Structure of Collagen Proteins

Structure of Collagen Proteins Collagen forms the majority of the protein that is found in mammalian organisms and constitutes 30% of the total protein mass of a human. By being used as a gibbet, collagen is utilized by body cells towards the molding of their surroundings. This eventually creates an atmosphere favorable for normal cell function as well as the development of the tissues. Apart from providing mechanical support, collagen have several ligands which improve the performance of factor receptors and integrins that can control cellular procedures such as cell union, cell migration commonly known as chemotaxis, remodeling of tissues, as well as the healing of wounds. Collagen comprises of between 25 and 35 percent of the total protein tissue present in a mammals body. The hair, connective tissues as well major connective tissues are made up of collagen. Collagen is structured into fibrous strands, precise to their role (Lamberg 226). Collagen is broken down into several sub-units known as tropocollagen. A Tropocollagen has a form of a triple helix attached to a hydrogen bond to form a polypeptide chain. A sample Collagen is predominantly made up of amino acids. It has high levels of proline and glycine alongside hydroxylysine and hydroxyproline. Vitamin C is essential during the building up process of collagens, although it is not a direct constituent of the amino acid chain. Currently, there are 29 known collagen types of fiber. The most prevalent in the body are the type 1, 2, 3 and 4. The type one collagen is present in all soft tissues inclusive of the internal organs, the bones and tendons as well as the skin. On the other hand, Type 2 collagen is found in the cartilage of the body structures while type 3 is common in reticular membranes and tissues. Additionally, Type 4 collagen is only found in the membranes of the cell basement. If the formation of collagen happens inside the cell, then the process is known as vivo formation. In this process, three peptide chains appear in the ribosomes all along the rough endoplasmic reticulum. On the contrary, if the collagen is formed outside the cell, then the method of formation is known as vitro formation. According to this process, Collagen is produced in a laboratory through manual procedures. One collagen is made up of a chain of five small tropocollagen molecules. The protein strand is made up of the ami no acid base. The staggered arrangement of Tropocollagen molecules permits them to adhere to adjoining strands and thus providing the fibers with additional strength (Murrieta 16). By designation, a collagen molecule is made up three ÃŽÂ ± chains also known as polypeptide chains and contains on the least, one domain having a repeating Gly-X-Y sequence in all of the essential chains (Myllyharju and Kivirikko 26). At present, all vertebrates are made up of at least 27 collagen types each having 42 distinct ÃŽÂ ± chain. A number of collagens make up homotrimers having three ÃŽÂ ± chains whereas others have two or even three distinct ÃŽÂ ± chains. The X and Y locations can contain any amino acid apart from glycine. Characteristically, proline is only available in the X spot with 4-hydroxyproline in the Y position. Whereas 4-hydroxyprolines are necessary for the solidity of the triple helix, glycines are essential for filling the three chains into a coiled-coil configuration. This formation is exemplified as a left-handed helix that is wound about a regular axis to form a triple helix with a one-dimensional right-handed superhelical pitch, producing the ultimate arrangement of a rope-like rod. Collagen Types With the aim of avoiding confusion, collagens are given roman numerals in the order that they have discovered. Whilst referring to the composition of a collagen, each of the three ÃŽÂ ± chains is initially quantified for chain number (1, 2, or 3) and thereafter the type of the collagen is identified. For instance, ÃŽÂ ±2 (I) refers to the second ÃŽÂ ± chain is type I whereas ÃŽÂ ±1 (II) refers to the first ÃŽÂ ± chain is type II collagen. Collagen division into families is made essentially by the apparatus and organization of matrix gathering. The following are the nine collagen families along with their respective types. fibril-forming (I, II, III, V, XI, XXIV and XXVII), fibril-associated collagens with interrupted triple helices (FACITs) positioned on the exterior of fibrils (IX, XII, XIV, XVI, XIX, XX, XXI, XXII and XXVI), hexagonal form (VIII and X), basement membrane forming (IV), beaded filaments (VI), affixing fibrils for basement membranes (VII), transmembrane domains (XIII, XVII, XXIII and XXV), and the family of type XV and XVIII collagens (Kivirriko 123). Definite collagens are articulated in a tissue definite approach, as depicted in types II, IX and XI that are set up almost entirely in cartilage, although type XVII is just found in skin hemidesmosomes. In addition, some collagen forms are ordinary in the majority of extracellular matrices, as in the case of type I. Furthermore, collagen fibrils that frequently comprise more than one kind of collagen. Such a type I collagen may also possesses smaller amounts of types III, V and XII. Additional heterogeneity in the super family may be as a result of unusual splicing of the records of several genes as well as the use of option promoters in a number of genes. Through the huge figure of structurally distinct members of the super family involves being caught up in numerous biological functions (Kadler 124). Collagen assembly Most of the collagens have a similar formulation procedure thats characteristically linked with type I. By starting inside the cell, three peptide chains are produced in ribosomes all along the Rough Endoplasmic Reticulum (RER). The chains formed are then referred to as preprocollagens and each one of them possess registration peptides on the end as well as a signal peptide. Upon completion, these peptide chains are then sent into the lumen of the RER somewhere they are slashed into their procollagen shapes. Whilst in the RER, the chains progress to undertake a chain of efficient changes. Initially, the lysine as well as proline amino acids are hydroxylated, a procedure that depends on ascorbic acid. Subsequently, precise hydroxylated amino acids are glycosylated, permitting the three chains to relate into a triple helical formation. Lastly, the procollagen is transported to the Golgi apparatus for packaging as well as secretion in a process known as exocytosis. The moment the collagen is outside the cell, it is again reordered into a functional matrix. listing peptides are sliced via procollagen peptidase, to form tropocollagen, which can which has the potential to aggregate itself and form collagen fibers. In the case of non-fibular collagen, the N- and C-propeptides remain in the cell where they assist in directing super molecular assembly. Following the formation of fiber, inter-chain cross-linking of collagen take place between lysine and hydroxylysine residues subsequent to deamination from lysyl oxidase (Kivirriko 123). Molecular Structure A collagen molecule also known as tropocollagen is a sub-unit of bigger collagen collection as in the case of fibrils. The molecule has a diameter of around 1.5nm and is 300nm long. It is made up of three polypeptide strand, each having left-handed helix conformation. In addition, the three left-handed helices are twisted collectively to form a right handed super helix, a joint quaternary structure alleviated by several hydrogen bonds. The association of type I collagen with possible fibrillar collagens to form a branded triple helix is referred to as microfibril. Every microfibril is interdigitated with its adjoining microfibrils to an extent that may propose that they are independently unbalanced even though within collagen fibrils they are so well structured to be crystalline. Since glycine is the least amino acid having no side chain, it has a unique responsibility in fibrous structural proteins. In the formation of collagen, Gly is essential at all third position since the assemblage of the triple helix holds this residue at the inner (axis) of the helix, wherever there is no gap for a larger side group than glycines sole hydrogen atom. For similar basis, the rings of the Pro and Hyp should point outward. The function of the two amino acids is to help stabilize the triple helix. Fibrillar Structure The tropocollagen subunits impulsively assemble itself with recurrently spread out ends, into even bigger arrays in the extracellular vacant places of tissues. In the case of fibrillar collagens, the molecules are spread out from each other by 67nm. Each and every D-period has 4 and fraction molecules of collagen. This is due to the fact that if you divide 300 by 67 doesnt yield a large integer. Therefore in each D-period duplicated of the microfibril, there exists a part having five molecules in a cross-section known as overlap. On the other hand, the part consisting of four molecules is known as the Gap. The triple-helices may also be prearranged in a hexagonal or quasi-hexagonal arrangement in section, both the overlap region and the Gap. Equally the gap and overlap regions (Xie 549). There exists a covalent is cross connections in the triple helices, as well as an amount of covalent cross connections involving tropocollagen helices outlining a well structured collection like fibrils. Bigger fibrillar bunches are produced with the support of numerous diverse categories of proteins as well as diverse collagen brands, proteoglycans and glycoprotein to shape the diverse kinds of fully-grown tissues from alternating blends of the similar major players. The insolubility of collagens has been a barrier to the research carried out on monomeric until it was discovered that tropocollagen from immature animals could be removed since by then, is it not yet completely cross connected. Nonetheless, progress in microscopy systems microscopy of electron (EM) and atomic force microscopy (AFM) and the diffraction of X-ray have facilitated those doing research to acquire gradually more comprehensive figures of collagen configuration in situ. This afterward progress is predominantly significant to improved perception of the system in which collagen configuration influences communication in both intracellular and cell-matrix stages, and how tissues are build in development and restoration, and altered in growth and infection. For instance by means of AFM -based nanoindentation, researchers have been able to show that a particular fibril of collagen is a varied substance alongside its axial course with extensively diverse automatic functions in its fissure and partly covered areas, connecting with its diverse molecular associations in these two areas. The fibrils of collagen are partially crystalline collections of molecules made of collagen. Collagen fibers (filaments) are bunches of fibrils. Fibrils/ collections of collagen are prearranged in diverse arrangements and attentiveness in a variety of tissues to offer unstable tissue elements. In fillets, complete triple helices of collagen are positioned in a parallel, reeled display. Forty nm spaces involving the endings of the tropocollagen subdivisions-roughly equivalent to the breach section- almost certainly act as nucleation position for the deposition of long, hard, fine crystals of the mineral component, which is (approximately) hydroxyapatite, Ca10(PO4)6(OH)2 with some phosphate. It is in this way that certain kinds of cartilage turn into bone. Type I collagen gives bone its tensile strength. Prolyl 4-Hydroxylase (P4H) As formerly stated, hydroxylation of the Y-position proline residues is a critical modification for generating stable triple helical collagen. This modification is carried out in the lumen of the RER by the enzyme prolyl 4-hydroxylase (Tandon 199). The vertebrate forms of these P4Hs are ÃŽÂ ±2 ÃŽÂ ²2 tetramers in which the ÃŽÂ ² subunit is identical to the protein disulfide isomerase PDI (Myllyharju, 2003). Various isoforms of the catalytic a subunit have been found in organisms of varying size and complexity; from humans to Drosophila. Another family of P4Hs in the cytoplasm has been uncovered and has been linked to the regulation of the hypoxia-inducible transcription factor HIF. Cytoplasmic P4Hs have no PDI subunit, require different sequences flanking the prolines that are hydroxylated, and have markedly higher Km values (Kivirikko and Myllyharju 199). No overall amino acid sequence homology is detected between the collagen and the cytoplasmic HIF P4Hs, with the exception of critical catalytic residues. HIF is continuously synthesized and under normoxic conditions a critical proline residue in a -Leu-X-X-Leu-Ala-Prosequence is hydroxylated by the cytoplasmic P4Hs, not by collagen P4Hs. The resulting 4-hydroxyproline residue is essential for HIFÃŽÂ ± binding to the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex for subsequent proteasomal degradation. However, under hypoxic conditions hydroxylation ceases, allowing HIFÃŽÂ ± to escape degradation and instead forms a stable dimer with HIFÃŽÂ ² (Jaakkol a, 2001). Once formed, the dimer is translocated into the nucleus and becomes bound to the HIF-responsive elements in a number of hypoxia-inducible genes, such as those for erythropoietin, vascular endothelial growth factor, glycolytic enzymes and even for the ÃŽÂ ±(I) subunit of human type I collagen (Takahashi 200). Illinois Institute of Technology biologist Joseph Orgel used the high-energy X-rays produced by the APS to examine the structure of collagen, a protein that composes more than a quarter of all protein in the human body and forms the principal component of skin, teeth, ligaments, the heart, blood vessels, bones and cartilage. In these tissues, collagen molecules pack themselves into overlapping bundles called fibrils. These fibrils, which each contain billions of atoms, entwine themselves into collagen fibres that are visible to the naked eye (Xuyang 2760). Scientists have known the basic molecular structure of collagen since the 1950s, when several different international groups of scientists discovered that it had a triple-stranded helical structure. However, researches had never before had the ability to study the structure of an entire fibril in the same way that they could study an individual collagen molecule, according to Orgel. Orgel and his team performed diffraction studies on intact collagen fibrils inside the tendons of rat tails in order to understand just how the protein functioned within unbroken tissue. We tried to draw a highly accurate map of the molecular structure of tissues, Orgel said. By doing so, we hope to transform a very basic understanding that we have of the molecular structure of tissue into a much more tangible form. Since the scientists kept the tendon tissue intact, they could see how the collagen molecule binds to collagenases, a class of enzymes which when working properly help to regulate the normal growth and development of animals but when malfunctioning can lead to the metastasis of cancerous tumors or rheumatoid arthritis. The visualization of this interaction could help drug developers to create an inhibitor to prevent the pathological action of the enzyme, Orgel said. Previous studies of the structure of collagen had looked only at crystals of small fragments of the protein, so scientists had little idea of how it looked within intact tissue. Its impossible to get the information that we did by removing tiny chunks of the tissue, Orgel said. We couldnt obtain this data by single-crystal crystallography. This research was made possible only because of the BioCAT beam line provided by the APS. Applications Collagen has been extensively used in beauty surgical procedures, hemostats, mechanism coatings, recovery fluids, formulation recipients, tablets, cartilage rebuilding, medicine release, in addition to skin substitutes for patients with burns. However, both medical and cosmetic use is declining because most commercially available collagens are derived from bovine or porcine tissues. Mainly enriched in type I collagen, these preparations also contain small amounts of type III as well as other collagens that are difficult and expensive to remove from the desired material. Moreover, there is a high rate of allergic reactions from animal-derived collagens, causing prolonged redness. Using collagen derived from cows also poses the risk of transmitting prion diseases such as bovine spongiform encephalopathy (BSE). The scientific community also uses collagen in its studying its role in tissue development and disease. Extracting sufficient quantities of nontraditional or less prominent colla gens is a costly and difficult task (Kadler 196). A processed form of collagen commonly used is gelatin. Derived from denatured collagen, gelatin is composed of a mixture of collagen chains of different length, structure, and composition. This distribution depends on what type(s) of collagens are extracted, the extraction method, as well as the pH and ionic strength of the solution used for processing. Because gelatin is a heterogeneous composition, especially in size and isoelectric point, the resulting products will inevitably have variable gelling and physical properties. This variability presents a significant challenge for medical applications where stability, safety, and control are necessary (Crissman 192). Cheaply produced recombinant collagens and gelatins have the potential to alleviate many of the issues associated with animal derived versions. Given the large number of aforementioned applications there is also a large market in this area. Scalable technology is needed to make microbial expression of recombinant collagens a viable alternative to tissue extraction. Using microbes to engineer collagen allows for greater control over collagen synthesis and organization, which in turn increases the quality, consistency, and safety of collagen production. It would also provide an easy platform for introducing altered primary sequences into recombinant collagens. Such genetic control over collagen structure is crucial in studying the impact of specific mutations on collagen structural hierarchical assembly and associated functions and also would allow for the creation of designer collagen-mimetic materials. Recombinant expression would also allow for the extraction of sufficient quantities of native collagen forms that are present at low levels which are otherwise mainly characterized at cDNA and genomic levels. This would allow for structural and functional analysis of these rarer collagens (Baneyx 114). Biomaterials applications for collagens in hemostats, as skin substitutes, in cartilage reconstruction, and for drug delivery can benefit from the improved purity of cloned sources of collagen. Purity in this case would include both reducing other extracellular matrix components that may be carried through the purification process leading to potential inflammatory responses, or bioburdens with potential impact on human heath, particularly neurological disorders due to prion concerns. Recombinant human collagen seems to avoid immune reactions previously described and is therefore more biocompatible. Recombinantly derived collagen was shown to have superior mechanical strength and haemostatic activity compared to animal derived collagen when formed into a matrix. They can be altered to include bioactive peptide sequences as well as to be collagenase resistant. Recombinant gelatins can be tailored to alter their gelling temperature by controlling their hydroxyproline content. Moreover, they have been shown to be less allergenic. As they are widely used in the food and drug industry, recombinantly derived gelatins can be made animal-free and thus open for consumption by vegetarians (Baez 252).

Ernest Hemingway and Zelda Fitzgerald :: Biography Biographies Essays

Ernest Hemingway and Zelda Fitzgerald Zelda Sayre Fitzgerald was born July 24th, 1900 to Anthony Sayre, a judge of the Alabama Supreme Court, and Minnie, a once aspiring actress. She was considered a sought-after Southern belle who had a collection of soldiers' insignia pins by the time she met Scott Fitzgerald at the age of twenty. However, Zelda refused marriage until 1920 when the publication of This Side of Paradise gave Scott the wealth and economic stability, which she demanded. The first few years of their marriage were characterized by extravagant spending, but shortly after the birth of their only child, Frances Scott "Scottie" Fitzgerald, the couple began frequent arguments usually triggered by alcohol (http://www.sc.edu/fitzgerald/biography.html). In 1924, when the Fitzgeralds went to France, Zelda became smitten with a French naval aviator named Jozan, who unlike Scott was tall and athletic. Although it is not known whether the two consummated their affair, many suspect that it was Scott who demanded tha t the two stop seeing each other that summer (Milford 110). In Paris, Fitzgerald met Ernest Hemingway with whom he formed a friendship based largely on his admiration for Hemingway's personality and genius. The Fitzgeralds remained in France until the end of 1926, alternating between Paris and the Riviera. Although Scott and Ernest were very close at this time, they usually only included their wives, Zelda and Hadley, in social gatherings as "wives of writers" (Milford 116) rather than in their intellectual and literary discussions. Ernest became upset when Zelda said to Hadley at this time, "I notice in the Hemingway family you do what Ernest wants"(Milford 116). Thus, Ernest who always did things his way, was greatly disgusted over the amount of influence that Zelda had over her husband (Bruccoli 21). Legend also has it that at Ernest and Zelda's first encounter in the summer of 1926, Hemingway took Fitzgerald aside saying that Zelda was crazy when she asked "Ernest, don't you think Al Jolson is greater than Jesus"(Bruccoli 22). Zelda, on the other hand, thought Hemmingway was a "bogus," a "phony he-man," and a "pansy with hair on his chest". Scott was disappointed by their mutual dislike as he had hoped Zelda would admire Hemingway as much as he did. Hemingway recounts his 1921-1926 Paris years in A Movable Feast. In "Hawks Do Not Share," he introduces Zelda at "a very bad lunch" in the Fitzgerald's "gloomy" apartment.

Solution for Classic Pen

Case Study: Classic Pen Company 1- Cost of production of the pens according to ABC method: INDIRECT FINGE BENEFICT INDIRECT LABOR TOTAL indirect Labor Indirect Labor Computer System Other Overhead Total overhead Quantity Overhear Rate 8,000 20,000 28,000 Production Runs Setup Time Administration Run Machines 14,000 11,200 2,800 8,000 2,000 14,000 22,000 11,200 4,800 14,000 150 526 4 10,000 146. 67 21. 29 1,200. 00 1. 40 Total 28,000 10,000 14,000 52,000 Overhead distribution among the cost Pool Amount of overhead 22,000. 00 11,200. 00 4,800. 00 14,000. 00 2,000. 00 100,000 Quantity 150 526 4 10,000 Rate Amount of overhead 8,000 100,000 0. 08 Quantity 100,000 Blue Production Runs Setup Time Administration Run Machines Total Overhead by pen Quantity of pen Overhead by unit of pen Black 0. 50 0. 20 0. 08 0. 38 1. 16 Blue 7,333. 33 4,258. 56 1,200. 00 7,000. 00 19,791. 89 50,000 0. 40 Black 7,333. 33 1,064. 64 1,200. 00 5,600. 00 15,197. 97 40,000 0. 38 Red 5,573. 33 4,854. 75 1,200. 00 1,260. 00 12,888. 09 9,000 1. 43 Purple 1,760. 00 1,022. 05 1,200. 00 140. 00 4,122. 05 1,000 4. 12 Blue 4,000. 00 50,000 . 08 Black 3,200. 00 40,000 0. 08 Red 720. 00 9,000 0. 08 Purple 80. 00 1,000 0. 08 Direct Fringe Benefit distribution among pen Direct Fringe Benefit Quantity of pen Direct Fringe Benefit by pen Cost of Production Material Cost Direct Labor Direct Fringe Benefit Overhead Cost Cost of Production 0. 50 0. 20 0. 08 0. 40 1. 18 Red 0. 52 0. 20 0. 08 1. 43 2. 23 Purple 0. 55 0. 20 0. 08 4. 12 4. 95 2- Actions that will be taken by Classic Pen Company As shown by the table below, the traditional cost shows the company is realizing benefit for all its pens.Blue Material Cost Direct Labor Overhead Cost Cost of Production Quantity of pen Cost of Production according to the Traditionnal Actual Unit Selling Price Profit/Loss $ Black 25,000 20,000 10,000 8,000 30,000 24,000 65,000. 00 52,000. 00 50,000 40,000 1. 30 1. 30 1. 50 1. 50 0. 20 $ 0. 20 $ Red Purple 4,680 550 1,80 0 200 5,400 600 11,880. 00 1,350. 00 9,000 1,000 1. 32 1. 35 1. 55 1. 65 0. 23 $ 0. 30 But with ABC Method we have realized that the unit selling price of the Red pen and Purple pen respectively $1. 5 and $1. 65 are less than the cost of production, therefore we expect that the Classic Pen Company will increase the unit selling price of these two pens. Blue Material Cost Direct Labor Direct Fringe Benefit Overhead Cost Cost of Production according to ABC Actual Unit Selling Price Profit/Loss $ 0. 50 0. 20 0. 08 0. 40 1. 18 1. 50 0. 32 $ Black 0. 50 0. 20 0. 08 0. 38 1. 16 1. 50 0. 34 $ Red 0. 52 0. 20 0. 08 1. 43 2. 23 1. 55 (0. 68) $ Purple 0. 55 0. 20 0. 08 4. 12 4. 95 1. 65 (3. 30) Solution for Classic Pen Case Study: Classic Pen Company 1- Cost of production of the pens according to ABC method: INDIRECT FINGE BENEFICT INDIRECT LABOR TOTAL indirect Labor Indirect Labor Computer System Other Overhead Total overhead Quantity Overhear Rate 8,000 20,000 28,000 Production Runs Setup Time Administration Run Machines 14,000 11,200 2,800 8,000 2,000 14,000 22,000 11,200 4,800 14,000 150 526 4 10,000 146. 67 21. 29 1,200. 00 1. 40 Total 28,000 10,000 14,000 52,000 Overhead distribution among the cost Pool Amount of overhead 22,000. 00 11,200. 00 4,800. 00 14,000. 00 2,000. 00 100,000 Quantity 150 526 4 10,000 Rate Amount of overhead 8,000 100,000 0. 08 Quantity 100,000 Blue Production Runs Setup Time Administration Run Machines Total Overhead by pen Quantity of pen Overhead by unit of pen Black 0. 50 0. 20 0. 08 0. 38 1. 16 Blue 7,333. 33 4,258. 56 1,200. 00 7,000. 00 19,791. 89 50,000 0. 40 Black 7,333. 33 1,064. 64 1,200. 00 5,600. 00 15,197. 97 40,000 0. 38 Red 5,573. 33 4,854. 75 1,200. 00 1,260. 00 12,888. 09 9,000 1. 43 Purple 1,760. 00 1,022. 05 1,200. 00 140. 00 4,122. 05 1,000 4. 12 Blue 4,000. 00 50,000 . 08 Black 3,200. 00 40,000 0. 08 Red 720. 00 9,000 0. 08 Purple 80. 00 1,000 0. 08 Direct Fringe Benefit distribution among pen Direct Fringe Benefit Quantity of pen Direct Fringe Benefit by pen Cost of Production Material Cost Direct Labor Direct Fringe Benefit Overhead Cost Cost of Production 0. 50 0. 20 0. 08 0. 40 1. 18 Red 0. 52 0. 20 0. 08 1. 43 2. 23 Purple 0. 55 0. 20 0. 08 4. 12 4. 95 2- Actions that will be taken by Classic Pen Company As shown by the table below, the traditional cost shows the company is realizing benefit for all its pens.Blue Material Cost Direct Labor Overhead Cost Cost of Production Quantity of pen Cost of Production according to the Traditionnal Actual Unit Selling Price Profit/Loss $ Black 25,000 20,000 10,000 8,000 30,000 24,000 65,000. 00 52,000. 00 50,000 40,000 1. 30 1. 30 1. 50 1. 50 0. 20 $ 0. 20 $ Red Purple 4,680 550 1,80 0 200 5,400 600 11,880. 00 1,350. 00 9,000 1,000 1. 32 1. 35 1. 55 1. 65 0. 23 $ 0. 30 But with ABC Method we have realized that the unit selling price of the Red pen and Purple pen respectively $1. 5 and $1. 65 are less than the cost of production, therefore we expect that the Classic Pen Company will increase the unit selling price of these two pens. Blue Material Cost Direct Labor Direct Fringe Benefit Overhead Cost Cost of Production according to ABC Actual Unit Selling Price Profit/Loss $ 0. 50 0. 20 0. 08 0. 40 1. 18 1. 50 0. 32 $ Black 0. 50 0. 20 0. 08 0. 38 1. 16 1. 50 0. 34 $ Red 0. 52 0. 20 0. 08 1. 43 2. 23 1. 55 (0. 68) $ Purple 0. 55 0. 20 0. 08 4. 12 4. 95 1. 65 (3. 30)

A Brief Note On International Business And The...

STUDENT ID: S00801773 International Business the Multinational Enterprise INB 430 Movement of Daimler AG in India Word Count: 1460 Contents Introduction 3 Barriers in Globalization 3 Movement to foreign market 5 Global Strategic Partnership 6 Conclusion 7 References 8 Introduction Moving to new country is never easy for any organization and lot of brainstorming and research needs to be done before offering the product in completely new arena. A fundamental shift has been occurring in the world economy. There has been a move away from a world in which national economies were relatively isolated from each other by barriers to†¦show more content†¦Every country has its own set of rules and regulations for doing business and with industry like Automobile there is more need of stringent set of rules. (Giddens, 2002)Government sets different set of regulations to stop foreign players to enter into the market. Few of them are higher tariffs which is basically imposing higher taxes on the companies or on the imported products which restricts trade and makes the imported goods more costly for customers. Moreover such tariffs pave way for domestic companies to grow themselves so as to compete with global players. (Bansal, 2001) Few other controls are †¢ Import Controls - Generally the foreign players come up with a very low priced products which can affect the sale of domestic players, and hence to protect them, the Government comes up with certain controls that does not allows the players in the market to price the ticket below a certain level. (Amin, 1995) †¢ Nontariff barriers –There are various kinds of other barriers as well which is not related to taxes, but are posed to restrict foreign players. Few of them are †¢ Quotas – Quota help the industry to establish domestic players and impose quota system whereby certain percentage of the sales or maybe certain segments within the country is only accessible to domestic players, and hence foreign players cannot

Cultural Conflict Can Bring Dramatic Changes to Socity...

Culture Conflict Can Bring Dramatic Changes to Societies Things Fall Apart written by Chinua Achebe analizes the coming of the white man and its results on the culture of the people of Umuofia. The coming of the white man brought about culture conflict which affects the people of Umuofias religion, their judicial system and their social life. Their lives are transformed in many different ways and change the perspective they have. The arrival of the white man affects the people of Umuofias religion and cause culture conflict. The people of Umuofia have many gods. Agbala- the oracle of the Hills and Caves. People come from far and near to consult it (12). People consult it when they have a discussion or altercation with their†¦show more content†¦Their egwugwu who gives justice is feared by the women and their children. Whenever the egwugwu is approaching, the women and children always shout and run away (63). They also dont unmask the masquerade. The masquerades identity is not known by anyone who doesnt belong to the clans secret cult. The religion of the people of Umuofia is totally completely different from the white mans religion. This situation caused a cultural conflict between the white man and the people of Umuofia. The white mans desire is to impose his religion on the people of Umuofia. The white man believes in one God which he believes has created the heaven and the earth. He also said his God made the entire world and the Umuofias gods. He wanted the people of Umuofia to abandon their gods and follow his own religion. The white men belittle the people of Umuofias gods by saying different things about their gods. The white man says that the people of Umuofias god are gods of deceit who tell them to kill their fellow and destroy innocent children. The white man says your gods are not alive and cannot do you any harm and they are made of piece of wood and stone (146). Hearing and seeing all these from the white man, the people of Umuofia were not satisfied with the white mans religion which was a cause for a culture conflict. The coming of the white man also influenced the form of justice in

A Christian Service Of Memorial - 934 Words

Hello family and friends†¦welcome. Today we have come together to remember sister Jean, but this is not just a service of remembrance. This is a Christian service of memorial. In that sense, we have come here to proclaim our faith in a God who has promised us a future; an eternity; in life beyond the grave. Jean lived this faith. Even after she was diagnosed with cancer, she came to a deep understanding of who Jesus is and what He had done for her, for us†¦so even in the midst of her pain and suffering she experienced God’s love and presence in a powerful way†¦she found the Way, she met the Way†¦she placed her complete trust and love in Him, and it changed her life forever. In the book of John chapter 14 verses 1 through 6 we read (Read†¦show more content†¦In my Father’s house, there are many rooms. If it were not so, would I have told you that I go to prepare a place for you? 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Ruby Brown Commentary free essay sample

Ruby Brown, a poem written by Langston Hughes is describing a black woman that faced both racism and sexism in her life. Like in most of his work, Langston Hughes uses motifs of color and white. Hughes characterizes Ruby in a way that allows us to see the restrictions she had in her way and her ability to mentally over come them. The visual imagery in the beginning talks about bright and golden sunshine but in actuality it was not. The characterization of Ruby shows her to be an upright respectable person but it does not matter because she is black. Her life was sad because she had so much talent but it did not get to show. This social commentary is significant because Ruby’s looks gave her advantages but even worse disadvantages. More specifically the poem reflects how the social issues of racism and sexism can hurt the confidence of anyone. We will write a custom essay sample on Ruby Brown Commentary or any similar topic specifically for you Do Not WasteYour Time HIRE WRITER Only 13.90 / page Hughes uses Ruby Brown to convey the theme that a hold in opportunity can greatly harm unsecure women. Irony is also used to convey how Ruby moves away from her original life in order to make sure she has security and happiness. The tone of the poem plays a big part in the readers’ thoughts of the poem itself and of Ruby. The last stanza sets the tone in a guilty and shameful manor. This is significant because it reveals the main idea of the poem and enhances the theme. Through this poem, Langston Hughes is trying to convey to the reader that changing who you are is not good and will only lead to your downfall. In regards the time-period that it was written in, Hughes is telling the black population to stand proud of what color they are and to not give burdens that the white people had placed on them.