11:02 PM SCl9-Q4-MOD1.pdf - Saved \( \alpha_{0}^{\infty} \) 17 CO_Q4_Science 9_ Module 1 What I Can Do Activity 2.4: Draw Time! The Scenario It was morning of January 21, 2021, you heard a distant gunshot. You went outside and found out that the neighbor's rooster was dead with a gunshot wound. Immediately the barangay police together with the crime investigators looked into the case. They gathered some information that would help solve the case. As a witness, your job is to help investigators pinpoint the location at which the shots originated by illustrating the scene. The details in the incident are stated below. Crime Scene Notes: The bullet that entered the rooster's body has been matched to a .45 caliber pistol. This gun releases bullets with an exit velocity of \( 260 \mathrm{~m} / \mathrm{s} \). The bullet entered the rooster at an angle of 12 degrees from the horizontal. The following suspects in the neighborhood are registered owners of .45 caliber pistols. The suspects were also found in their residence during the time of the incident. Arthur Abellardo: He has a record of noise violations for loud parties he frequently holds at his residence 2.54 kilometers away from the crime scene. Carlos Sarial: He has no criminal record and residing 2.8 kilometers away from the crime scene. Ramon Ricorda: Ramon has a record that includes possession of prohibited drugs. He served time in prison and was released after the completion of his sentence. He is currently residing 3.05 kilometers away from the crime scene. The rooster was lying on the ground when it was shot. The fence is \( 1.73 \mathrm{~m} \) above the ground where the rooster was. Note: Focus only in making the illustration/sketch. Calculating and solving the case is not required. Rubrics can be found on the next page. Disclaimer: The characters, places, incidents in the scenario are hypothetical. Any resemblance to actual persons living or dead or actual events are purely coincidental. 22 of 30 CO_Q4_Science 9_Module 1
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You are a world-famous physicist-lawyer defending a client who has been charged with murder. It is alleged that your client, Mr. Smith, shot the victim, Mr. Wesson. The detective who investigated the scene of the crime found a second bullet, from a shot that missed Mr. Wesson, that had embedded itself into a chair. You arise to cross-examine the detective. You: In what type of chair did you find the bullet? Det: A wooden chair. You: How massive was this chair? Det: It had a mass of $20 \mathrm{kg}$.You: How did the chair respond to being struck with a bullet? Det: It slid across the floor. You: How far? Det: Three centimeters. The slide marks on the dusty floor are quite distinct. You: What kind of floor was it? Det: A wood floor, very nice oak planks. You: What was the mass of the bullet you retrieved from the chair? Det: Its mass was $10 \mathrm{g}$. You: And how far had it penetrated into the chair? Det: A distance of $4 \mathrm{cm}$ You: Have you tested the gun you found in Mr. Smith's possession? Det: I have. You: What is the muzzle velocity of bullets fired from that gun? Det: The muzzle velocity is $450 \mathrm{m} / \mathrm{s}$ You: And the barrel length? Det: The gun has a barrel length of $62 \mathrm{cm} .$ With only a slight hesitation, you turn confidently to the jury and proclaim, "My client's gun did not fire these shots!" How are you going to convince the jury and the judge?
(Denizli'de ikamet edip Aydın Adnan Menderes Üniversitesi'nde çalışan bir akademisyen sıklıkla Aydın Denizli arasında otomobili ile seyahat etmektedir ve yol üzerinde özellikle Nazilli ilçesinde denk geldiği kırmızı ışıklardan dolayı oldukça şikayetçidir. Yeterli sayıda yolculuktan elde ettiği veriler sonucunda hem gidiş hem de dönüş güzergahı için Nazilli yolu üzerinde karşılaştığı kırmızı ışık sayılarına ilişkin aşağıdaki ortak olasılık dağılım fonksiyonu verilerini elde etmiştir. Burada X, Denizli'den Aydın'a gidiş güzergahında Nazilli yolu üzerinde karşılaşılan kırmızı ışık sayısını, Y ise Aydın'dan Denizli'ye dönüş güzergahında Nazilli yolu üzerinde karşılaşılan kırmızı ışık sayısını belirtmektedir.) (Gidiş yolunda karşılaşılan ortalama kırmızı ışık sayısını hesaplayınız.) (Dönüş yolunda karşılaşılan kırmızı ışık sayısının standart sapmasını hesaplayınız.)
Paul A.
Figure $3-24$ shows the amino acid sequence of bovine insulin. This structure was determined by Frederick Sanger and his coworkers. Most of this work is described in a series of articles published in the Biochemical Journal from 1945 to 1955. When Sanger and colleagues began their work in $1945,$ it was known that insulin was a small protein consisting of two or four polypeptide chains linked by disulfide bonds. Sanger's team had developed a few simple methods for studying protein sequences. Treatment with FDNB. FDNB (1-fluoro-2,4-dinitrobenzene) reacted with free amino (but not amide or guanidinium) groups in proteins to produce dinitrophenyl (DNP) derivatives of amino acids: Acid Hydrolysis. Boiling a protein with $10 \%$ HCl for several hours hydrolyzed all of its peptide and amide bonds. Short treatments produced short polypeptides; the longer the treatment, the more complete the breakdown of the protein into its amino acids. Oxidation of Cysteines. Treatment of a protein with performic acid cleaved all the disulfide bonds and converted all Cys residues to cysteic acid residues (see Fig. $3-28$ ). Paper Chromatography. This more primitive version of thin-layer chromatography (see Fig. $10-25$ ) separated compounds based on their chemical properties, allowing identification of single amino acids and, in some cases, dipeptides. Thin-layer chromatography also separates larger peptides. As reported in his first paper (1945), Sanger reacted insulin with FDNB and hydrolyzed the resulting protein. He found many free amino acids, but only three DNP-amino acids: $a-$ DNP-glycine (DNP group attached to the $\alpha$ -amino group), $a$ -DNP-phenylalanine, and $\varepsilon$ DNP-lysine (DNP attached to the $\alpha$ -amino group). Sanger interpreted these results as showing that insulin had two protein chains: one with Gly at its amino terminus and one with Phe at its amino terminus. One of the two chains also contained a Lys residue, not at the amino terminus. He named the chain beginning with a Gly residue "A" and the chain beginning with Phe "B." (a) Explain how Sanger's results support his conclusions. (b) Are the results consistent with the known structure of bovine insulin (see Fig. 3-24) ? In a later paper ( $1949)$, Sanger described how he used these techniques to determine the first few amino acids (amino-terminal end) of each insulin chain. To analyze the B chain, for example, he carried out the following steps: 1. Oxidized insulin to separate the A and B chains. 2. Prepared a sample of pure B chain with paper chromatography. 3. Reacted the B chain with FDNB. 4. Gently acid-hydrolyzed the protein so that some small peptides would be produced. 5. Separated the DNP-peptides from the peptides that did not contain DNP groups. 6. Isolated four of the DNP-peptides, which were named B1 through B4. 7. Strongly hydrolyzed each DNP-peptide to give free amino acids. 8. Identified the amino acids in each peptide with paper chromatography. The results were as follows: B1: $ \alpha$ -DNP-phenylalanine only B2: $ \alpha$ -DNP-phenylalanine; valine B3: aspartic acid; $\alpha$ -DNP-phenylalanine; valine B4: aspartic acid; glutamic acid; $a$ -DNP-phenylalanine; valine (c) Based on these data, what are the first four (amino-terminal) amino acids of the B chain? Explain your reasoning. (d) Does this result match the known sequence of bovine insulin (Fig. $3-24$ )? Explain any discrepancies. Sanger and colleagues used these and related methods to determine the entire sequence of the A and B chains. Their sequence for the A chain was as follows: Because acid hydrolysis had converted all Asn to Asp and all Gln to Glu, these residues had to be designated Asx and Glx, respectively (exact identity in the peptide unknown). Sanger solved this problem by using protease enzymes that cleave peptide bonds, but not the amide bonds in Asn and Gln residues, to prepare short peptides. He then determined the number of amide groups present in each peptide by measuring the $\mathbf{N H}_{4}^{+}$ released when the peptide was acid-hydrolyzed. Some of the results for the A chain are shown below. The peptides may not have been completely pure, so the numbers were approximate - but good enough for Sanger's purposes. (e) Based on these data, determine the amino acid sequence of the A chain. Explain how you reached your answer. Compare it with Figure $3-24$. (TABLE CAN'T COPY)(EQUATION CAN'T COPY)
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