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Collagen triple helix Collagen is a component of bone and connective tissue and is organized as strong water-insoluble fibres. It has elsa pun beauty slimming institute unique periodic structure comprising of three polypeptide chains wrapped around each other in a repeat sequence of X-Pro-Gly or X-Hyp-Gly where X can be any amino acid.
Every third position in the collagen triple helix is Gly because every third residue must sit inside the helix and only Gly is small enough. The individual collagen chains are also helices and the three strands are held together by hydrogen bonds involving hydroxyproline and hydroxylysine residues.
The molecular weight of the triple-stranded array is approximatelyDaltons, involving approximately amino acid residues. Intra- and intermolecular cross-linking stabilizes the collagen triple helix structure, especially covalent bonds between lysine and histidine. The amount of crosslinking increases with age.
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A major role for vitamin C L-ascorbic acid in vivo is in making collagen: proline and lysine in collagen are converted to 4hydroxyproline and 5-hydroxylysine using this vitamin. Scurvy is a disease arising from a deficiency of vitamin C, and results in skin lesions, bleeding gums and fragile blood vessels.
Proteins fold to make the most stable structure and this structure will generally minimize solvent contact with residues of opposing polarity and hence minimize overall free energy. Therefore, in aqueous solution, proteins generally exist pierdere în greutate portland dr quinn their hydrophobic residues to the inside and their hydrophilic residues to the outside of their three-dimensional conformation.
Globular proteins — helical and pleated sheet sections fold back on each other; interactions between side chains important for protein folding; polar residues face surface and interact with solvent; non-polar residues face interior and interact with each other; structure is not static; generally more sensitive to temperature and pH change than their fibrous counterparts. The tertiary structure of a protein is held together by interactions between the side chains.
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These can be through non-covalent interactions or covalent bonds. The most common non-covalent interactions are electrostatic ionic bonds, salt bridges, ion pairinghydrogen bonds, hydrophobic interactions and van der Waals dispersion forces.
Covalent bonds in protein structure are primarily disulphide bonds sulphur bridges between cysteine residues, although other types of covalent bond can form between residues. Electrostatic interactions Some amino acids contain an extra carboxyl group aspartic acid and glutamic acid or an extra amino group lysine, arginine, histidine.
These groups can be ionized and therefore an ionic bond could be formed between the negative and the positive group if the chains folded in such a way that they were close to each other. Hydrogen bonds Hydrogen bonds can form between side chains since many amino acids contain groups in their side chains which have a hydrogen atom attached to either an oxygen or a nitrogen atom.
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This is a classic situation where hydrogen bonding can occur. For example, the amino acid serine contains a hydroxyl group slim4vit ebay its side chain; therefore, hydrogen bonding could occur between two serine residues in different parts of a folded chain.
Hydrophobic interactions Non-polar molecules or groups tend to cluster together in water; these associations are called hydrophobic interactions.
The driving force for hydrophobic interactions is not the attraction of the BLBKCampbell-Platt Food chemistry non-polar molecules for one another, but is due to entropic factors relating to the strength of hydrogen bonding between water molecules.
Van der Waals dispersion forces Several amino acids have quite large hydrocarbon groups in their side chains e. Temporary fluctuating dipoles in one of these groups could induce opposite dipoles in another group on a nearby folded chain.
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The dispersion forces set up would be enough to hold the folded structure together, although van der Waals forces are weaker and less specific than electrostatic and hydrogen bonds. Disulphide bonding If two cysteine side chains are oriented next to each other because of folding in the peptide chain, they can react to form a covalent bond called a disulphide bond or a sulphur bridge.
Each chain is a subunit of the oligomer proteinwhich is commonly a dimer, trimer or tetramer.
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Haemoglobin has quaternary structure. The chains are similar to myoglobin and haemoglobin is able to bind four oxygen atoms through positive cooperativity. This disruption of the native protein structure is defined as protein denaturation, which is an important process that may occur during the processing of foods.
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It is generally observed as unfolding of the protein molecule from its uniquely ordered structure to a randomly ordered peptide chain. In the case of globular proteins, the denaturing process is often followed by aggregation, since previously buried hydrophobic residues are exposed to solution.
Loss of solubility and changes to water-binding capacity. Increased intrinsic viscosity. Increased susceptibility to proteolysis.
Denaturation can be reversible, but if disulphide bonds are broken the denaturation process is often considered irreversible. Different proteins have different susceptibilities to denaturation since their individual structures are different. There are various denaturing agents that can destabilize protein structures that are categorized as physical agents or chemical agents.
Physical agents include heat, mechanical treatment, hydrostatic pressure, irradiation, and adsorption at interfaces. Heat is the most commonly encountered physical agent and is able to destabilize many bonds within proteins, including electrostatic bonds, hydrogen bonds and van der Waals interactions. Heat denaturation is useful in food processing since it tends elsa pun beauty slimming institute lead to improvement of sensory properties and protein digestibility, and can be used to manipulate foaming and emulsifying properties.
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Heating also promotes the participation of proteins in the Maillard reaction, which leads to the loss of nutritionally available lysine residues. Chemical agents to denature proteins include acids, alkalis, metals, organic solvents and various organic solutes.
Exposure to acids or alkalis i.
Most proteins are stable within a pH range around their isoelectric point zero net charge and the effects of acids or elsa pun beauty slimming institute are normally reversible.
The presence of organic solvents weakens hydrophobic interactions since non-polar side chains become more soluble.
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Organic solutes can have a variety of effects. Urea alters the structure of water in such a way as to weaken hydrophobic interactions, leading to protein unfolding. Sodium dodecyl sulphate SDS is an anionic detergent that binds irreversibly to charged groups within a protein, inducing a large net negative charge that increases electrostatic repulsion, leading to unfolding.