Princess Diana Essays (305 words) - House Of Windsor,

Princess Diana Princess Diana was an exceptional leader. Diana worked as a kindergarten teacher in London until her engagement to Prince Charles was announced in February of 1981. She wed Prince Charles in an internationally televised ceremony on July 29, 1981. Almost immediately, "Shy Di" as she was initially called by the press, blossomed into the "people's Princess". Princess Diana contributed to society in so many ways; she would always go the extra mile to help people in need. While she became the president or patron for over 100 charities, there were many more that she raised funds and campaigned for. Diana was the busiest of the royal family. She was not just fulfilling a schedule or participating just for the adulation; she was a person of compassion expressing a genuine love for people. Princess Diana was spontaneous in ways, happily turning away from royal protocol to kiss a child in a crowd or writing letters to individuals of the public and signing them "love, Diana". Her leadership was truly remarkable because she made every effort to reach out to those that not everyone wanted to reach out to. Princess Diana could always be found walking with, hugging, really listening to those people in situations that some might help from a distance such as the sick, the elderly, those with aids, the homeless, the battered, the drug-addicted, people maimed by land mines. Princess Diana led the royal family out of a period of rapidly declining support from the people. Since her death, the royal family continues to make efforts in maintain the closeness with the people that the Princess had formed. They have learned much about leadership from the Princess and it is a legacy to her that the royal family practices what they have learned. In recognition of all her charity work, representatives of the charities with which Princess Diana had worked were asked to walk behind her coffin with her family the day of her funeral.

11 Steps to Writing the Perfect Resume

11 Steps to Writing the Perfect Resume Whether you’re planning to use a resume-writing service or give it a go on your own, it’s important to take some time to prepare for your resume rewrite. Your resume will only be as good as the information you or your writer has work with. Gather the following details ahead of time to craft a powerful document that effectively tells your story and markets your qualifications. Contact information.While this section may seem obvious, there are a few factors to consider. For instance, how will you display your name? Are you planning to use a nickname, such as Bob, or will you use your full name for the job search? Whichever you choose, make sure you consistently represent your name on all your personal branding materials such as your business cards, LinkedIn profile, and online portfolio or blog.Select one email address and one phone number to include on your resume. I recommend setting up an email address that’s dedicated to your job-search activities and using you r cell phone number on your resume, as this gives you the ability to control the voicemail message, who answers the phone, and when.Online presence.A Jobvite social recruiting survey found that 93 percent of recruiters will search for your online profiles before they decide to interview you. Save them some time by including the URL to your LinkedIn profile. Don’t have a LinkedIn profile yet? Check out this video tutorial by Lindsey Pollak for help creating your profile.In addition to your LinkedIn account, include any links that are relevant to your work, such as a personal website, portfolio, or blog. If your work involves social media, you may include the links to other social media accounts such as Twitter, Instagram, and so forth.Sample job descriptionsA great resume is tailored to support a specific job goal. One of the best ways to ensure your resume is properly positioned is to identify sample jobs that you’re interested in and qualified to perform.Search online and gather a few job postings that represent the type of position you’re targeting. It doesn’t matter if the location is ideal; for this purpose, you should only be concerned with the job description and its requirements.Copy and paste the text of the description itself into a Word or Google document and then highlight or bold any requirements or desirable skills from the posting you possess. This will help you or your writer identify which of your qualifications should be showcased throughout the resume.Technical skills and proficienciesWhat technical platforms and tools are you proficient? List all that apply to your work. Be specific and as comprehensive as possible. This list can include anything from social media platforms to project management systems and computer languages. If you’ve worked with proprietary platforms, list those as well.Need to brush up on a skill or tool that’s routinely popping up in the job descriptions you’re targeting?   Check out edX, Coursera, and SkillShare for free or low-cost online courses.Your professional experience.Start with your most recent job and work your way backwards. You’ll need to detail out all your professional positions within the past 15 years. If you served in the military or held a board position, list this experience as you would any other role in your work history. If you recently graduated from college, include your internships and any work experience that took place since you entered college.For each role, list the following information:Company Name and URLJob Title: If your title is very specific to your organization, you can include a translation of sorts in parentheses next to your official job title.Start and End Dates: Include the month and year for each of these dates.Job Description: Think about your roles and responsibilities as they relate to your target role. This is especially important if you’d like to change careers. Include details such as how many people you managed or supervised, the territories you covered, etc.Achievements: Brainstorm a list your accomplishments and major contributions that benefited the organization during your tenure. The number of achievements you provide will depend upon how long you remained in that role and how relevant it is to your current job goals. Quantify your accomplishments whenever possible; for instance, how did you help save the company money, generate revenue, improve customer satisfaction, increase productivity, and so forth?If you have an existing resume, only include new details in this section. There’s no reason to repeat anything that already appears in your current resume.Early career historyIf you’ve been in the workforce for over 15 years, chances are you have a few positions that got left out of the previous section. Make a list of the job titles you held, the names of each employer, the locations where you worked, and your dates of employment for these rol es. While the dates will likely not get used in your resume, it’s good to have a clear record of your earlier experiences for the writer.Volunteer workHave you been actively volunteering with a non-profit organization? Skills-based volunteering (SBV) is a great way to fill an employment gap or supplement your work history when you’re trying to change careers.   Please list any volunteer work you’ve done that’s relevant to your current job goals in chronological order, beginning with your most recent work.  If you’re new to the workforce, include any campus activities or clubs in which you were active.Record the name of the organization and its website URL, the positions you held, your years of involvement, and your responsibilities and contributions to the non-profit. Looking for new volunteer opportunities?  Visit sites such as Catchafireand VolunteerMatch.Professional affiliationsList any relevant professional organizations or affiliations you’re a member of that aren’t listed on your resume. For each group, please list their name and URL, when you became a member, and any positions you’ve held. If you took an active role in the organization, describe your responsibilities and any notable achievements.Interested in joining a new association? Check out WEDDLE’s Association Directory or research which groups your peers and managers belong to. You can often find this information on their LinkedIn profiles.Language skillsLanguage skills can be a great selling point on your resume. If you’re multilingual, be sure to list each language you speak and your proficiency level.Education and professional developmentCreate a record of all your education, beginning with your most recent degree. List the institution, its location, the name of your degree, your major and minor, your graduation year, and any honors associated with the degree, such as summa or magna cum laude. Do the same for any rele vant certifications you’ve obtained or additional training opportunities or workshops you’ve attended.Third-party feedbackHave you received positive customer testimonials or a great performance review? Include this information in your preparation materials. You or your resume writer  may be able to work some of this information into your resume to demonstrate your hard and soft skills in the workplace.While this may feel like a lot of work now, by taking the time to examine your career now, you’ll see the benefits in your future resume.Note: this article was originally published on TopResume.TopResume is a Talent Inc. company, the personal branding destination for all career-driven professionals. Through our extensive network of professional writers, we offer career advice and analyze and write more resumes and LinkedIn profiles than any other service in the world. Ready to get started? Request a free resume critique today.

Strange Heaven by Lynn Coady Coursework Example | Topics and Well Written Essays - 250 words

Strange Heaven by Lynn Coady - Coursework Example And here adds to the hilarious, complicated life of the Joan his husband, Robert. Joan tries to keep the lid on, but she's no match for Robert's wild profanity. Facing all these dilemmas, anyone would wonder how she is trying to handle her dysfunctional family. Uncle Albert arrives to whisk her back to the bedlam of home and the booze-soaked social life that got Bridget into trouble in the first place. Uncle Albert, a kind man who saves his eloquent wrath for outsiders, springs Bridget from the hospital for Christmas. He was the only person who thought of Bridget and has concerns about her depression or maybe the only person who feels how tough was Bridget’s experience was. He’s the only person who sees the problem while everybody is working on their own dysfunctions. He was the only person who observed that she was changed. Byron, an acne-ridden geek with bizarre delusions of grandeur. As described by Coady, life on the ward is both a nightmare and laugh-out-loud funny experience. Byron seems to be annoying and arrogant, continues his desperate bids for Bridget’s attention. He explodes and have to be put in the quiet room where he'd sit cross-legged and howl like a hound.

The Community Health Systems, Stress and Their Meanings Research Paper

The Community Health Systems, Stress and Their Meanings - Research Paper Example The employees realized that the due to the prevalent condition of the industry where reimbursements were waning and regulations were mounting, the Community Health Systems was facing financial complexity; yet they were not satisfied with the offer the company had proposed and believed that they should be paid better compensation. Jim Brentwood had said that they would conduct an informational picket on Thursday and after that, they would decide depending on the strike vote by the group of employees. He had added that although the employees did not wish to strike there was a strong possibility of one if the company did not collaborate with them. Mary Martin, on the other side, found it hard to believe that the employees would go for a strike because if they did so, they would be paid only half the amount that they would have earned for a week. The 2000 employees involved were at the bottom end of the company’s pay scale, and hence Mary Martin was confident that due to monetary constraints the employees would not vote in favor of a strike. Moreover, this group of employees included patient transporters, housekeeping and cafeteria workers, and the Community Health Systems was already thinking of outsourcing their dietary department to another firm, Thomson Healthcare Food Services; and hence even if the employees did go for a strike, the organization could carry on their cafeteria services without interruption. Instead of reconciling the existing differences and trying to arrive at a consensus agreement, both the sides were rigid in their stands and were not in a mood for negotiation. Generally, the outcome of a negotiation is reliant on the power relationship between the two sides. In this context, the employee union was not aware of the company’s plan to outsource their dietary requirements.

Individual organizational analysis with State Farm Essay

Individual organizational analysis with State Farm - Essay Example This precedent was set after the Paul v. Virginia case in which the power of the state to regulate state based insurance and mutual companies was challenged (Grace & Klein, 2009). Major industry players characterizing the mutual and insurance sector in United States have massive global influence and market dominance. This results into increased competition between well-established insurance and mutual companies like State Farm and other small scale and state based industry players. As a mutual industry player, State Farm provides impetus for economic growth by holding trust and providing funds for economic growth and development. The development of life insurance and other human based mutual services have changed the societal view of the industry as a whole. From an industry that was once viewed with skepticism, the insurance industry has attracted significant societal support due to the values it adds to insured individuals (Turner, 2005). Technological craze has created significant impacts in major industries in the United States economy including the insurance and mutual industries. Competition is currently defined by the ability of an organization to integrate proper information technology systems into its operations as a way of increasing efficiency and accuracy. Insurance companies are currency deploying significant technological tools in the operations such as the use of mobile technology, cloud computing and interactive web 2.0 to integrate its customer service and ensure proper service delivery. It is estimated that the insurance industry in the United States spent over $40.6 billion in 2012 in information technology services and products with an aim of... With the current competitions in the market, the adoption of sound strategies defines the success of a company especially in the insurance industry. State Farm has achieved great success this far as a result of its approaches and strategies that seeks to blend with the events within the market. However, to remain relevant in the face of the current competition, State Farm should adopt a customer-centered strategy that seeks to increase customer satisfaction. To identify the different concerns of the customers, the company should organize regular open days for interaction with the current and prospective customers. From this, the company can be able to gauge the overall view of the customers and act on their different concerns. The company has developed into one major insurance and mutual company in the United States with a great pool of loyal customers thus giving it a strong market backing. However, the participation in mutual business restricts its investment opportunities and rest rains its financial source to stock and the sale of shares. The company should improve its financial and credit services especially targeting its traditional customers as this will broaden its source of revenue and cushion it from loss during economic meltdowns.

Expression of Recombinant Green Fluorescent Protein (rGFP)

Expression of Recombinant Green Fluorescent Protein (rGFP) Expression and Purification of recombinant Green Fluorescent Protein (rGFP) from E. coli using Ni2+-Agarose Column Chromatography. Andrea Bustamante Janakikeerthika Darmarpandi Abstract Green Fluorescent Proteins are vital components of bioluminescence in marine animals. There unique ability to withstand and recover from harsh conditions and regain fluorescence was of great interest. The purpose of the following set of experiments was to express and purify a His6-Xpress epitope tagged recombinant form of Green Fluorescent Protein grown and harvested from E. coli. The desired protein is initially released into solution using the properties of freeze-quick thaw cycles that then help release the contents of the nucleus of neighboring bacteria following a chain reaction. It is then submitted through a Ni2+-agarose affinity chromatography column where the target protein was purified. The resulting wash and elution fractions where run through a Bradford assay, SDS-PAGE/Coomassie blue staining, and a Western blot to determine the molecular weight of the protein to be 32kDa. The overall specific activity was determined to be 433000 RFU/ mg of total protein with a resulting 20 percent purity. The results show that expression and purification of rGFP from bacterial cells was possible. Introduction Aequorea victoria is a jellyfish capable of producing a green fluorescent light when Ca2+ ions activate a photoprotein, known as aequorin, which excites Green Fluorescent Protein (GFP). Wild type GFP is a 27kDa, homodimer composed of 238 amino acid residues that absorbs light at an excitation wavelength of 395nm (blue light) and emits light at an emission wavelength of 510nm (green light). Aequorea victoria GFP has a distinctive three dimensional structure that encases a chromophore (formed by cyclization of Ser65-dehydrogenized Tyr-Gly67) and allows for stability under harsh conditions (Prasher, 229-230.) . This structure allows for regaining of fluorescence even after the protein has been denatured upon removal of the denaturant. Therefore, GFP’s are extremely stable to changes in pH, temperature, oxidation and reduction, and chemical reagents (Pan, Pickett, and Rippel 225.) Poly-histidine tags involve addition of a series of histidine residues to the N or C terminus of a protein of interest. Poly-histidine tags are affinity tags that serve to facilitate protein purification by exploiting the positively charged histidine residue’s affinity for negatively charged columns. This series of experiments involved a six repeat histidine codon contained within a DNA plasmid which resulted in a recombinant Green Fluorescent Protein that contained a six residue histidine tag located at the N-terminus. The His ­6 tagged recombinant Green Fluorescent Protein was then subjected to Ni2+-agarose column affinity chromatography. Ni2+-agarose affinity chromatography allows for the purification of poly-histidine tagged proteins due to the selectivity and affinity of the Ni2+-agarose matrix for His6 tagged proteins. rGFP binds the column due to the interactions between the His6 tagged proteins in the mobile phase with the metal Ni2+ ions immobilized within the matrix in the stationary phase. The Ni2+ ions contained within the matrix are capable of binding electron rich molecules including histidine residues and allowing most other molecules to pass unbound. This results in the binding of the desired protein to the column and the purging of most undesired proteins and contaminants from the column into wash fractions (Ninfa, et al. 100-101.) The column was then subjected to imidazole, which competes with rGFP for Ni2+ ion attachment, and this allows for the elution of the target protein. Due to its unique properties, isolation of GFP was of great interest and expression and purification were the main focus of the following series of experiments. A suitable way to accomplish this was devised using the combination of poly-histidine tagging and affinity chromatography. The purpose of this experiment was to express and purify a six-Histidine tagged recombinant form of Green Fluorescent Protein from E. coli through the use of Ni2+-agarose affinity chromatography. After expression and purification, a Bradford assay was performed to estimate total protein amount. This was followed by SDS-PAGE/Coomassie blue staining to determine purity and molecular weight. The confirmation of the presence of rGFP was done using the Western Blot. Materials and Methods Growth of G strain In a test tube, 10ml of liquid LB growth media containing 100ug/ml Amp and 25ug/ml Cam was inoculated with a single bacterial colony of strain G (BL21(DE3)uv>) and was allowed to grow overnight at 37 °C. The culture was shaken until saturated. In a flask, 500ml of liquid LB media (pre-warmed to 30 °C) was inoculated with about 4 ml of the saturated overnight culture (or until the 500ml culture reached an OD600 reading of 0.1) and allowed to grow at 37 °C until the OD600 reading reached 0.5. At approximately OD600 ~0.5, or time zero, 1ml of the culture was harvested into a 1.5ml centrifuge tube and pelleted. The supernatant was discarded and the â€Å"G0† pellet stored at -20 °C for later use. The remaining culture was induced with 1mM IPTG and allowed to grow. After 3 hours, 1ml of the culture was harvested into a 1.5ml centrifuge tube and pelleted. The supernatant was discarded and the â€Å"G3† pellet stored at -20 °C for later use. An additional 15ml of the IPTG induced culture was harvested into a 15ml centrifuge tube and pelleted. The supernatant was discarded and the â€Å"G3-15ml† was stored at -20 °C. Preparation of rGFP Crude Extract Immediately after removal of the â€Å"G3-15ml† pellet from freezer, breaking buffer [10mM Tris, pH 8.0; 150mM NaCl] was added into the centrifuge tube. The breaking buffer was pipetted up and down (being careful not to introduce air) until pellet had thawed and homogeneity was reached. The solution was transferred into a 1.5ml centrifuge tube, vortexed for 5 minutes, labeled and placed in 37 °C water bath for 10minutes after which the centrifuge tube was transferred to a rotating platform shaker in a dry air 37 °C incubator for 20 minutes. After lysis, the mixture was centrifuged at 14000xg, 4 °C, for 10 minutes. In a dark room in the presence of a hand held UV light, the fluorescence of the pellet and supernatant where observed the recorded. The supernatant was then decanted and care was taken not to get the pellet back into the supernatant as centrifugation would be required if this did occur. This supernatant was the GCE (rGFP crude extract) Preparation of Ni2+-agarose Column In a 3ml plastic syringe, enough glass wool was placed into the well to cover up to the 1/4 ml marking. The syringe was secured onto a ring stand and placed perpendicular to the ground. About 100ul of breaking buffer was pipetted into the top of a closed luer-lock and allowed to overflow. 1ml of buffer was then pipetted into the syringe column and the luer-lock was immediately screwed onto the syringe. An additional 2ml of breaking buffer was added to the column and several drops of buffer were allowed to flow out. The luer-lock was then returned to the closed position. A total of 500ul of breaking buffer was added to the column and then 1ml of a 0.5ml bed volume Ni2+-agarose slurry was added to the column. The luer-lock was opened and agarose matrix was allowed to â€Å"gravity pack.† The column was pre-equilibrated with 5ml of breaking buffer and then the luer-lock was returned to the closed position. Ni2+-NTA Chromatography Separation Procedures 100ul of GCE was transferred into a centrifuge tube, labeled, and set aside. Breaking buffer was added to remaining GCE if content was less than 1ml. GCE was slowly applied to the Ni2+-agarose column and allowed about 5-10 minutes for protein to bind to column. The luer-lock was opened and 0.5ml of effluent was collected into 1.5ml centrifuge tube and labeled W1. This was repeated with the subsequent effluent labeled W2.The column was then observed under an ultraviolet light and fluorescence recorded. The column was then washed with 4ml of buffer in 0.5ml increments. The effluent was collected and labeled W3 to W10. The column was then washed again with a total of 5ml of breaking buffer. This effluent was discarded. A total of 5ml of elution buffer containing 10mM Tris, pH 8.0; 150mM NaCl, 300mM imidazole was added to the column in 0.5ml increments. The eluents were collected and labeled E1-E10.The column was then observed under a UV light and the fluorescence recorded. The W1-W6 and E1-E6 fractions were also observed under UV light and their fluorescence rec orded qualitatively. Determining Total Protein Amount A standard curve was created using six different samples of Bovine Serum Albumin (1mg/ml) of known amount. The amounts of BSA used all had a final volume of 50ul and included 0ug, 3ug, 5ug, 10ug, and 20ug total proteins. A total of 1ml of Bradford reagent was added to each, vortexed, and allowed to incubate for 10 minutes. The results where read using 200ul in a microtiter dish and read using a microplate reader set to 595nm. The results where plotted on a graph as absorbance (595nm) vs. BSA (ug) and a best fit line was drawn. The Bradford assay was then performed once on the W1-W6 and E1-E6 samples. Any samples whose absorbance fell outside the standard curve were repeated less sample in the assay. Once all samples fell within the standard curve, the Bradford assay was repeated two more times for each sample. The total protein amount was then extrapolated from the standard curve using the absorbance values. Estimating Purity and Molecular Weight The SDS-PAGE was prepared using a 12 percent resolving gel that was poured between the Bio-Rad glass plate â€Å"sandwich† and allowed to polymerize. A 5 percent stacking gel was prepared and added on top of the resolving gel, a comb was inserted, and the gel was allowed to polymerize. Once that polymerized, the combs were removed and the electrophoresis tank was set up. 15ul of G0, G3, GCE, W3, W4, E2, and E3 samples were added to the SDS-PAGE along with a standard molecular weight ladder. The samples were electrophoresed at 200volts for 45 minutes. The gel was then stained using Coomassie blue dye and the stain removed. Confirmation of rGFP 2-ÃŽ ²-mercaptoethanol was added to the centrifuge tubes containing the G0, G3, GCE, W3, W4, E2, and E3 samples and were loaded along with a molecular weight ladder and electrophoresed as described above. The stacker was removed and the resulting gel set up for transfer onto a nitrocellulose membrane for Western Blot analysis. The overall setup required a â€Å"building up† of components with the positive electrode base on the bottom, followed by filter paper soaked in transfer buffer, nitrocellulose paper above that, the SDS/PAGE layer, another layer of filter paper soaked in transfer buffer, Western blot solution was poured over all the components, and finally the negative electrode lid was locked into position. To ensure transfer, the nitrocellulose gel was stained using Ponceau S and allowed to incubate for two minutes on a rocker and then destained using ddH2O. The membrane was then blocked using 5% non-fat dry milk/TBS solution and incubated for 30 minutes on a rocking p latform. This was then and washed three times with 0.05%Tween 20/TBS with 5 minutes of incubation between each wash. It was then probed with mouse IgG anti-Xpress epitope MAb solution and allowed to incubate for 45 minutes. The 0.05%Tween 20/TBS wash was repeated in triplicate. A secondary probe using sheep IgG anti-mouse IgG conjugated horseradish peroxidase polyclonal anti-serum solution was performed as above and then washed in triplicate. The nitrocellulose gel was developed using TMB until desired intensity was reached and development was stopped with water and results recorded immediately. Results The expression of the target protein was doubly repressed in the G0 (uninduced) sample of E. coli. First, the Lac repressor protein binds to the lac operator and prevents transcription by T7 RNA polymerase (Garrett and Grisham 915-916). Second, T7 RNA was repressed by lysozyme protein that binds to T7 RNA polymerase and inhibits transcription. Expression of rGFP in the G3 (3 hour post induction) sample was made possible through the use of IPTG (Garrett and Grisham 914.) The purpose of IPTG was to repress the Lac repressor which resulted in T7 RNA polymerase being able to transcribe DNA downstream of the T7 promoter and expression of His6-Xpress-GFPuv, resulting in the fluorescent capable recombinant Green Fluorescent Protein. (Figure 1) This resulting recombinant GFP is a 279 amino acid protein. rGFP has a six Histidine tag at its N terminus between amino acids 5 and 10, an Xpress epitope between amino acids 24 and 31, Green Fluorescent Protein between amino acids 39 and 277, and a 3 amino acid end tag between amino acids 277 and 279. The chromophore is found between amino acids 103 and 105 in the DNA sequence. (Figure 2) Results of Ni2+-agarose affinity chromatography and Bradford assay indicated that the E3 (elution 3) sample contained the most rGFP activity with approximately 18,600 RFU (relative fluorescent units) and an estimate 43ug of total protein. The specific activity calculated for the sample was 433000 RFU/ mg of total protein. (Figure 3) The SDS-PAGE/Coomassie staining gave an estimate molecular weight for rGFP of 32kDa based on a total traveled distance of 2.3cm along the SDS/PAGE. The overall purity of the band was approximately 20 percent. The higher molecular weight band was most likely contaminants at about 45kDa and the lower molecular weight band was possibly a result of the degradation of the c-terminus at 27kDa. (Figure 4) Western Blot indicated prominent bands in the E3, E2, GCE, and G3 lanes. Lanes W4 and W3 showed very light bands and lane G0 shows an absence of bands. All visible bands appear at about 32 kDa and therefore confirm the presence of rGFP. (Figure 5) Conclusion The successful expression and purification of recombinant Green Fluorescent Protein is significant in the scientific community due to the possible uses for it in the future. Green Fluorescent Protein is significant because it provides an inexpensive and relatively easy method of detection. The possibility for real time detection means result could be obtained in real time. Future experiments will focus on linking rGFP to proteins during transcription and translation. This would result in a desired protein with a GFP tag whose fluorescence can then be used for identification. This should result in the ability to locate a target protein using the fluorescence of rGFP. Future applications of GFP could include incorporation into the genetic code of small mammals. These could encode fluorescent neurons which in turn could help further research in areas such as nerve tissue regeneration or other advances in neurobiology. Its unique properties of endurance could be exploited to understand how it can endure harsh environments and still regain functionality after remediation. This would have significant applications in molecular and cellular biology in understanding cellular degeneration and how help patients with diseases involving cellular degeneration. Bibliography Pan, Jing, Elizabeth Pickett, and Scott Rippel. Biochemistry Laboratory Lecture Notes. Dallas: UTD copy center, 2013. 225-289. Print. Pan, Jing, Elizabeth Pickett, and Scott Rippel. Biochemistry Laboratory Manual. Dallas: UTD copy center, 2013. 38-77. Print. Prasher, Douglas C., Virginia K. Eckenrode, et al. Primary Structure of the Aequorea victoria green-fluorescent protein. Gene. 111. (1992): 229-233. Print. Garrett, R., and Charles M. Grisham. Biochemistry. 4th ed. Belmont, CA: Brooks/Cole, Cengage Learning, 2010. Print. Ninfa, Alexander J., and David P. Ballou. Fundamental laboratory approaches for biochemistry and biotechnology. Bethesda, Md.: Fitzgerald Science Press, 1998. 89-107. Print.

The Individual and Society in the Communist Manifesto Essay -- Karl Ma

The Individual and Society in the Communist Manifesto The end of 19th century, Western Society was changing physically, philosophically, economically, and politically. It was an influential and critical time in that the Industrial Revolution created a new class. Many contemporary observers realized the dramatic changes in society. Among these were Karl Marx and Friedrich Engels who observed the conditions of the working man, or the proletariat, and saw a change in how goods and wealth were distributed. In their Communist Manifesto, they described their observations of the inequalities between the emerging wealthy middle class and the proletariat as well as the condition of the proletariat. They argued that the proletariat was at the mercy of the new emerging middle class, or bourgeoisie, and could only be rescued by Communism: a new economic form. During the 19th century, the proletariat was at the mercy of the bourgeoisie for survival. The bourgeoisie imposed conditions that required the proletariat to work under harsh, unsafe, and unhealthy industries. Cities were overcrowded, unsafe, and hazardous due to the many factors including the smoke from the factories that clouded the skies. Earlier, Friederich Engels had described the conditions of the proletariat in the town of Manchester. He saw, â€Å"everything which here [aroused] horror and indignation [as] of recent origin which [belonged] to the Industrial Epoch†.1 Not only did the proletariat have to work in unsafe factories but also was doomed to life long misery. Marx and Engels saw both the proletariat and the bourgeoisie as an outgrowth of feudal society. They argued that the bourgeoisie emerged as a result of exploration and discovery of new land, ... ... 8 Hadley Cantril, The Politics of Despair (New York: Basic Books, Inc., 1958), 41 9 Bertell Ollman, Alienation: Marx’s Conception of Man in the Capitalist Society (New York: Cambridge University Press, 1971), 131. 10 Neil Harding, â€Å"Marx, Engels and the Manifesto: Working Class, Party, and Proletariat.† Journal of Political Ideologies (1998): 13-44 11 Karl Marx and Friederich Engels, The Communist Manifesto (London: England 1848): Proletarians and Communists. 12 Hadley Cantril, The Politics of Despair (New York: Basic Books, Inc., 1958), 85-86, 87, 95. 13 Hadley Cantril, The Politics of Despair (New York: Basic Books, Inc., 1958), 87 14 Hadley Cantril, The Politics of Despair (New York: Basic Books, Inc., 1958), 94 15 Antonio Gilman, â€Å"The Communist Manifesto, 150 years later.† Antiquity (1998): 910- 913.