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Casein, Ovalbumin and Collagen: Composition and Function

Introduction

Proteins are very important complex substances that play significant natural functions in the cells that are most significant alive (progress, repair, regeneration, etc). Protein are polymers composed of proteins (blocks) which fluctuate to other substances due to their nitrogen content, and are connected by peptide bonds. The structure of protein is dependent on the amino acid solution sequence (main structure) which establishes the molecular conformation (extra and tertiary structures). Amino acids are extremely soluble, anticipated to occurrence of oxygen and nitrogen in them is very electronegative (proteins are readily transported around in aqueous state). Proteins can also happen as quaternary buildings. Primary structure provides linear series of proteins in a polypeptide chain while the secondary structure discloses the agreement of the string in space (polypeptide chain coiled into a spiral or helix to truly have a three dimensional framework, alpha helix). Tertiary (disulphide connection) (helical polypeptide molecule is folded on itself as spherical or fishing rod like) and quaternary structured protein can be dived into two communities on basis of conformation; fibrous or scleroproteins, and globular or folded protein.

In this article I will start by discussing the framework of proteins and can go on to go over about their functions. Three main health proteins examples will be used; casein, ovalbumin and collagen proteins.

Structure of proteins

The primary framework of a proteins defines an integral location called the dynamic site, the region that is associated with the most important activity of a proteins, even though it is often made up of only a small range of residues. Therefore, the amino acid unique linear collection in polypeptide string defines the health proteins primary structure. Main structure is composed of various amino acids held together by peptide bonds.

Secondary framework makes 60% of the necessary protein structure involves alpha helix or beta strand (linens) conformation. It is most typical spiral framework of health proteins form right handed helix (right handed agreement). Each flip of a alpha helix has 3. 6 amino acids. This coiled structure is locally stabilized by hydrogen bonding which occurs between C=O band of one amino acidity and N-H band of fourth amino acidity in the chain, disulphide bond, fascination between negative and positive charges, and hydrophobic and hydrophilic radical, that are responsible for the stableness to the composition. All amino acids in a polypeptide string have L- settings which can result in a well balanced helix if is right handed structure. Unlike ovalbumin protein, casein proteins do not have interaction intramolecularly to from a tertiary structure. Local interactions may occur within the molecule in beta sheet but no connections occur between the distant part of the same molecule. The molecule has a hydrophobic key. In О-Pleated, the conformation is linear a peptide string and is also stabilized by hydrogen bonding to adjacent parallel chains of the same kind. Steric interactions cause a small twisting of the peptide chains, resulting in a wrinkled distortion (the pleated sheet). Most proteins and large peptides such as ovalbumin have alpha-helix or beta-sheet sections, their tertiary constructions may contain less highly arranged changes, strands and coils. Converts reverse the path of the peptide chain, and are believed to be a third common extra structure style. Beta sheets in ovalbumin are twisted by about 5 to 25 per residue; thus, the planes of the mattress sheets aren't parallel. B-pleated bed linens that are shaped by separate or solo polypeptide chains and two neighbouring chains are kept by intermolecular

hydrogen bonds, established in parallel (same course) or anti parallel. The supplementary framework of the protein is the consequence of interactions of aspect chains that are located within the few residues of each other. Protein are sufficiently long that they can eventually fold again on themselves, allowing residues that are farther apart in the principal structure to connect to each other. These interactions bring about the tertiary structure of the proteins.

In tertiary composition the protein flip is 3D. Moecules are extremely small in this structure. Various proteins interact (hydrophobic connections or disulphide bonds) to form a cluster at the heart of the proteins which completely folds and bends the proteins to offers its required tertiary framework for example collagen and ovalbumin protein. Ovalbumin is a globular nutrient and storage area glycoprotein which plays a vital role in safe-keeping of amino acids around the body. Ovalbumin, for example, is the proteins within egg white ( 368 amino acids ), which exists 70% in egg white. The collection includes six cysteines with an individual disulfide relationship between Cys74 and Cys121. The amino terminus of the proteins is acetylated. Ovalbumin doesn't have a classical N-terminal leader collection, although it is a secretory health proteins. Instead, the hydrophobic collection may become an internal transmission sequence involved with transmembrane location. This proteins is neutral and soluble in drinking water. (Huntington et al, 2001). Ovalbumin is rich in glutamate and aspartate proteins. It has a tertiary composition and has a hydrophobic central in centre of the spherical shape (soluble in aqueous). The framework is small in length and width and therefore, posses ovoid or spherical form. Ovalbumin protein are more technical in conformation than collagen protein.

Collagen proteins is an extended fibre like structure (parallel polypeptide) which contain three peptide chains which form triple helical framework by intramolecular hydrogen bonds which gives structures its stableness. OH residues provide extra strength scheduled to H-bonding, and the glyciene residues which can be found in high amount( 33%) permit the proteins to coil more tightly, since they fit within the helix. Within a collagen fibre, three of the helices are coiled together to form a rope-like structure called a brilliant helical coil. It really is this structure that provides collagen its great power. The secondary framework (alpha helical conformation) further folds into a tertiary structure. The hydrophobic chains are placed interiorly while the hydrophilic chains occur outside, which folds and coils the framework giving stableness to the molecule. This tertiary framework is taken care of by hydrogen bonds, disulphide bonds, ionic bonds, and hydrophobic interactions. This composition brings distant proteins side chains better. Covalent linkages are shaped between lysine resides which strengthen the protein structure and can expand and recoil to original span when needed. (Woster, n. d).

Function of proteins

Casein, is the dairy phosphoprotein made up of phosphoric acid esters of serine and threonine, these protein are important for teeth and bone fragments. Casein proteins are present in milk 70-80% and consist of a high number of proline peptides and also have no disulfide bonds. Therefore, there it has moderately little secondary or tertiary structure. Casein is improperly soluble in water but conveniently dissolves in alkaline or strong acids, exhibiting hydrophobic properties, and looks in dairy as a suspension of particles. Casein is also used in the make of adhesives, binders, protective coatings, plastics (such as blade deals with and knitting fine needles), fabric and food chemicals and is non-toxic and highly steady. These protein are rich in lysine which is one of the essential proteins in milk. Casein proteins vary in various mammals milk such as pets and humans, and are of three types; О±, О and О These differ one another in their molecular weights, rate of migration in an electric field and phosphorus content (Horne, 2002; Wang et al, 2009).

Collagen is the most numerous necessary protein in mammals, within connective tissue (skin, bone, tendons, cartilage, the cornea, etc) which provides rigidity, protection, flexibility and lubrication. This protein is quite insoluble in water and damaged by heat change. Abundant with glycine and alanine but also have serine and tyrosine. Contains three long polypeptide chains, each composed of about a large number of amino acids. Thhese chain curl into a normal triple helix, in charge of the elasticity of your skin and tendons. Under high heating up these turn into gelation, gelation is soluble in water and provides a viscous solution, which may be used as a glue so that as a thickener is food industry. If collagen is partially hydrolysed under mild condition ( acid, heating up, etc), the three collagen strands separate into globular, arbitrary coils, producing gelatine which includes lower antigenicity but nonetheless maintains some of its sequence to promote cell adhesion and proliferation (Wang et al, 2009).

Many processes can lead to denaturation of protein this means it influences the supplementary, tertiary or quaternary structure. Solubility is can result from the various levels of structure. For example, connective proteins are not soluble in water. While ovalbumin proteins are soluble in drinking water and more hypersensitive to heat or heating system (unlike collagen, these shortage glycine collection) this means it can conveniently lose its supplementary and tertiary structure, an activity called denaturation (Huntington et al, 2001). When denatured molecules aggregate to form protein network, the procedure is named coagulation or gel. This health proteins network formed traps water in food between its meshes to create gel or coagulation providing food its steady ( egg meats) it can be used for drinking water absorbing (thickening) also to stabilise emulsion and foams. When an egg is prepared, the viscosity is reduced and the color of egg changes, this color change implies the change in composition that occurs in the albumin proteins during heating up. The connections of both polar and nonpolar products, often causes the protein to flip into spherical conformations. Although ovalbumin proteins are sensitive to denaturation (structural unfolding), some can be remarkably stable. Heating proteins can cleavage hydrogen bonds, ionic or hydrophobic bonds. Health proteins Structures are very sensitive to temps and PH specially the aggregation of proteins unfold alpha helix content is denatured or ruined when warmed under high temperature. Some proteins are tough and not soluble in normal water, either bonded covalently or positioned by other pushes which are not easily destroyed, types of conjugated protein include collagen (Gossett et al, 1984, Huntington et al, 2001).

Conclusion

The food proteins such as collagen, casein and ovalbumin provide high or low nutritional quality for humans. The grade of food will depend on the composition and practical properties of health proteins. Some of practical properties of protein are solubility, hydration, viscosity, texturing, development of dough, emulsifying and foaming properties. Solubility is the ability of proteins to dissolve in drinking water decreases during heat therapy, this loss of solubility has major results for emulsifying and foaming properties of necessary protein.

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