Admission essay Example | Topics and Well Written Essays - 500 words - 10

Admission - Essay Example ge of health information technology (HIT) employees is evident in the health centres and facilities since the industry started the implementation of electronic records. The 2008 bureau of labour pointed out that the by 2018, health facilities will require an addition of 35,000 workers. In America, there is a shortage of 50,000 HIT workers requires in the next five years according to the American Medical Informatics Association (Health Informatics and Health Information Management, 2014). There is the need to train HIT workers to deal with the data entry standards and the new coding methods in addition to the online insurance requirements. In the rural areas, the case is worse as the adoption of the health information technology and staff training due to the high costs of implementation. A number of the medical staff lacks experiences in the project management skills and the health care processes. The frequent training changes since technology changes rapidly and also due to inadequat e sustainability plans. The cost of hiring IT workers is expensive making it challenging for all the health facilities to employ new staff especially replacement due to attrition. The other issue experienced by the Health Management System is competition for IT workers in the other industries. All sectors of the economy are recruiting Information Technologists as they try to digitalize their industries (Health Informatics and Health Information Management, 2014). The candidates graduating from colleges and technical institutions offering IT training are not enough for the entire market. As a result, some of the industries such as health are understaffed. Some government and public hospitals do not pay well as compared to the private sector, which makes most of the IT specialists prefer working in the private industry as opposed to the public health facilities. The terms and conditions of employment are also good in the private sector leading to the exodus of IT staff from the health

Steve Jobs Essay Example | Topics and Well Written Essays - 500 words

Steve Jobs - Essay Example He worked with NeXT Computer and later on bought the Pixar in 1986. He returned to Apple in 1996 and purchased NeXT the same year. The company introduced products like iMac, iPod, iPad, iTunes, iPhone, Mac OS and many others. Jobs was time and again criticized for his complete mastery towards persuasion and salesmanship. He made keynote speeches and defied the odds (Siegler, 2011). Eventually he resigned in 2011 from Apple Inc. as the CEO but remained as a pivotal Chairman on the company’s board. This was the reason why Apple’s shares dropped around five percent in the after hour trading within the stock exchange. There was so much more that the naked eye could see when one thought of Steve Jobs. He was a born leader who showcased complete control over what he did, thought and showed to the world through the different tools, gadgets and devices. This is the reason why his death is mourned across the board for a number of reasons (Appleyard, 2009). Nearly the entire planet hailed him as an exceptional human being, who changed beliefs, stood up against the tough times no matter these concerned his own personal health domains and the ones he encountered at work. He was considered to be a very wealthy person who did not earn more than $1 million per year as CEO of Apple. He also held 5.426 million shares of Apple and another 138 million Disney shares. His net wealth is estimated at around $8.3 billion when the same was conducted in the year 2010, which made him America’s 42nd wealthiest individual. Steve Jobs was not known for his philanthropic acts in a public manner which is entirely opp osite to how Bill Gates showcases his philanthropic role (Kopun, 2011). However, Steve Jobs was known to have helped the poor and needy through private acts of charity. It was in the year 2003 when Jobs was diagnosed with cancer and in the following year (2004), he announced to the Apple employees that he was suffering from cancer in his pancreas. He died

Reggio Emilia Essay Example for Free

Reggio Emilia Essay The Reggio Emilia approach focuses on a childs natural development. Its child-centered and directed, taking the philosophy that learning must make sense to the student in order to be effective and meaningful. A childs point of view is completely respected and the student is encouraged to follow their own educational path. The method follow four key principles: The Reggio Emilia philosophy is based upon the following set of principles: children must have some say over what they learn; the senses play a big role in the learning process children must be able to touch, move, listen, see and hear in order to fully process something; children are encouraged to interact with other children and explore the world through material items and relationships; children should be encouraged to always express themselves and be given infinite means and opportunities to do so. Parental involvement is invited and encouraged. Many parents volunteer in the classroom and employ many of the methods found in the classroom at home. A variety of materials are used clay, paint, dramatic play among others. The approach was founded in the villages around Reggio Emilia, Italy after World War II. Parents were looking for a way to teach their children and found that the early years of development were the best time to help children figure out who they are as individuals. What is Documentation? Among many other possibilities, documentation is visible listening. The term documentation conjures up different meanings for different people. To our minds, one of the primary features of documentation as practiced in Reggio Emilia is a focus on how and what children learn. This focus is reminiscent of careful listening; thus, documentation, in many ways, is visible listening. Some of the elements of documentation include: conducting careful observations eveloping questions and tentative answers about how and what children are learning collecting evidence of individual and group learning interpreting observations and evidence in relation to your question(s) inviting others interpretations using the information to guide future teaching starting all over again Documentation can take many formsobservation notes, partial transcripts, audiotapes, a list of students responses to a prompt, photographs or videos of individual and group learning, and adult or student analyses of or reflections on student work.

Structures of Bacterial Tyrosinases

Structures of Bacterial Tyrosinases Tyrosinases oxidise phenolic hydroxyl groups of small molecules or large polymeric substrates such as proteins. Tyrosinases catalyse first the ortho-hydroxylation of the phenolic substrate and second its subsequent oxidation to quinone (Figure 1) with the concomitant reduction of oxygen to water. The reaction is chromogenic as the quinones produced can undergo further non-enzymatic polymerisation to form black eu-melanins and, when reacting with thiol groups, brownish pheo-melanins [14]. This process can be inhibited by antioxidants such as ascorbic acid, for example to prevent the browning reaction in food preparations [15]. Tyrosinase activity is generally measured by either determining the consumption of oxygen during the reaction or spectrophotometrically by following the increase of absorbance at 475 nm due to dopachrome formation. The cross-linking activity of tyrosinase on proteins is usually analysed by SDS PAGE, size-exclusion chromatography, UV spectroscopy or mass spectrom etry [16]. The active site of tyrosinases interacts with both the phenolic substrates and the co-substrate oxygen and it alternates among three different oxidation states. When in the oxy state, tyrosinase binds oxygen and is able to catalyse the hydroxylation of monophenols to diphenols, thus changing into the met form. The met form of tyrosinase is responsible for the oxidation of diphenols to quinones and the reaction turns the enzyme into the deoxy form that, upon binding molecular oxygen, returns to the oxy form. The met form is the resting state of the enzyme and it has been calculated that up to 85% of the enzyme is in this state when in solution [17, 18]. The inability of most of the enzymes in an enzyme population to act on monophenols explains why a significant lag phase is detected in the activity when monophenols are the substrate of the reaction. Bacterial tyrosinases have been divided in five types according to the organisation of domains and the possible requirement of a caddie protein for enzyme activity [12]. The necessity of a secondary helper protein (caddie protein) for secretion, correct folding, assembly of the copper atoms and activity of the enzyme is common to tyrosinases of type I, e.g. the enzyme from S. castaneoglobisporus and S. antibioticus [19, 20]. Type II tyrosinases are small, monomeric enzymes containing only the catalytic domain, which do not require additional helper proteins and are possibly secreted. An example is the tyrosinase from B. megaterium [6]. Type III tyrosinases are represented by the enzyme from Verrucomicrobium spinosum. Like the fungal tyrosinases it carries a C-terminal domain whose removal led to about 100-fold higher activity [21]. This supports the theory that the role of the C-terminal extension in plant and fungal tyrosinases is to keep the enzyme in an inactive form inside the ce ll [22-24]. Among the smallest bacterial tyrosinases reported (Type IV) are the ones produced by Streptomyces nigrifaciens (18 kDa) and Bacillus thuringiensis (14 kDa) [25, 26]. However, it is debated whether these proteins are true tyrosinases [12]. Type V tyrosinases include enzymes that do not carry the sequence features of tyrosinases but show features typical of laccase and have only marginal activity on tyrosine. For example, a membrane-bound tyrosinase active on the typical laccase substrate ABTS (NCBI ID: AAF75831.2) has been isolated from Marinomonas mediterranea. A tyrosinase with a classical substrate specificity that is activated by SDS (NCBI ID: AAV49996.1) has also been reported from the same organism [27]. Similar to catechol oxidases and the oxygen carrying haemocyanins, tyrosinases are type-3 copper proteins, containing two copper atoms in the active site. The absorbance spectrum of oxy-tyrosinases has a characteristic maximum in the UV region (330-345 nm). As reported for the structurally similar catechol oxidases, a fluorescence intensity maximum at 330 nm upon excitation at 280 nm is also detected [28, 29]. Copper is essential for the catalytic activity of tyrosinases. The crystal structure of these enzymes has demonstrated the presence of two copper ions in the catalytic core (Table 1). In all tyrosinases of different origins and in the haemocyanins each of the copper ions is coordinated by three histidine residues that are found in a characteristic pattern in the primary structure (Figure 2). In the tyrosinase from Streptomyces glaucescens, for example, the key role of histidines at position 37, 53, 62, 189, 193 and 215 in the coordination of copper, and thus in catalytic activi ty, was confirmed by the decrease of activity upon their substitution with other amino acids [30, 31]. Various additional residues have been identified to have a function in fungal and bacterial tyrosinases, either being essential for or modulating tyrosinase activity. Sequence analysis and various mutagenesis studies have been performed in order to identify the residues necessary for the activity of the enzyme. In tyrosinase sequences from plants and fungi, the N-terminal signal peptide, when present, is followed by a conserved arginine residue that marks the beginning of the central catalytic domain and that forms a pi-cation interaction with a conserved C-terminal Y/FXY tyrosine motif, where X is any amino acid [32]. These residues are conserved also in bacterial tyrosinases (Supplementary file 1). Substitution of the N-terminal conserved arginine (R40) has been reported to abolish the production of tyrosinase from V. spinosum [21]. Two single-amino acid substitutions have been reported to improve the catalytic activity of the tyrosinase from Rhizobium etli CFN42. The independent r eplacement of proline at position 334 and of aspartic acid at position 535 (Supplementary file 1) with a smaller residue such as serine (P334S) or glycine (D535G), respectively, led to a significant enhancement of the catalytic activity and melanin formation [33-35]. In the tyrosinase from B. megaterium, a single substitution of arginine by histidine within the copper B binding region (R209H) has been sufficient for a 1.7-fold improvement of the activity towards tyrosine (monophenolase) and for a 1.5-fold reduction of activity on L-DOPA (diphenolase), whereby the overall protein stability was not affected [36]. The crystal structure of the tyrosinase from B. megaterium showed that this arginine is positioned at the entrance of the active site in a flexible position and plays a role in the docking of the substrate [6]. However, the conservative substitution of the corresponding residue asparagine 190 to glutamine (N190Q) in S. glaucescens tyrosinase abolished the catalytic activity, indicating that this residue was possibly involved in hydrogen bonding at the active site [30]. Moreover, the conservative substitution of the residue aspartic acid 209 (D209E) has been reported to stabilise the oxy-form of the same enzyme [37]. To our knowledge, no study has investigated the role of the oxygen binding motif PYWDW [38] with regards to the affinity for oxygen in tyrosinase. The affinity for the co-substrate oxygen has been evaluated for the tyrosinase from Streptomyces antibioticus that carries the PYWDW motif. It was found that this enzyme had a three-fold lower dissociation constant (kD) for oxygen than the A. bisporus tyrosinase [39, 40] that carries a PFWDW motif, i.e. 16.5 ÃŽ ¼M compared to 46.6 ÃŽ ¼M. The analysis of the characterised bacterial tyrosinases evidenced the presence of functionally active variants of this motif (Supplementary file 1 and 2), e.g. PYWNY in the tyrosinase from M. mediterranea, PFWDW in tyrosinase from R. etli, PYWEW in the tyrosinase from B. megaterium, PYWRF and PYWNW in the tyrosinases from Ralstonia solanacearum. Mutational studies have also addressed the interaction of tyrosinases from streptomycetes and their caddie protein. In S. antibioticus, the two histidine residues at positions 102 and 117 of the caddie protein MelC1 have been found to be crucial for the biosynthesis of active tyrosinase [41]. The available crystal structures of bacterial tyrosinases and their mutant forms have been obtained from Gram-positive S. castaneoglobisporus and B. megaterium (Table 1). While the B. megaterium tyrosinase formed crystals containing only the enzyme, the S. castaneoglobisporus tyrosinase required the presence of a second protein, referred to as caddie protein, to stabilise its structure [4]. Moreover, the structure of the Streptomyces tyrosinase has been solved in different states of oxidation. Aiming at understanding the interaction between tyrosinase and caddie protein, tyrosinase has been crystallised in the presence of mutant forms of the caddie protein (Table 1). Likewise, the fungal tyrosinase from A. bisporus was crystallised as a tetramer in a complex with a second protein, a lectin-like protein [7]. Both intracellular and secreted bacterial tyrosinases have been isolated and characterised. For example, the tyrosinases from Streptomyces nigrifaciens, Bacillus thuringiensis, M. mediterranea, R. solanacearum and Thermomicrobium roseum were isolated from cell biomass and the ones from S. antibioticus, S. glaucescens, S. castaneoglobisporus, Streptomyces albus, B. megaterium, Sinorhizobium meliloti, Aeromonas media, R. etli and V. spinosum were either isolated from the culture medium or predicted to be secreted [19, 21, 25, 26,42-51]. The twin-arginine signal peptide is often found in cofactor-binding oxidoreductases that undergo complete folding in the cytoplasm prior to secretion to the periplasmic or extracellular space. Twin-arginine type signal peptides [52] could be identified in the N-terminal region of tyrosinases from R. solanacearum (34-amino acid long) and V. spinosum (33-amino acid long). A more detailed analysis of the sequence retrieved for the tyrosinase from R. etli a nd the alignment with the other sequences of tyrosinases (Supplementary File 1) suggests the possibility of incorrect open reading frame prediction. The true N-terminal methionine may be M112 (underlined in Supplementary file 1) as it aligns with the initial residue of the tyrosinase from R. solanacearum (number 15 in Supplementary file 1) and is followed by a predicted twin-arginine signal peptide of 31 amino acids [51]. Thus, we suggest that these proteins purified from the cell biomass but carrying a signal peptide for secretion are localised in the periplasm. Tyrosinases, also from bacteria, and their caddie proteins generally lack conserved cysteine residues (for comments see [11, 12]). The paucity of cysteine residues, and thus disulphide bonds, allowed, however, the isolation of tyrosinases with significant thermal stability, e.g. the enzyme from B. megaterium had an optimum temperature of 50Â °C [48]. A single cysteine residue is conserved in proximity of the second histidine residue of the copper A binding motif in the characterised tyrosinases from M. mediterranea, R. solanacearum, S. meliloti, R. etli and V. spinosum (Supplementary file 1). A cysteine residue at this position has been found to be covalently bound to a histidine residue two positions forward in, for example, the fungal tyrosinase from Neurospora crassa [53], the plant catechol oxidase from I. batata [8] and haemocyanins from the snail Helix pomatia [54]. The function of this unusual cysteine-histidine bond is not established, but it could confer structural rigidity to the copper-binding region and affect the redox potential [8]. Replacement of this cysteine residue (C84) with serine abolished the production of the tyrosinase from V. spinosum [21]. Type-3 copper proteins carrying six conserved cysteines (forming three in silico predicted disulphide bonds) and characterised by significant thermal stability have been reported in fungi [26]. No mutagenesis study has addressed a possible improvement of the thermal stability of bacterial tyrosinases by introducing disulphide bonds. However, in silico analysis revealed the possible presence of one disulphide bond in the tyrosinases from R. solanacearum and S. meliloti and two in the enzymes from M. mediterranea and R. etli (Dianna software, http://clavius.bc.edu/~clotelab/DiANNA). The tyrosinase from S. castaneoglobisporus and the one from B. megaterium share approximately 30% sequence similarity with a catechol oxidase from Aspergillus oryzae that showed a melting temperature above 70Â °C and a ha lf-life of 20 hours when incubated at 50Â °C [29]. It should be noted that the tyrosinase from A. media exhibits different sequence features when compared to the other enzymes. The sequence alignment with bacterial tyrosinases shows that none of the typical signature motifs (copper A and B regions, oxygen binding motif and tyrosine motif) are present (see Supplementary file 1). Moreover, this enzyme has a predicted 23-amino acid long signal peptide [50] and shows strong sequence similarity to bacterial periplasmic proteins that are responsible for the uptake of peptides and involved in nutrition and sensing of the environment [55].

Life in Maycomb in To Kill a Mockingbird :: English Literature

What impressions are there of life in Maycomb in To Kill a Mockingbird Maycomb is seen as a tired and sleepy town, where nothing happens. Maycomb is a very isolated town itself, so it is insular. There are no nearby towns or villages so are very alone. This makes the town so boring and tired. Nothing very exciting happens in Maycomb, if there is something reasonably different from to Maycomb’s usual routine then the community get both excited but also scared. For example when it snowed Scout was scared that the sky was falling, but Jem knew what it was and got very excited and managed to make a snowman. When the Radleys’ house is supposedly broken into by Negroes, and the mad dog incident are both examples of Maycomb’s panic at something different. The trial is a very prominent example of something that Maycomb finds exciting and new, the new part being a white man trying to prove a black man innocent. The Maycomb community make a family day out or picnic out of the trial, even thought is a very serious and unpleasant court case. â€Å"It was a gala occasion.† â€Å"The courthouse square was covered with picnic parties sitting on newspapers, washing down biscuit and syrup with warm milk from fruit jars.† Nothing has changed in Maycomb, it is very traditional and tries to keep as much of its past as possible. Maycomb town is obsessed with background; it clings to old views the main one being prejudice against blacks. Maycomb needs the likes of Atticus and his children to bring the town forward. For example the Maycomb County Courthouse: â€Å"a view indicating a people determined to preserve every physical scrap of the past.† Racism in Maycomb has existed since the Indians. It shows how Maycomb is based on extreme racial and prejudice. â€Å"If General Jackson hadn’t run the Creeks.† Maycomb is also shown as a town that has not been brought up to present times by the state of the actual town. It is very poor and in disrepair, it only has one taxi. When Miss Maudie’s house catches on fire the fire engine does not reach Maycomb for a while because Maycomb is a very isolated town and not very important so therefore there is now nearby fire station. â€Å"In rainy weather the streets turned to red slop; grass grew on the sidewalks, the courthouse sagged in the square.† Maycomb seems to be an innocent, peaceful town when first seen. Harper Lee proves to show this is a misconception made by outsiders. Throughout the novel we learn the ways and life of Maycomb. â€Å"Maycomb County had recently been told it had nothing to fear but fear

Bitterness in Faulkners A Rose For Emily :: A Rose For Emily, William Faulkner

Essay a rose for Emily In William Faulkner's short story "A Rose for Emily," Emily's lack of social skills, exclusiveness and bitterness display Emily's refusal to adapt to the present. In the short story "A Rose for Emily", Emily displays her lack of social skills when the other ladies in the story try to call for her and she refuses to see them. Emily was not very social with the other towns? people. When the town gets the mail system for free, Emily refuses to let the towns? people put a mail box or postal number letters outside of her home. Emily was very unsocial. Emily never left the house much, she would have everything she needed brought to the house for her. She portrays her refusal to adapt to the present by not keeping up with the new mailing system and by refusing to pay taxes. She wanted to keep everything how it was when her father was alive. Emily was not willing to accept the new changes in her life, she wanted to live in the past where she was comfortable. Emily is very excluded from the rest of the town. Emily hardly ever came out of her house and refused to let anyone in on her life. Emily displays her refusal to adapt to the present by not wanting to let anyone in when her father passed on because she believed that he was still alive. Emily was very close to her father and when he passed on it was hard for her to adapt to the present. Emily never left the house much that her father left her, and when she did she did not talk to anyone at all. Emily was very private with her life, she made sure that no one knew anything about her life. Emily portrays her refusal to adapt to the present by keeping herself very excluded from the present time. The people that lived in the town with her would have to ask her servant questions just to receive any information about her life at all. Emily did not even let the servant into her personal life, she kept all her thoughts and feelings very private from the rest of the world. After Emily?s father passed away, Emily became very bitter with the world. She refused to pay taxes to the town because her father had given a lot of money to the town.

Assess the View That Life in a ‘State of Nature’

The state of nature Is the term used to describe a lawless state of human behavior, wherein all people are free of legal and moral restraint. It would create a state where all people would be able to act on their wants and desires without fear of punishment from a governing body, as there wouldn't be one, and that man would only have to fear the retaliation from other people against their actions. In this essay, I will be outlining the views of both Hobbes and Locke on the state of nature and drawing a conclusion from their opinions.Hobbes' view on the state of nature is that such a thing would lead only to a state of war. He believed that without moral or legal constraints, mankind will simply pillage, murder, and plunder In order to get what they desire, regardless of the views of others. In a state of war, man will use power as he sees fit In order to survive and with no clear definition of rights or duty, each Individual will be free to Judge the rights and duties of others and of themselves.There will be no duty to keep other people safe and out of harm and no-one will have the explicit right to live or to keep heir property. If another claims that you hold something he needs to survive, you would have no right to deny him as there is no law or right outlining that it was yours and yours alone. As our desires are never satisfied and we have a continuous want of things, man will continue to overturn others if it means he gets what he wants in life, whether or not he truly needs it.He believes in the state of nature translating to a state of anarchy, as no human will ever be satisfied with what they have and will always strive for more. Hobbes claims that In a lawless state, we may not wish direct arm onto others, but we will be constantly aware that other people may wish to harm us. In order to prevent being the volt, we would attack first In order to stay alive, thus becoming the aggressor. Self-preservation In a lawless state, In Hobbes' opinion, would o nly ever lead to conflict as man turns on man In order to keep themselves alive.Due to this, we would never trust another person and the lack of alliance or allegiance would lead to us all being equally vulnerable. So despite the lack of rights or duty, each of us are equal in a state of nature, as we are all equally able to be pushed over by the person beside us, whether they are friend or otherwise. Hobbes is very much in agreement that living in a state of nature would be truly awful. Locke, however, doesn't completely agree.He doesn't believe – as Hobbes does – that scarcity In society and living in a state lawlessness would lead to man killing man In order to stay alive. He believes that people will provide themselves with natural moral principles that we are all inclined towards. Locke drew this belief from his belief in God and the creation of Man and all things on the Earth. By this logic, we have a duty to protect others from harm. We are therefore obligated, as God's creations, to punish those that cause harm to others, and those principals would be our natural obligations.He also believes that we cannot claim property unless our labor helped create what is on the land, but we still have no lawful right to it and the supposed right to it is not dependable. He proposed that removal from a state of law would create a form of democracy among men where they would govern themselves and keep themselves in equal measure in order to create a fair semblance of society. Locke thinks that society can exist in a state of nature and exist informally, so he disagrees with the statement that living in a state of nature would be awful in any sense.He believes that people can and will work together to protect themselves and each other as we have an obligation to care for other people as a natural instinct. By Locker's reasoning, man would eventually enter into an unspoken social contract and form a crude government to better protect their rights and pro mote organization in their society. I believe that although a state of nature would initially lead to man taking whatever he pleased from others and doing what he had been previously unable to do, eventually a form of society would emerge.People cannot continue without governing themselves and eventually they would create some form of law in order to govern themselves and protect their rights and duties. Initially living in a state of nature would be awful because there would be the breakaway from lawful restraint and that new freedom would lead to complete uproar as the population of the world indulged in all they had been unable to do. I still, however, believe that Locker's state of things would prevail and that man would find a way to organize themselves in order to survive and beat the inevitable scarcity.