century’? • The essay should be written in a professional academic style, all material/sources utilized in the essay must be properly cited both in the body of the text and in the reference/bibliography section using Harvard referencing style (http://www.surrey.ac.uk/library/learning/informationskills/referencin g.htm ) • The submitted essay should be formatted using Arial 11pt and 1.5 line spacing • Submit on SurreyLearn as a Word file to help us provide feedback. Consider the following questions: 1. What is a recombinant protein? 2. Why would we want to produce recombinant proteins? 3. What type of proteins could be or are being produced? 4. Explore the title of the essay, are they important economically, medically, for food security /manufacturing or any other reasons; how do they contribute to society? 5. Support your argument by giving examples to illustrate why you agree or disagree with the statement: ‘Recombinant proteins are important in the 21st century’ Reference resources: Start with web searches for commercially available recombinant proteins involved in fields you are interested in, such as specific areas of medicine or scientific research. Many recombinant proteins used as pharmaceutical drugs are also referred to as “biologics.” The recombinant protein of the day will give further examples. Deadline for submission via SurreyLearn is Tuesday 31st October 2017 at 16:00 (4pm). Learning objectives 1. Students will better understand the importance of recombinant proteins in a wide variety of uses 2. Students will be able to discuss why producing recombinant proteins is important http://www.surrey.ac.uk/library/learning/informationskills/referencing.htm http://www.surrey.ac.uk/library/learning/informationskills/referencing.htm 3. Students will have increased ability to identify, find and use appropriate resources 4. Students will have increase their academic writing skills Guidelines for the structure of a professional academic essay An academic essay should address or answer a question or task. It should address/answer a question by developing a logical argument to support the thesis. It should include relevant examples, supporting evidence and information from academic texts or credible sources. Introduction The length of an introduction is usually one to three paragraphs. Include a few opening sentences that introduce and briefly explain the topic of the essay. Present the aim of the essay and summarize the main finding or key argument. Conclude the introduction with a brief statement of your evaluation of the question. Critique The critique should be a balanced discussion and evaluation of the strengths, weakness of the topic or question posed. Remember to base your discussion on specific criteria and include other sources to support your evaluation but remember to reference them. You can address each point you choose in a separate paragraph. You may also find it helpful and choose to use subheadings. Do not forget that you can use diagrams, tables and illustrations where appropriate but remember to number them Figure 1, 2, etc and do not forget to include a Figure Title and legend and of course refer to them in the text. Conclusion This is usually a short paragraph restating your overall opinion of the topic. If necessary some further qualification or explanation of your judgment can be included. This can help your critique sound fair and reasonable. You can also include a view of the future direction of the topic. References If you have used other sources in your essay to support your discussion then cite them within the text as appropriate and include a list of references at the end of the review correctly formatted as required. Grading Rubric Low Medium High Marks Available Essay content The essay is incomplete or inaccurate. One or more questions/topics have been missed or incorrectly answered The essay is complete and questions/topics are addressed accurately/adeq uately. Demonstrates an adequate breadth and depth of substantive knowledge but with only a few errors or omissions The essay not only addresses and answers the question but Demonstrates a breadth and depth of substantive knowledge that is comprehensive, accurate, relevant and informed by advanced scholarship 80 Presentation and Format Hard to read and poorly organized /structured. No references included or inappropriately formatted Average clarity and organization somewhat deviates from accepted formats, but is neat in appearance. Some citations incorrectly formatted Essay is well structured and organized with appropriate use of subheadings and citations are appropriately formatted 10 Language, Grammar, and Spelling Essay contains numerous grammatical mistakes or misspellings. Language may not be appropriate for an academic essay Essay contains some grammatical mistakes or grammatical errors. Language is not professional/aca demic in some instances Only a few grammatical mistakes and misspellings are in the essay. Language is professional/aca demic 10 Total 100 Essay Feedforward • Read the instructions, exactly the same as read the question! • Structure o Read-Plan-Write o Use headings & subheadings to help you organise your thoughts o Ask the question is this relevant to addressing the question o If you make a statement you have to provide supporting evidence. Data, examples and/or references • Figures o Use them if they are applicable – do they add value? Do they save you writing a lengthy explanation o Refer to them in the text o They need a figure legend – you should be able to understand a figure without any further information • Proof read carefully o Use a spell checker o Use the grammar checker it is quite good at picking up nonsense • References o Do not rely on internet based resources o Format them correctly –use a citation tool o Available at? Specific comments Many described the process of molecular cloning in great detail was this relevant to the question posed? In many cases the description stopped at cloning a sequence and did not describe or discuss the requirements of an expression vector which could be relevant. Remember cloning does not mean expression! Essay BMS3092 ‘Recombinant proteins are important in the 21st century?’ Introduction Recombinant proteins first came to light in 1970’s. The method was initially proposed by a graduate student called Peter Lobban. It was then acknowledged by two scientists called Stanley Norman Cohen and Herbert Boyer, who went on to publicize their work. Herbert Boyer then went on to use this recombinant technology to create the first recombinant drug, a biosynthetic human insulin product (Berg and Mertz, 2010). These proteins are coded for by a recombinant DNA sequence. This technology allows us to cut different fragments of DNA from different sources so that they could later be combined to create a recombinant DNA strand. These new DNA strands could be used in a multitude of ways and changed how scientists could analyse and manipulate biological molecules. The revelation of this technology led to many breakthroughs and discoveries, some of which I will cover later. In this essay I will discuss the advantages of using recombinant proteins as well as the challenges associated with them. I will look at the contribution of these proteins in areas such as medicine, scientific research and the food industry. Lastly I will come to a conclusion on whether or not recombinant proteins are important in this day and age. Production of recombinant proteins There are generally two ways of producing recombinant DNA. These include molecular cloning and the polymerase chain reaction (PCR). The difference between these two methods are that molecular cloning replicates DNA within a living cell while PCR does not need a living cell (Wilson and Walker, 2010). Once you have your recombinant DNA it is important to select a suitable expression system. Different expression systems include bacteria, yeast, mammalian cells and insects. Each of these systems have their merits and flaws. Deciding which system to use is dictated by two things: the intended use for the protein and the nature of the protein itself. You need to think about the cost, production time, how much yield you need and is the host capable of post-translational modifications (Jayaraj and Smooker, 2009). Why do we want to produce recombinant proteins? There are many benefits in using recombinant proteins compared to older methods. First of all, it is possible to produce high yields of these proteins in a short period of time which is good in an industry setting. They are easy to manipulate and can be made in a continuous supply with a high consistency rate. In addition to this these recombinant proteins will have a high percentage of purity making them a better product than previous ones. In the past it was necessary to procure kilograms of animal and plant tissue to isolate the amount of protein needed. The earliest recombinant product, insulin, had to be harvested from the pancreas of a pig before this technology existed. It was necessary to separate this insulin from the rest of the proteins found in the pancreas (Quianzon and Cheikh, 2012). A three amino acid difference in protein sequence resulted in an immune response. Recombinant technology has made it easier and more ethical to produce insulin products and many other recombinant proteins. Furthermore, there is much more freedom associated with these proteins. They can be made using any DNA sequence. This allows for much more specificity associated with the protein. Challenges associated with recombinant
Answered Same DayOct 14, 2019BMS3092

Answer To: Introduction Recombinant proteins first came to light in 1970’s. The method was initially proposed...

David answered on Dec 28 2019
142 Votes
“Recombinant proteins are important in the 21st century?”
Introduction
“Recombinant proteins” are manipulated form of proteins that are encoded by “recombinant DNA” molecules using biomolecular engineering. These “Recombinant DNAs” are generated by using “Recombinant technology”. In “Recombinant technology”, DNA molecules from at-least two different species are joined together to bring genetic material from multiple sources creating such sequence that are not found in genome under natural conditions. The joining is done by inserting them into a host organis
m such as bacteria, yeast, or mammalian cells to create new genetic combinations which are for medical, academic and research uses.
The method of “Recombinant DNA” was developed during seventies of 20th Century (1970 to 1979). In the starting of the decade, a graduate student, Peter Lobban, initially planned this method along with a biochemist, A. Dale Kaiser at Stanford University. The method was later acknowledged by two scientists called Stanley Norman Cohen and Herbert Boyer when their predictions were published in a journal named "Enzymatic end-to-end joining of DNA molecules" in 1973. The method reached at a new advanced level in 1977 with creation of the biosynthetic "human" insulin by Herbert Boyer, which was the first recombinant drug.
For the purpose of this assignment, I would write this essay in such a way that it would cover advantages, challenges of using recombinant proteins along with its contribution in the area of medicine, scientific research and the food industry. At the end, we would conclude whether or not recombinant proteins are important in 21st century.
Creation of Recombinant Protein
Recombinant DNAs are produced by one of the two ways; “Molecular Cloning” & “Polymerase Chain Reaction”. Under the molecular cloning, one molecule is replicated to a population of cells with identical DNA molecules by using DNA sequences from different organisms of the source species (i.e. source of the DNA to be cloned) and the living host for replication of the recombinant DNA. Wherein, under PCR technique, a single copy or a few copies of a segment of DNA is amplified across several orders of magnitude that generate thousands to millions of copies of that specific DNA sequence.
When we look for the differences between these two methods, we would find two fundamental differences;
(i) In “Molecular cloning”, DNAs are replicated within a living cell whereas in “PCR” DNAs are replicated in a test tube that is free of living cells.
(ii) DNA sequences are copied and pasted in “Molecular cloning” whereas they are amplified by copying their existing sequence under “PCR”.
Advantages of Recombinant Protein
The emergence of “Recombinant Proteins” has brought number of advancements in the fields of food & agriculture and medicines. The major benefits using these proteins are;
(a) Purity percentage of these proteins is quite high compared to other methods when the required proteins are not easily available from a natural system. This makes Recombinant proteins a better product compared to the previous ones.
(b) The supply of these proteins is continuous with high yields which wasn’t the case previously. This helps in fulfilling the demand of the market irrespective of demand levels.
(c) Producing peptides using Recombinant protein is cheaper than chemical synthesis.
(d) Recombinant proteins can provide type of proteins that do not exist naturally.
(e) Production of Recombinant proteins shows high level of consistency in batch to batch production.
(f) These proteins are easier to be modified which helps in improvement of mutant versions of known proteins.
(g) Recombinant proteins much more freedom in creation of a new protein as any DNA sequence can be used in production of these proteins. This results in higher specificity of the proteins.
Challenges faced in the production of Recombinant Protein:
Recombinant proteins have experienced a surge in demand in recent decades due to the higher number of applications of recombinant proteins in different fields gaining commercial grounds. As per www.pharma.org, as of today there are more than 75 recombinant proteins being used as pharmaceuticals and there are more than 360 new medicines that are being developed based on these proteins. However, production of these proteins still constitutes a challenge that need to be taken care.
One of the major challenges related to production of recombinant protein is “loss of expression”. Efficient expression of the gene of interest is a necessary condition in order to produce adequate recombinant protein. However, there always exists a possibility of “loss of these expressions” that can be lost because of structural changes in the recombinant gene or dissolution of the gene from host cells. The major issues related to “loss of expression” are Codon bias & Aggregation of protein. Another challenge associated with production of Recombinant protein is “Protein toxicity”. When these proteins perform a function that creates an interference with the homeostasis of the host cell, there is a possibility of “Protein toxicity” that would most probably slower down the growth rate and at extreme, cell death.
Proper formation of disulphide bonds is an important aspect of the production of most recombinant proteins. If this formation is disrupted or not done in a proper manner, it could result into misfolding and the formation of inclusion bodies.
Pharmaceutical Products based on Recombinant Protein:
There are certain proteins that could be utilized as pharmaceutical agents for the treatment of many human...
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