The Effect Of The On Crystallization Of Lysozyme Protein Crystals

The shape and magnitude of the UV spectra depends on the composition of amino acid in each protein. Due to the aromatic amino acid residues in the protein, the observed UV absorbance was mainly in the 240 nm to 340 nm region. In Figure 1 to 3, the maximal absorbance of each protein was approximately at 280 nm. The difference in magnitudes of the peak observed was linked to the differences in the amino acid contents in each of the proteins. The peak of lysozyme was greater than those of BSA and gelatin, because lysozyme has a greater number of tryptophan residues. Lysozyme has six tryptophan residues, whereas BSA and gelatin has two and zero, respectively (Department of Chemistry, 2014). Lysozyme has three times more tryptophan residues

Controlled crystal formation is important to acquire a certain texture in crystalline candy. Crystalline candies are smooth, creamy, and easily chewed with a definite structure of small crystals that resemble tiny snowflakes. Examples of crystalline candies are fondant, fudge, and penuche. When a concentration of sugar is higher than 121 degrees Celsius, it is an amorphous or non-crystalline candy, these are candies formed from a sugar solution that does not crystallize such as peanut brittle, and caramel. The purpose of this lab is to understand how temperature influences the texture, and firmness of

Proteins are the metabolic workhorses of the cell; they engage in a variety of essential activities ranging from enzymatically catabolizing macromolecular food sources to serving as structural components that maintain cell stability. Maximizing protein function relies on intricate non-covalent interactions occurring on the secondary, tertiary, and quaternary levels that help determine the overall shape of the protein. In their native states, proteins will assume the most energetically favorable configuration. Occasionally however, cells are exposed to exogenous disruptions such as heat stress. Heat Stress can compromise protein three-dimensional structure. Hydrophobic residues tend to be buried in the interior of the protein but when

The solution was subsequently arranged into a reflux apparatus which included a wet paper towel in order to prevent vapor loss. The solution was refluxed at a temperature ranging from 180°C-185°C for thirty minutes via sand bath. The contents of the micro-test tube were then cooled to room temperature followed by an ice bath in order for crystals to form. The crystals were then collected via suction filtration using a Hirsch funnel. The product was washed with ice-cold xylene (3

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

By following the above procedure, it was determined that my hypothesis was accepted. Initially, I predicted that sugar will have the best solution for making crystals because the sugar dissolves better in water and will be able to make the best crystals in size and shape. During the experiment, I investigated which solution made the best crystals. However, there was some inconsistencies and consistencies. The inconsistencies and consistencies were finding the perfect spot to put the solutions,the crystals forming, and the right materials. The first inconsistency was finding the perfect spot to put my solutions. It was very difficult for me

Minerals are naturally occurring, inorganic, solid, crystalline substances which have a fixed structure and chemical composition. Minerals are an important part of Geology, especially when studying Crystal and mineral growth. Understanding how crystals grow and the difference between slow and fast cooling rates is also important in Geology. Knowing the difference between cooling rates is important because cooling rate changes the texture of rocks and minerals. The purpose for the Crystal Growth experiment is to identify which Solubility and temperature produces larger crystals, and to simulate natural crystal growth. We will achieve the results we desire by conducting the experiment thoroughly and correctly, as well as correctly

For the second part of the experiment, one had to use the knowledge learn from viewing protein molecules in FirstGlance in Jmol to analyze the protein PDB ID: 4EEY. The analysis of this protein was done using the RSCB protein data bank (PDB) at (http://www.rcsb.org/pdb/home/home.do).2

In this experiment, two sets of variables were manipulated to see the effect it would have on the crystallization of the lysozymes via the hanging drop method. In order to help visualize which will bring optimal crystallization of the protein, two sets of variables were tested in this experiment: salt concentration and the concentration of polyethylene glycol (PEG). Our experiment dealt with increasing the concentration of both these sets of variables to see how it would affect the quantity of protein crystals produced. As concentration of NaCl increased, so did the yield of crystals and the same could be said with PEG. As PEG concentration neared a concentration of 20% we saw an increase of crystals.

The diffraction patterns of PXRD analysis for co-crystals of the three ratios are completely different from those of the pure drugs (acetaminophen and thiourea). According to Savjani et al. (2013), the different patterns in diffractogram of PXRD analysis suggest a complete formation of

The catalyst site is where the enzymes reduces the activation energy level. The protein structure, the rest of the space, is used to support and position the active site. The protein’s structure is essential to understand how it can become

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

For a mechanistic understanding of macromolecular and biochemical functions and processes of a wide variety of biological structures (i.e. cells, proteins, bacteria and viruses) (Milne et al., 2013) optical devices (i.e. X-ray crystallography and NMR, among others) have long been implicated in characterizing biomolecular structures into 3D

INTRODUCTION: The pharmaceutical industry has long been trying to improve the effectiveness of certain drugs it would like to introduce and mass-produce. The concept behind many of these drugs is sound; however, they appear to fall short when it comes to some of their chemical properties. These properties, including solubility, stability, intrinsic dissolution and bioavailability, affect the extent to which the body can utilize the drug effectively, and it is thus vital that drugs are developed to have a maximum effect on an individual after administration. This is where pharmaceutical co-crystals are the potential key to advancing drastically the design of drugs by enhancing their bioavailability and solubility. There has been a growing interest in the design of pharmaceutical co-crystals over the past decade and this is only going to escalate as the focus is shifted to designing, synthesising and characterising better and more improved crystalline structures. This report aims to examine and compare several methods in the design, synthesis and characterisation processes of pharmaceutical co-crystals in addition to providing examples of the effectiveness of these co-crystals in pharmaceutics.

As a result, the interactions between protein molecules exceed protein-water interactions, and the solubility decreases. Moreover, the differences in the amino acid sequence makes proteins differ in their salting in and salting out behavior. This is the basis for the fractional precipitation of proteins by means of salt. Most commonly used salt is ammonium sulfate because it is available in highly purified form and because of its high solubility. (Boyer, 2000)