A is determined by the peptide bond

A primarystructure is the distinctive sequence of amino acids which make up aprotein. This sequence is also known as a polypeptide chain. Ala-Gly-Val-Tyr-Arg-Leu-Ser-Met-Asn-Cys-ProAGVYRLSMNCPTo make it less complicated and abbreviate each aminoacid residue with either a three letter or one. The proteinchain in the primary structure depends all on the identification of the aminoacid sequence.

These molecules determine how the molecular chain will fold. Diagram:    The polypeptide bonds are created by enzymecatalysed condensationreactions. Then it is broken by the enzyme catalysedhydrolysis reactions. The monomers in the diagram below show that they formproteins. Proteins are made up of a variation ofamino acid polymers, and they are different type of bio-molecule in our bodies.Differentprotein types include enzymes that catalyse chemical reactions receptors thatcontrol signalling in bodies.

Haemoglobin carried oxygen throughout the bloodstream,muscle and organ tissue, which gives your body structure and mobility, and somany other things.Amino acids form peptide bonds with one another, thepeptide bond between the two–NH and CO units, cause a condensation reaction.     This is called a carboxyl group.

Every amino acid has this.   A condensationreaction is the reaction of two small molecules that make a larger molecule– e.g. H2OIn this process water is removed. *draw picture*                                        Protein is a longpolypeptide chain of amino acids.

Amino acids are attached together via thepeptide bonds. Then they make chains of amino acid chain. Once the primarystructure of the polypeptide is formed, it begins to twist into regularpatterns that make up the secondary structure.

The primary structure just describesthe linear sequence of amino acids, and it is determined by the peptide bondthat links to each amino acid. This is a simple linear structure. You take anamino acid and bond them together and that bond is called a peptide bond , verystrong covalent bonds. Seondary structure forms as hydrogen bonds form betweenbackbone atoms. The teriary structure is the final fold of the protein and thatis held by hydrogen, ionic and disulfide bonds. The proteins which have morethan one polypeptide chain is a quaternary structure and that is represtned bythree dimensional arrangement. Beta pleated sheet and ?loop. Thesetwists are formed of as a regular pattern of hydrogen bonds between NH and C=O groupson thee polypeptide chain.

This is called a zigzag pleated sheet and are formed by hydrogenbonds.             In secondarystructure there are hydrogen bonds forming between the peptide groups. In thesecondary structure the major bond is the hydrogen bond apart from the peptidebond and disulphate bond.In this they refer to the platedsheet or helix that a protein chain can form due to hydrogen boding. Theoverall shape of a polupeptide is called tertiary structure ; this happens inthe r groups of amino acids in the chain.

After they have formed polypeptidechains they are now called proteins.  Each amino acidconsists of a central atom with an amino acid group a carboxyl group and ahydrogen atom. Peptide bon is formed when a water molecule is taken on during areaction between –NH2 of one amino acid and –COOH of another amino acid.  Disulphide bondoccurs only in certain amino and specific group which is referred as asulfhydryl group. When the SH groupsof two cysteine residues are covalently linked as a dithiol by oxidation thatis when disulphide bonds arise.

Hydrogen bond is abond between a hydrogen atom and an electronegative atom like oxygen, nitrogen.In amino acids the electromagnetic attract interactions between polarmolecules. So the bond is weak when hydrogen is stuck to a highlyelectronegativeatom, like N or O. Task2 Tertiarystructure there are hydrophobic bonds, hydrogen bonds, ionic bonds, Van derWalls forces, Di-sulphite bonds. As amino acids interact the protein may foldupon itself. Inthe Quaternary structure there are hydrophobic bonds, hydrogen bonds, ionicbonds, Van der walls forced an di-sulphite bonds. Ionicbond is a bond between oppositely charged amino acids of an aspartic acid whichis a base acidic amino acid it is a negatively charged where as lysine is apositively charged amino acid.

Van der walls force is a weak electrical force betweenatoms. Also it is the sum total of all non covalentbonds between electricallyequal molecules. They hold molecules together. Hydrophobic:      These bluemolecules in the figure are hydrophilic regions and the red ones are thehydrophobic regions. The hydrophobic is also referred as water-hating aminoacids. Hydrophobicinteractions actually the bond between two no polar groups.

The structureof  the side chain can closely associateand are protected from interaction with solvent water.  So each type of a proteinhas a three-dimensional structure; this shows the order of the amino acids inits chain. A protein can be unfolded or denatured by exploringwith certain solvents, which causes disturbance to the no covalent interactionsthat hold the folded chain together.

This causes the protein to transfer into aflexible polypeptide chain which loses its original shape. When the denaturingsolvent is removed, the protein often refolds automatically. 


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