Preparation Of L-Phenylalanine Lab Report

Experiment VIII was performed to analyze SN2 and SN1 using tertiary and primary substrates and use gas chromatography (GC) to examine the SN1 reaction. The product of the SN2 reaction was classified as n-butyl iodide by using infrared spectroscopy and gas chromatography mass spectroscopy and the product of the SN1 reaction was identified as of t-butyl chloride by using infrared spectroscopy and gas chromatography. For the SN2 reaction, 7.62 grams of n-butyl bromide, 20.0 grams of sodium iodide, and 79.1 grams of acetone were used to produce 3.12 grams of n-butyl iodide. The limited reagent was identified as n-butyl bromide and the theoretical yield of n-butyl iodide was calculated as 10.3 grams. The percent yield of this reaction was calculated

Whereas phenylalanine is more of an essential amino

When the electricity is turned on, the proteins and Tris-glycine enter the stacking gel. In stacking gel with pH 6.8, the N-terminal amino group of the proteins and amino acids are protonated at equilibrium, which makes them less negative. The average electrophoretic mobility is very slow. A Gly-chloride ion boundary is formed since glycine moves slower than chloride ion. However, glycine still runs slightly faster than other proteins.

Experiment # 3 – Resolution Of ( )- -Phenylethylamine Name: Krishna Binu Class: Chem 2020 Due Date: October 23, 2015 Table 1 Shows the experimental results. Name Result Mass of Amine (g) 3.32 Mass of Salt (g) 1.26 Observed Rotation of Isolated Amine (Degrees) -36.33 1) Draw the chemical structures of the two diastereomeric salts produced in Part A using a proper perspective (line-angle) representation.

Explain the relationship between the ionisation of amino acids and pH |Structural diagram of the neutral structure| |Structural diagram of positively charged structure| |Structural diagram of negatively charged structure| Explain how the form of an amino acid, whether positively charged, negatively charged or neutral, depends of the pH of the solution ? If you increase the pH of a solution of an amino acid by adding hydroxide ions, if this is done then the hydrogen ions will then be removed from the -NH3+group . . To test if it is now a negative ion a process called electrophoresis.although it is colourless its position can be detected using ninhydrin. If the amino acid has dried and then heated gently it would appear as

The purpose of this experiment was to learn about the electrophilic aromatic substitution reactions that take place on benzene, and how the presence of substituents in the ring affect the orientation of the incoming electrophile. Using acetanilide, as the starting material, glacial acetic acid, sulfuric acid, and nitric acid were mixed and stirred to produce p-nitroacetanilide. In a 125 mL Erlenmeyer flask, 3.305 g of acetanilide were allowed to mix with 5.0 mL of glacial acetic acid. This mixture was warmed in a hot plate with constantly stirring at a lukewarm temperature so as to avoid excess heating. If this happens, the mixture boils and it would be necessary to start the experiment all over again.

Benzyne Formation and the Diels-Alder Reaction Preparation of 1,2,3,4 Tetraphenylnaphthalene Aubree Edwards Purpose: 1,2,3,4-tetraphenylnaphthalene is prepared by first producing benzyne via the unstable diazonium salt. Then tetraphenylcyclopentadienone and benzyne undergo a diels-alder reaction to create 1,2,3,4-tetraphenylnaphthalene. Reactions: Procedure: The reaction mixture was created. Tetraphenylcyclopentadienone (0.1197g, 0.3113 mmol) a black solid powder, anthranilic acid ( 0.0482g, 0.3516 mmol) a yellowish sand, and 1,2-dimethoxyethane (1.2 ml) was added to a 5-ml conical vial.

By completing this experiment, knowledge collected about optimal pH in enzymes will help

purpose the propose of this experiment was too see if the chemical reaction of a enzyme can be made faster. Hypothesis I think that a warm environment would be best to make an enzyme’s reaction faster. because a protein can move faster in heat.

The first test that gave us an indication that catharant hus ovalis (species Z), is most closely related to Catharanthus roseus (Rosy periwinkle) is test 5 (Test for enzyme M). We found that both species Z and rosy periwinkle have enzyme m present which suggests that share similar enzymes, which helps prove that species Z can produce the same alkaloids. Enzymes are used to increase reaction and help with digestion/ synthesis. Enzyme m, which is present in periwinkle, is used to synthesize the alkaloids of interest. We tested the 3 other species to see if this enzyme was present to help bring us to our conclusion of which is most similar to rosy periwinkle.

LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.

Experiment 2 Report Scaffold (Substitution Reactions, Purification, and Identification) Purpose/Introduction 1. A Sn2 reaction was conducted; this involved benzyl bromide, sodium hydroxide, an unknown compound and ethanol through reflux technique, mel-temp recordings, recrystallization, and analysis of TLC plates. 2. There was one unknown compound in the reaction that was later discovered after a series of techniques described above.

Arianna Diazwightman - Biology Lab Report PID - 5869132 Gabby Vazquez, Catalina Ortega, and Jerry Lab Section 41 Table 5 Lemme Break It Down Ft. Amylase The effects of temperature on the ability of an enzyme to break down starch. Abstract

Hardee and his group developed a process of activation of aliphatic carboxylic acids taking 3, 3-dichlorocyclopropenes in presence of tertiary amine base , DIPEA (diisopropylethylamine)[22] FIGURE 3.3 ACTIVATION OF ALIPHATIC ACID Racemization is frequent in the course of coupling reaction at the C-terminal amino acid residue due to the ionization of the α-hydrogen atom and formation of an oxazolone intermediate in peptide synthesis, so of course this will not reagent of choice in peptide synthesis, where suitable peptide coupling reagent can be selected, which is out of scope of this review.[22] 3.2 SELECTED PROCESS Out of all the processes mentioned in the survey, these processes were selected on the behalf of having most appropriate reaction conditions and environment of the research lab, i.e modification with

Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution