Jazz Essay Example | Topics and Well Written Essays - 1250 words - 2

Jazz - Essay Example Miles Davis one of the most famous jazz players worked on the modern jazz musical concepts that have helped to grow this genre to a next level. The very first jazz melody â€Å"Agitation† gives the listener a very exotic feeling by using his trumpet. It combines the different aspects from the musical perspectives. The song follows quick transitions with specific background sounds. The background music keeps the flow of the music steady and continuous. The trumpet is used throughout the music owing to its main emphasis on the intensity to the certain point it shows. Miles Davis improvisation in this specific type of Jazz know as Modal Jazz music has helped specifically to stretch out the harmony of the music into certain parts which makes the it more systematic and helps the music to proceed in an organized manner. Miles Davis stretched out certain improvements in different types of Jazz music, such as bebop, hard bop, cool jazz, modal jazz and jazz fusion. This specific piece from Miles Davis joins in with different instruments to give the feel of the environment producing a story of its sort. This modal jazz requires knowledge of musical nodes beforehand. Miles Davis, the most well-known protagonist of Jazz Music history had been on top of creating creative method for Modal Jazz. The video specifically has piano to create the specific background rhyme to the music that follows throughout the length of the video. Throughout the video there are specific changes in the chords which at times follow a certain transition and after a break follow another set of harmonies. In its historical aspect, this piece shows the jazz music that followed up in the 60’s. Miles Davis, who was a pro trumpeter, performed his music based either solo or like in the video, along with different instruments such as French horn, Tuba, Wood winds. The video reflects on the charismatic methods of attaining the attention by progressive music. This video stretches

leadership :: essays research papers

There are two broad approaches to seeking to shape values in society. One is by being "salt and light" in the world (Mt 5:13,14), where by living distinctively Christian lifestyles we seek to influence those around us, and through this the values, decisions and priorities adopted by our communities. The other approach is to confront a particular value, decision or priority which the Christian community feels is out of place, and this may require a more structured and focused campaign. This page offers a six step approach to run such a campaign, whilst click here to view some thoughts on being salt and light. The six steps below seek to help a leader put some structure around an influencing campaign. This may be related to a specific proposal within a community, or more generally trying to influence the values that the community adopts. This community may be a geographic community : neighbourhood, town or even country, or it may be another form of network eg work or interest related. 1. Know what you're trying to achieve. Â · Write down some specific aims for your influencing. If possible, make these aims measurable. Â · These may be related to a specific issue that has arisen within the community, or it may be seeking to change more general values and behaviours. Don't overload with issues - it's better to focus on one or two and achieve something, than make little progress against a broad agenda 2. Decide on your audience and message. Â · Who are the people who hold the key to achieving your objectives? This may include those with formal responsibility (councillors and MPs) , those who can influence them (respected thought leaders and influential organizations) and influential channels such as the media. Â · What is the action you want them to take, and therefore, what is the message that you need to deliver to them to persuade them to take such action? Can you write it down - physically writing the message down is very worthwhile as it ensures that there is sufficient clarity of thinking. Â · The same message can be received very differently when delivered by different people or organizations. Taking the time to identify the most credible and capable people to deliver the message is important. In some cases, you may want to focus on people with specific skills, knowledge or position who can speak with authority.

Quantification of Proteins in Solution by Spectrophotometer Essay

Introduction: Absorption spectroscopy is a common method for finding the concentration of proteins or protein complexes in a solution. Proteins absorb light at specific wavelengths and can be defined by the equation A = log (Io/I). This equation states that an absorbance at a specific wavelength, A is equal to the log of the ratio of incident light intensity (Io), to transmitted light intensity (I). A spectrophotometer can be used quantitatively and qualitatively. A spectrophotometer is used qualitatively to obtain an absorption spectrum, which can be obtained by plotting the absorbance values, over the range of wavelengths tested for the solution. This helps to find out the suitable wavelength that the compound absorbs maximum. And the spectrophotometer is used quantitatively by using the Beer-Lambert Law; Log [ Io/I] = A = ÃŽ ¾cl, where ÃŽ ¾ is the molar extinction coefficient (unit = Lmol-1cm-1), helps to define the absorbance of the protein, c is the concentration of the substance (mol liter-1), and l is the path length of the light (unit = cm) through the medium. Log [Io/I] is called optical density or absorbance of the substance, and does not have units. Also, an absorption spectrum is created, which deals with absorption and wavelength (nm) of light used, with which â€Å"maximum absorption† is observed. Maximum absorption is when most of the solution particles are absorbed, and this happens at a specific wavelength. Since the Beer Lambert law is useful only for a range of wavelengths, it is not applicable to all protein solutions. In this experiment, an absolute standard was calculated using BSA, so that the concentrations of the other unknown protein solutions can be determined (Lambert et.al, 2011).The different assays used for this protein quantification were Lowry, Bradford (Coomassie Blue) and UV direct. Protein assays help to determine the amount of desired particle present (Srivastava, 2008). The aim of this lab is to understand the various aspects of spectrophotometry and its applications in biochemistry, such as quanitification of protein solutions. Methods: (Carleton University, 2012) The steps were followed without any changes made. Results: Figure1. Absorption spectrum of 6Ãâ€"10-5M p-np solution in 0.02M NaOH, for wavelength range between 330-800nm using a Novaspec spectrophotometer. Sample Calculation: c = 6Ãâ€"10-5M l = 1cm A = 1.166 The Beer Lambert equation is A = Æ cl Rearranged, Æ  = A/cl Æ  = 1.166/(6Ãâ€"10-5)*1 Æ  = 1.94Ãâ€"104 L mol-1 cm-1 Table1. Values of extinction coefficient (Lmol-1cm-1) determined using Beer-Lambert Law. Figure2. Absolute standard curve obtained for BSA test protein solution with the 3 different assays tested (Lowry, Coomassie Blue, UV). Table 2. Absorbance values recorded for different protein dilutions (2X, 5X, 10X) for the three assays used, namely Lowry, Coomassie Blue and UV direct. Sample Calculation for BSA stock protein: * Lowry Equation of line from Fig2; y = -5Ãâ€"10-7Ãâ€"2 + 0.0016x + 0.038 For 5 fold; y = 5 * 0.44 = 2.20 Substituting in equation; 2.20 = 5Ãâ€"10-7Ãâ€"2 + 0.0016x + 0.038 X1 = 1600  µg/ml = 1.6mg/ml For 10 fold; y = 10 * 0.23 = 2.30 Substituting in equation; 2.30 = 5Ãâ€"10-7Ãâ€"2 + 0.0016x + 0.038 X2 = 1600  µg/ml = 1.6mg/ml (X1 + x2)/2 = 1.6mg/ml * Coomassie Blue Equation of line from fig2; y = -7Ãâ€"10-7Ãâ€"2 + 0.002x + 0.0219 For 5 fold; y = 5 * 0.36 = 1.80 Substituting in equation; 1.80 = -7Ãâ€"10-7Ãâ€"2 + 0.002x + 0.0219 X1 = 1428.57  µg/ml = 1.4mg/ml For 10 fold; y = 10 * 0.20 = 2.00 Substituting in equation; 2.00 = -7Ãâ€"10-7Ãâ€"2 + 0.002x + 0.0219 X2 = 1428.57  µg/ml = 1.4mg/ml (x1+ x2)/2 = 1.4mg/ml * UV direct Equation of line from fig 2; y = 0.0006x + 0.0175 For 2 fold; y = 2 * 0.42 = 0.84 Substituting in equation; 0.84 = 0.0006x + 0.0175 X1 = 1374.16  µg/ml = 1.4mg/ml For 5 fold; y = 5 * 0.15 = 0.75 Substituting in equation; 0.75 = 0.0006x + 0.0175 X2 = 1179.16  µg/ml = 1.2mg/ml (x1 + x2)/2 = 1.3mg/ml Discussion: Figure 1 shows the absorption spectrum of stock solution (6Ãâ€"10-5M), p-nitrophenol and 0.02M NaOH, and from the graph it can be inferred that 400nm is the wavelength of maximum absorption because absorption is noted to be the highest at this point. Absorbance is noted to increase when wavelength increases till it reaches the point of maximum absorption, after which it decreases till it nearly reaches zero. It is best to consider wavelength of maximum absorption because stronger the intensity, the more accurate will be the readings for absorbance. As seen from table 1, the path lengths remain the same as the cuvettes used were of the same size. The Beer-Lambert Law states that Abs = Æ .c.l, where Æ  = molar extinction coefficient, c = concentration of protein solution, and l = path length of light through medium. Thus, it is noted that absorbance and path length share a directly proportional relationship, i.e. if path length increases, absorbance increases as well. It was clear ly observed in the wide and narrow test-tubes, that as the path length was doubled, the absorbance value doubled too (Srivastava, 2008). Also, from the same equation, it can be determined that absorbance and concentration share a directly proportional relationship meaning that as the concentration decreases, it directly affects the absorbance value obtained, and this value decreases too. Thus, as seen for the four cuvettes tested (in Table 1) as the concentration is halved in every cuvette, the absorbance value is halved correspondingly as well. It is known that the Beer-Lambert law says absorbance is proportional to number of absorbing molecules, and that this is valid for a variety of compounds over a wide range of concentrations. But even as the molar extinction coefficient is seen to be attributed to wavelength, it is true only for monochromatic light (Lambert et.al, 2011). The relationship can be stated as â€Å"Æ  is a measure of the amount of light absorbed per unit concentration†. Molar extinction coefficient is a constant for a particular substance, therefore according to the Beer-Lambert Law it is expected that if the concentration of the solution is halved so is the absorbance. A compound with a high molar extinction is very effective at absorbing light (of the appropriate wavelength), and hence low concentrations of a compound with a high molar extinction can be easily detected. In the values determined (Table 1), the experimental values are in accordance with the theoretical statement except for one cuvette. The cuvette no.3 with Æ  = 1.8Ãâ€"10-4 L mol-1cm-1 does not agree with the trend. Thus it can be deduced that due to experimental error, the Æ  value is inaccurate. Also, from the equation it is understood that Æ  and path-length are inversely proportional as well (i.e. Æ  = Abs/cl) that means that as path-length increases, Æ  decreases, assuming that the concentration is kept constant. But the experimental values do not agree with this statement, because it is seen that as the path-length increases so does the molar extinction coefficient, Æ . Biochemical methods are applied for to determine protein concentration in solutions. Many techniques are less used because they have limitations such as reduced sensitivity, time available for the assay, or they are highly specific about the amino acids in the protein solution being tested. But for e very protein, the component amino acids are different, so there is no single assay that can be used for quantification of all proteins. The absorbance assays use the method of testing the intensity of the color produced by the protein solutions when chemical reagents are added to it. A â€Å"standard protein† whose concentration is known, is treated using the same chemical reagents and thus an absolute standard curve is obtained (Boyer, 2000). In this experiment, the standard used was Bovine Serum Albumin (BSA). Development of color is significantly better in BSA than any other protein, and this makes it one of the most preferred test solutions for quantification of proteins (Antharavally et.al, 2008). Hence figure 2 is obtained by performing the three suitable assays on BSA to produce a standard curve, also it can be noted that only the UV direct gave a straight line passing through zero, whereas the Lowry and Coomassie Blue gave curved lines, passing through zero. Table 2 shows the absorbance values recorded, for different dilutions of the test protein in three different assays. With the help of the values obtained in Table 2, and with the equations obtained from Figure 2, the concentration of protein (mg/ml) was calculated and presented in Table 3. Since all the values in Table 3 were deduced from the equation of standard curve BSA, it is considered as the absolute standard, and the other test protein solutions are known as the relative standards. Using the values from Table 3, taking BSA as the absolute standard, the almost actual concentration of the protein (mg/ml) can be concluded, and they are 1.6 (mg/ml) for Lowry assay, 1.4 (mg/ml) for Coomassie Blue and 1.3 (mg/ml) for UV direct. For Lowry assay, the concentration value for all test proteins was 1.6 mg/ml, which must mean that the value obtained is accurate. For Coomassie blue, BSA and Hemoglobin were the same (1.4mg/ml), Ovalbumin and Lysozyme had similar values of 1.9mg/ml, and 1.8mg/ml respectively, whereas Gamma globulin showed 2.5mg/ml. The value for Gamma globulin is off because of experimental error, of spilling some of the contents from the cuvette while transferring it to the spectrophotometer for calibration. For UV direct, BSA and Ovalbumin have similar readings (1.3mg/ml and 1.5mg/ml respectively), Gamma globulin is 2.5mg/ml, but Lysozyme is 5.9mg/ml and Hemoglobin is 3.8mg/ml. The reason for this could be due to the fact that UV direct helps to identify the presence of aromatic compounds indicating that Lysozyme and Hemoglobin contain aromatic compounds present in them. The Lowry protein assay is the most common and one of the more sensitive, but it is time consuming, on the other hand Coomassie blue (the Bradford assay) is much more sensitive as compared to Lowry, and requires less time too. They both show change of color with proteins. As for UV direct method, it is one of the faster methods too, and it is helpful to identify aromatic compounds because aromatic residues absorb 280nm light (Boyer, 2000). The Lowry procedure can detect protein levels as low as 5 µg (Boyer, 2000). It depends on the color development by the reagent Folin-Ciocalteu. Peptide bonds are formed under alkaline Cu2+ conditions and reduced from Folin-Ciocalteu phosphomolybdate-phosphotungsten by aromatic amino acids (tyrosine and tryptophan) to heteropolymolybdenum blue. The standard curve obtained with BSA helps to determine concentration of unknown protein solutions (Antharapally et.al, 2008). In the case of Coomassie blue, it is more efficient than Lowry because even though there is variation with different proteins, there is very less interference by non protein components (Borley, 2000). Therefore, according to literature, Coomassie Blue is the most preferred protein assay but this contrasts the experimental inferences, because through experimental procedure it was seen that Lowry method gave the most accurate and precise results. With this experiment, the method to quantify unknown protein concentrations has been understood. Also, that this process must be performed carefully to avoid irrational experimental errors. References: Antharavally B.S, Bell P.A, Haney P, Mallia K.A, Rangaraj P. 2008. Quantitation of proteins using a dye–metal-based colorimetric protein assay. Analytical Biochemistry. 385; 342-245. Boyer R, 2000. Modern Experimental Biochemistry, third edition. Addison-Wesley Longman, Inc. USA. (41-45). Lambert J.B, Gronert S, Lightner D.A, Shurvell H.F, 2011. Organic Structural Spectroscopy, second edition. Pearson Education, Inc, New Jersey. (401, 404) Srivastava M.L, 2008. Bioanalytical Techniques. Alpha Science International, Ltd. Oxford, UK. (58,118)

The Pros and Cons of Three Types of Online Communities-...

An online community is a network of people who come together and communicate online, usually because of a common interest or goal. There are many different types of online communities. Some examples of online communities are: email distribution lists, message boards and newsgroups, instant message (IM) services, chat rooms, blogging sites, social networking sites such as MySpace and Facebook, and online classrooms/school groups. I intend to discuss three of these types of online communities – chat rooms, social network sites, and online classrooms/school groups – and look into the pros and cons of using each of these. First, I will talk about internet chat rooms. A chat room is a site where users can talk live to other users. Users†¦show more content†¦There is no face to face with online chat rooms. Chat rooms enable people to act or say things in ways that they may not normally if they were face to face. This could also be a pro or a con, depending on the situation. One last con of chat rooms would be that, although you can talk to other people almost as if you were face to face instead of waiting for a response as you would have to with an email, you still have to wait for the other person to be online. If you want to chat with someone and they are not online, the chat room isn’t going to do you much good. Sometimes people will prearrange times to get online and chat with another person. This is one way to overcome this con. Next, I will discuss social networking sites. Some examples of social networking sites would be MySpace, Facebook, Classmates.com, and Twitter. Social networking can be a wonderful and fun way to keep in touch and communicate with your family, friends, and colleagues. They can save you time and effort. If you need to get in touch with someone, and you are both members of the same social networking site, you can quickly and easily send him/her a message on the site. Instead of having to make arrangements and plans to meet at a certain place, at a certain time, you can discuss things on the site. Social networking sites can also be a great place to get in touch with old friends or talk to people that you don’t often get to see. You canShow MoreRelatedSocial Research 2.0: Virtual Snowball Sampling Method9226 Words   |  37 PagesInternet Research Emerald Article: Social research 2.0: virtual snowball sampling method using Facebook Fabiola Baltar, Ignasi Brunet Article information: To cite this document: Fabiola Baltar, Ignasi Brunet, (2012),Social research 2.0: virtual snowball sampling method using Facebook, Internet Research, Vol. 22 Iss: 1 pp. 57 - 74 Permanent link to this document: http://dx.doi.org/10.1108/10662241211199960 Downloaded on: 11-05-2012 References: This document contains references to 48 other documentsRead MoreTechnology Essay11684 Words   |  47 PagesRelationships are being built online or through phones. 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