Protein Denaturation

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Explain Denaturation of Protein?

Denaturation meaning can be given as, when the solution of a protein is boiled frequently, the protein becomes insoluble. That means it is denatured and remains insoluble even when the solution gets cooled. The denaturation of the proteins of egg white by the heat process, as when boiling an egg is given as an example of irreversible denaturation. The denatured protein contains a primary structure as the native or original protein. At high temperatures, the weak forces between charged groups and the weaker forces of nonpolar groups' mutual attraction are disturbed. However, resultantly, the tertiary structure of the protein is lost. This is the protein denaturation definition.

About Denaturation

Denaturation is brought about in multiple ways. Proteins are denatured by acid or alkaline treatment, reducing or oxidizing agents, and certain organic solvents. Attractive among the denaturing agents are the ones that affect both secondary and tertiary structures without the effect on the primary structure. Most frequently, the agents used for this purpose are guanidinium chloride and urea. These molecules break the hydrogen bonds and salt bridges between the positive and negative side chains, removing the peptide chain's tertiary structure.

When the denaturing agents are removed from a protein solution, the native protein reforms in several cases, denaturation is also accomplished by reducing the disulfide bonds of cystine. It means the disulfide bond conversion (―S―S―) to the two sulfhydryl groups (―SH). This produces two cysteines, and the reoxidation of cysteines by exposure to air can sometimes regenerate the native protein. However, in the other cases, the wrong cysteines become bound to each other by resulting in a variable protein. Ultimately, denaturation is also accomplished by exposing the proteins to organic solvents such as acetone or ethanol. Organic solvents are also thought to interfere with the nonpolar group's mutual attraction.

Conformation of Proteins in Interfaces

Similar to several other substances with both hydrophobic and hydrophilic groups, the soluble proteins tend to migrate into the interface between water and oil and water and air; here, the term oil means a hydrophobic liquid such as xylene or benzene. Proteins spread within the interface form thin films. Measurements of the interfacial tension or surface tension of such films represent that the tension can be reduced by the protein film. Proteins form a monomolecular layer when forming an interfacial film.

That is a layer one molecule in terms of height. Although once it was thought that globular protein molecules unfold completely in the interface, now, it has been established that several proteins can be recovered from native state films. The lateral pressure application of protein denaturation film causes it to increase in thickness and ultimately to form a layer with a height corresponding to the native protein molecule’s diameter.

In an interface, the protein molecules, because of Brownian motions (which are called molecular vibrations), occupy more space than perform those in the film after the application of protein denaturation pressure. This Brownian motion of compressed molecules given as limited to the two dimensions of the interface since the protein molecules cannot move either upward or downward.

Classification of Proteins

Classification by Solubility

Franz Hofmeister and Emil Fischer, after two German chemists, independently stated in 1902 that proteins are importantly polypeptides consisting of several amino acids; an attempt was made to classify the proteins based on their physical and chemical properties because the biological function of the proteins had not yet been established.

Primarily, proteins were classified based on their solubility in a solvent count. However, this particular classification is no longer satisfactory because proteins having quite a different function and structure at times have the same solubilities; conversely, proteins of similar structure and function at times have variable solubilities. However, still, the terms associated with the old classification are widely used. They are defined as follows:

Classification by Biological Functions

Because the old classification is in such a bad state, it is much more preferable to classify proteins according to their biological function. However, such a type of classification is far from the ideal situation because one protein can contain more than one function. For example, the contractile protein myosin also acts as an ATPase (otherwise adenosine triphosphatase), which is a denatured enzyme that hydrolyzes adenosine triphosphate (that removes a phosphate group from the ATP by introducing the water molecule).

The other problem with the functional classification is that the protein’s definite function frequently is unknown. A protein is not called an enzyme as long as its substrate (it means the specific compound upon which it acts) is unknown. Even it cannot be tested for its enzymatic action when its substrate is unknown.

Function and Special Structure of Proteins

Despite the limitations of proteins, a functional classification can be used to explain the relationship between a protein's function and structure whenever possible. Because their structure is simpler than that of globular proteins, and their function, the maintenance of either a flexible or rigid structure, is more clearly related to their function, structural and fibrous proteins are discussed first.

FAQ (Frequently Asked Questions)

1. Explain about Muscle Proteins?

Answer: The total amount of muscle proteins in mammals and humans exceeds that of any other protein. About 40% of the body weight of a healthy human adult weighing about 70 kg (150 pounds) is the muscle that is composed of about 20% of the muscle protein. Therefore, the human body holds about 5 to 6 kg (which means 11 to 13 pounds) of muscle protein. A fraction, which is albumin-like of these proteins, originally known as myogenic, contains multiple aldolases, enzymes-phosphorylase, glyceraldehyde phosphate dehydrogenase, and also others; it does not seem to be involved in the contraction.

2. What are Fibrinogen and Fibrin?

Answer: During the clotting process, fibrinogen, a protein found in blood plasma, can be converted to the insoluble protein fibrin. Blood serum, or blood plasma minus fibrinogen, is the fibrinogen-free fluid derived after the clot has been removed. The blood plasma’s fibrinogen content is 0.2 to 0.4%.

3. Explain about Milk Proteins?

Answer: Milk contains albumin - α-lactalbumin; globulin - a beta-lactoglobulin; and also a phosphoprotein - casein. When acid is added to milk, casein gets precipitates. The rest of the watery liquid (which is the supernatant solution), or whey, contains the α-lactalbumin and β-lactoglobulin.

4. Explain about Egg Proteins?

Answer: About 50% of the proteins of egg white comprises ovalbumin, which can be easily obtained in the crystals. It has a molecular weight of 46,000 and an amino acid composition that differs from serum albumin. At the same time, the other proteins of egg white are lysozyme, conalbumin, ovomucoid, ovoglobulin, and avidin.