Ovalbumin Research Paper

Different types of bonds/interactions in proteins lead to different kinds of structures. Three of the most commonly known chemical bonds in proteins include the hydrogen bond, the covalent bond, and the ionic bond. In hydrogen bonds, hydrogen interacts with oxygen, nitrogen, or fluorine to form either the alpha helix, or the beta sheet, which in turn determines its secondary, tertiary, or quaternary structure. Another type of bonds, the covalent bond, links amino acids together by sharing electrons;

This Lab Report is an analysis of the results of a two-part experiment. In the first part, we used a gel filtration column to separate the components of a mixture composed of protein and non-protein molecules. By doing so we hoped to obtain fractions that contained single components of the mixture, while also gaining insight into the relative molecular weight of each component compared to each other. We would then plot these fractions onto nitrocellulose paper in order to determine which fractions had protein. In the second part, we would use the fractions which we had determined had protein to conduct an SDS-PAGE. By doing so we hoped to determine an estimate on the molecular weight of the proteins present in each fraction by comparing it to a tracker dye composed of a variety of molecules of differing molecular weight.

Box on right illustrates the peptide bond resulting from the condensation of both the amino acids. The box on the left illustrates the separation of the hydroxide group from glycine and the hydrogen atom from valine.

This difference in values can be explained by the denaturing agents used in the experiment. The absorbance value used in the calculations came from reaction mixture B which contained no denaturing agent therefore not all the thiol groups where available to react with DTNB; DNTB alkylates thiolgroups. Denaturing agents can be added to the reaction mixture to free more thiol groups and therefore reveal the remaining residues; but not the two involved in the S-S bond.

The determination of the number of thiol groups by DTNB is carried out at pH> 7.5 because the extinction coefficient is strongly pH dependent at pH values more acidic than 7.5. With an altered pH the maximal extinction may be altered, meaning that the absorbency figures will be

Data from previous studies suggest that the inactive sHSP takes on the oligomer conformation Upon stress, these oligomers assemble into active dimeric species, exposing previously inaccessible hydrophobic surfaces that can then interact with nonpolar patches on the misfolded substrate, capturing them in large complexes. The sHSP-substrate complexes maintain the substrate in a folding-competent state for extended periods of time. Biologically this is of utmost importance since it is

Threonine is an essential amino acid that is classified as slightly polar due to its hydroxyl group and the ability to easily donate a hydrogen atom. This as well makes it hydrophilic and often will saturate the outer region of a water soluble protein. They hydroxyl side chain can undergo glycosylation by adding saccharides and phosphorylation by adding phosphate through the actions of threonine kinase (New World Encyclopedia, 2015).

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Thiols are more reactive than hydroxyl groups and react easily with mercurails and heavy metal salts. The reaction with p-chloro-mercuribenzoate (PCMB) can be used to measure thiol groups, as there are changes in the

Boucherville is a city in the Montérégie region in Quebec, Canada. It is a suburb of Montreal on the South shore of the Saint Lawrence River.

During week one, dissolve ScCl2 H2O (50.920g, 0.0065mol, 1 equiv.) in concentrated hydrochloric acid (55mL) all in an Erlenmeyer flask, might need to heat for complete dissolution. In another Erlenmeyer flask dissolve 2,6-dimethylnitrobenzene (6.744g, 0.0045mol, 1.4 equiv.) in glacial acetic acid (70mL). Then add ScCl2 H2O to 2,6-dimethylnitrobenzene at one time, swirl shortly and let solution sit for 15 minutes. After time is up, cool reaction to room temperature with a water bath, then vacuum filtrate. Then transfer damp solid into an Erlenmeyer flask and add deionized water (40mL). Then turn mixture basic by adding KOH (8M, 40mL). After mixture is basic, cool mixture to room temperature in ice bath and transfer it to the separatory funnel and extract it with diethyl ether (2 x 15mL). Drain all of the organic layers into the same flask. Next wash the organic layer with deionized water (2 x 10mL) and then dry it with anhydrous magnesium sulfate. Gravity filtrate the solution and then rotary evaporate it. Transfer the evaporated solution into a culture tube and store with a loose cap. The following week weigh the product, which is 2,6-dimethylaniline, perform an IR, and 1H NMR. Yield: 2.832g (0.023mol, 47.1%). IR (neat): 1624 cm-1 (C=C), 3468 and 3386 cm-1 (N-H), 2967 cm-1 (C-H). 1H NMR (300 MHz, CDCl3): δ 2.68 (methyl groups off ring), 3.65 (NH2), 6.74, 7.03 (H’s on ring)

Introduction: The goal of this experiment was to practice using the FirstGlance in Jmol molecular visualization to examine key structural features of proteins. This work is important because protein structure can be related to function, multiple-sequence alignments and evolutionary preservation, and designing drug. FirstGlance in Jmol makes it fairly easy to perceive structure-function relationships in the protein you chose. Using FirstGlance, it is easy to visualize and distinguish chains, and disulfide bonds are obvious. Alpha helices and beta strands are evident due to the "cartoon" secondary structural schematic.

Specifically, the egg whites, which contain six grams of serine for every 100 grams of egg whites (Haney, 2012). Not only do egg whites contain serine, they contain considerable amounts of other amino acids as well. One egg white contains only about seventeen kilocalories, three and a half grams of protein, and virtually no fat, cholesterol, or carbs (Haney, 2012). In other words, egg whites are considered a “super food”.

The cysteine (CYS-14, in view 2) is connected to the heme by two covalent bonds. A covalent bond is characterized by sharing of an electron between atoms. In this case, two thioesther bonds are formed between the sulphur in the cysteine residue and the vinyl group (H2C=CH2) of the heme. This covalent linkage between the heme and the cysteine is very important because it does not dissociate easily, and is the bond that ‘holds’ the heme to the protein complex (1).

The physicochemical and organoleptic qualities of proteins may be refined by controlled enzymatic hydrolysis, which generates free amino acids and abundant short peptides with less salt and carcinogenic compounds (Weir, 1992). Significantly milder conditions are employed: The pH is typically maintained at pH 5–7 corresponding to optimum enzyme activity and the hydrolytic process occurs at 50–60°C for 10–24 h, which minimizes unwanted side reactions (Clemente, 2000). Proteins are only partially hydrolysed due to the inability of most proteases to cleave glycoproteins, phosphoproteins and protein domains containing numerous covalent-linked disulfide bridges (Gibbs et al., 2004).