Function Of Ovalbumin Casein And Collagen Proteins Biology

Proteins are really of import complex molecules that play important biological maps in the cells that are most of import to life ( growing, fix, regeneration, etc ) . Proteins are polymers made up of amino acids ( constructing blocks ) which differ to other molecules due to their N content, and are linked by peptide bonds. The construction of protein is dependent on the amino acid sequence ( primary construction ) which determines the molecular conformation ( secondary and third constructions ) . Amino acids are really soluble, due to presence of O and N in them is really negatively charged ( aminic acids are readily carried around in aqueous province ) .Proteins can besides happen as quaternate constructions.Primary construction gives the additive sequence of aminic acids in a polypeptide concatenation while the secondary construction reveals the agreement of the concatenation in infinite ( polypeptide concatenation coiled into a coiling or spiral to hold a three dimensional construction, alpha spiral ) . Tertiary ( disulphide bond ) ( coiling polypeptide molecule is folded on itself as spherical or rod like ) and quaternate structured proteins can be dived into two groups on footing of conformation ; hempen or albuminoids, and globular or folded proteins.

In this essay I will get down by speaking about the construction of proteins and will travel on to discourse about their maps. Three chief protein illustrations will be used ; casein, egg white and collagen protein.

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Structure of proteins

The primary construction of a protein defines a cardinal location called the active site, the part that is associated with the primary activity of a protein, even though it is frequently made up of merely a little figure of residues. Therefore, the amino acid alone additive sequence in polypeptide concatenation defines the protein primary construction. Primary construction is composed of assorted aminic acids held together by peptide bonds.

Secondary construction makes 60 % of the protein construction consists of alpha spiral or beta strand ( sheets ) conformation. It is most common coiling construction of protein signifier right handed spiral ( right handed agreement ) . Each bend of a alpha spiral has 3.6 amino acids. This coiled construction is locally stabilized by H bonding which occurs between C=O group of one amino acid and N-H group of 4th amino acid in the concatenation, disulphide bond, attractive force between positive and negative charges, and hydrophobic and hydrophilic group, which are responsible for the stableness to the construction. All aminic acids in a polypeptide concatenation have L- constellation which can ensue in a stable spiral if is right handed construction. Unlike ovalbumin proteins, casein proteins do non interact intramolecularly to from a third construction. Local interactions may happen within the molecule in beta sheet but no interactions occur between the distant portion of the same molecule. The molecule has a hydrophobic nucleus. In ?-Pleated, the conformation is linear a peptide concatenation and is stabilized by H bonding to adjacent parallel ironss of the same sort. Steric interactions cause a little bending of the peptide ironss, ensuing in a wrinkly deformation ( the pleated sheet ) . Most proteins and big peptides such as egg whites have alpha-helix or beta-sheet sections, their third constructions may dwell of less extremely organized bends, strands and spirals. Turns reverse the way of the peptide concatenation, and are considered to be a 3rd common secondary construction form. Beta sheets in egg white are twisted by approximately 5 to 25 & A ; deg ; per residue ; therefore, the planes of the sheets are non parallel. B-pleated sheets that are formed by separate or individual polypeptide ironss and two neighbouring ironss are held by intermolecular

H bonds, arranged in analogue ( same way ) or anti analogue. The secondary construction of the protein is the consequence of interactions of side ironss that are located within a few residues of each other. Proteins are sufficiently long that they can finally turn up back on themselves, leting residues that are farther apart in the primary construction to interact with each other. These interactions give rise to the third construction of the protein.

Fig.1.1 Secondary construction ( alpha spiral )

In third construction the protein crease is 3D.Moecules are really compact in this construction.Various amino acids interact ( hydrophobic interaction or disulphide bonds ) to organize a bunch in the Centre of the protein which wholly creases and bends the protein to gives its needed third construction illustrations include collagen and ovalbumin protein.Ovalbumin is a ball-shaped food and storage glycoprotein which plays a critical function in storage of aminic acids around the organic structure. Ovalbumin, for illustration, is the protein nowadays in egg white ( 368 amino acids ) , which is present 70 % in egg white. The sequence includes six cysteines with a individual disulfide bond between Cys74 and Cys121. The aminic end point of the protein is acetylated. Ovalbumin does non hold a classical N-terminal leader sequence, although it is a secretory protein. Alternatively, the hydrophobic sequence may move as an internal signal sequence involved in transmembrane location. This protein is impersonal and soluble in H2O. ( Huntington et al, 2001 ) . Ovalbumin is rich in glutamate and aspartate amino acids. It has a third construction and has a hydrophobic nucleus in Centre of the spherical form ( soluble in aqueous ) . The construction is little in length and breadth and hence,

posses ovoid or spherical form. Ovalbumin proteins are more complex in conformation than collagen proteins.

Collagen protein is a long fiber like construction ( parallel polypeptide ) that contain three peptide ironss which form ternary coiling construction by intramolecular H bonds which gives structures its stableness. OH residues supply excess strength due to H-bonding, and the glyciene residues which are present in high sum ( 33 % ) allow the protein to gyrate more tightly, since they fit on the interior of the spiral. In a collagen fiber, three of these spirals are coiled together to organize a rope-like construction called a ace coiling spiral. It is this construction that gives collagen its great strength. The secondary construction ( alpha coiling conformation ) farther creases into a third construction. The hydrophobic ironss are held interiorly while the hydrophilic chains occur outside, which folds and coils the construction giving stableness to the molecule. This third construction is maintained by H bonds, disulphide bonds, ionic bonds, and hydrophobic interactions. This construction brings distant amino acids side ironss closer. Covalent linkages are formed between lysine resides which strengthen the protein construction leting it to stretch and flinch to original length when needed. ( Woster, n.d ) .

Function of proteins.

Casein, is the milk phosphoprotein incorporating phosphorous acerb esters of serine and threonine, these proteins are of import for dentitions and castanetss. Casein proteins are present in milk 70-80 % and consist of a high figure of proline peptides and have no disulfide bonds. Therefore, there it has reasonably small secondary or third construction. Casein is ill soluble in H2O but readily dissolves in alkaline or strong acids, exhibiting hydrophobic belongingss, and appears in milk as a suspension of atoms. Casein is besides used in the industry of adhesives, binders, protective coatings, plastics ( such as knife grips and knitting acerate leafs ) , cloths and nutrient additives and is non-toxic and extremely stable. These proteins are rich in lysine which is one of the indispensable amino acids in milk. Casein proteins differ in different mammals milk such as animate beings and worlds, and

are of three types ; ? , ? and ? These differ one another in their molecular weights, rate of migration in an electric field and P content ( Horne, 2002 ; Wang et Al, 2009 ) .

Collagen is the most abundant protein in mammals, present in connective tissues ( tegument, bone, sinews, gristle, the cornea, etc ) which provides rigidness, protection, flexibleness and lubrication. This protein is rather indissoluble in H2O and affected by temperature alteration. Rich in glycine and alanine but besides have serine and tyrosine. Contains three long polypeptide ironss, each composed of about 1000s of aminic acids. Thhese concatenation coil into a regular three-base hit spiral, responsible for the snap of the tegument and sinews.Under high warming these turn into gelation, gelation is soluble in H2O and gives a syrupy solution, which can be used as a gum and as a thickening is nutrient industry. If collagen is partly hydrolysed under mild status ( acerb, warming, etc ) , the three collagen strands separate into globular, random spirals, bring forthing gelatine which has lower antigenicity but still maintains some of its sequence to advance cell adhesion and proliferation ( Wang et al, 2009 ) .

Many procedures can take to denaturation of protein which means it affects the secondary, third or quaternate construction. Solubility is can ensue from the assorted degrees of construction. For illustration, connective proteins are non soluble in H2O. While ovalbumin proteins are soluble in H2O and more sensitive to temperature or heating ( unlike collagen, these lack glycine sequence ) which means it can readily lose its secondary and third construction, a procedure called denaturation ( Huntington et al,2001 ) . When denaturized molecules aggregate to organize protein web, the procedure is called curdling or gel. This protein web formed traps H2O in nutrient between its meshes to organize gel or curdling giving nutrient its consistent ( egg meat ) it is used for H2O absorbing ( inspissating ) and to brace emulsion and foams.When an egg is cooked, the viscousness is reduced and the coloring material of egg alterations, this colour alteration indicates the alteration in construction that takes topographic point in the albumin proteins during warming. The interactions of both polar and nonionic units, frequently causes the protein to turn up into spherical conformations. Although ovalbumin proteins are sensitive to denaturation ( structural flowering ) , some can be unusually stable. Heating proteins can cleavage hydrogen bonds, Attic or hydrophobic bonds.Protein Structures are sensitive to temperature and PH specially the collection of proteins unfold alpha spiral content is denatured or destroyed when heated under high temperature. Some proteins are tough and non soluble in H2O, either bonded covalently or positioned by other forces which are

non easy destroyed, illustrations of conjugated proteins include collagen ( Gossett et al,1984, Huntington et Al, 2001 ) .


The nutrient proteins such as collagen, casein and ovalbumin provide high or low nutritionary quality for worlds. The quality of nutrient depends on the construction and functional belongingss of protein. Some of functional belongingss of proteins are solubility, hydration, viscousness, texturing, formation of dough, emulsifying and frothing belongingss. Solubility is the ability of proteins to fade out in H2O lessenings during heat intervention, this loss of solubility has major effects for emulsifying and frothing belongingss of protein.

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Function Of Ovalbumin Casein And Collagen Proteins Biology. (2017, Jul 06). Retrieved from