Sunday, February 23, 2020

Programming with Alice Assignment Example | Topics and Well Written Essays - 750 words

Programming with Alice - Assignment Example Alice does not have primitive methods to perform front left leg up and front left leg down. It is therefore required that the code for this movement be designed. Elegant design requires that methods are kept from being too large. To maintain a small size for the methods, additional methods are added to do the small tasks. The following is done A loop is implemented at the point where the mouse takes a step ahead of the mouse. This loop ensures that whenever the mouse takes a step the cat takes another step of the same magnitude so that the mouse is always one step ahead of the cat. The next step is transforming the storyboard into program code. The first action of the storyboard is the mouse turns to see the cat. The first method is therefore turn to face. We use the turn to face to make the mouse turn to look in the direction of the cat. The next step is the cat taking one step away from the cat. We use the move away method. Alice contains control statements that are vital in controlling movements. In the cat chase program the cat moves away from the cat while the cat moves towards the mouse. The control statement Do in order is used to tell Alice to first make the cat look at the mouse and the mouse move away from the cat. Other actions must be done together. When the front right leg is up for example, the front left leg must be held down. To achieve this functionality Alice is told to Do this actions together through the DO together control statement. To implement this program into Alice a scene must first be created. The initial scene is a room (Farooq, 2012). The intention of the cat is to catch the mouse. It should follow it while the mouse should always be one step ahead of the cat. We select the room scene and then a cat and a mouse. The next stage is in the program code editor. The code that makes the program is written. In Alice the program code editor is at the bottom right of the main window. The instructions are edited in the area

Thursday, February 6, 2020

Molecular Fluorescence Analysis of Proteins Lab Report

Molecular Fluorescence Analysis of Proteins - Lab Report Example As the electron returns from the lowest triplet state to the singlet ground state, a photon is released. The high sensitivity and specificity of fluorescence techniques facilitates the study of individual protein molecules. Therefore, this experiment sought to determine the source of fluorescence in serum albumin by first establishing the fluorescence of two key amino acids that make up serum albumin. Such a study would enable a detailed study of serum albumin as a protein. The experiment also aimed at establishing the concentration of riboflavin using the absorption of known concentrations of riboflavin. Solutions of 10 Â µM tyrosine and tryptophan were made to volumes of 100Â µL each by first preparing 100 mL of 1mM solutions and diluting them to 10 Â µM. The applications software of the fluorescent instrument was loaded after which the condition parameters were set. An emission scan range of between 290 and 380 nm was set alongside slits of 5nm. The emission wavelength was set to 280 nm, and the emission tab was clicked to obtain the emission spectrum of the buffer solution. The spectrum was saved after which the same procedure was repeated for tryptophan. Thereafter, an excitation spectrum for tryptophan was prepared by choosing the optimal emission wavelength according to the results of the emission spectrum. A tyrosine spectrum was obtained using similar conditions as those of the buffer. The tyrosine band was then obtained by subtracting the buffer spectrum from the tyrosine spectrum. All these steps were repeated for serum albumin making sure to save all the spectra. 1.0 mL of 10 ppm riboflavin solution was measured into a 100 mL volumetric flask and diluted using the buffer to make a 100 ppb stock solution. Standard solutions were then prepared using clean volumetric pipettes rinsed with HPLC water. The final concentrations of the standard solutions were