Essay Example on A primary structure is the distinctive sequence of amino Acids








A primary structure is the distinctive sequence of amino acids which make up a protein This sequence is also known as a polypeptide chain Ala Gly Val Tyr Arg Leu Ser Met Asn Cys Pro AGVYRLSMNCP To make it less complicated and abbreviate each amino acid residue with either a three letter or one The protein chain in the primary structure depends all on the identification of the amino acid sequence These molecules determine how the molecular chain will fold Diagram The polypeptide bonds are created by enzyme catalysed condensation reactions Then it is broken by the enzyme catalysed hydrolysis reactions The monomers in the diagram below show that they form proteins Proteins are made up of a variation of amino acid polymers and they are different type of biomolecule in our bodies Different protein types include enzymes that catalyse chemical reactions receptors that control signalling in bodies Haemoglobin carries oxygen throughout the bloodstream muscle and organ tissue which gives your body structure and mobility and so many other things Amino acids form peptide bonds with one another the peptide bond between the two NH and CO units cause a condensation reaction A condensation reaction is the reaction of two small molecules that make a larger molecule e g H2O In this process water is removed draw picture

Protein is a long polypeptide chain of amino acids Amino acids are attached together via the peptide bonds Then they make chains of amino acid chain Once the primary structure of the polypeptide is formed it begins to twist into regular patterns that make up the secondary structure The primary structure just describes the linear sequence of amino acids and it is determined by the peptide bond that links to each amino acid This is a simple linear structure You take an amino acid and bond them together and that bond is called a peptide bond very strong covalent bonds Secondary structure forms as hydrogen bonds form between backbone atoms The tertiary structure is the final fold of the protein and that is held by hydrogen ionic and disulfide bonds The proteins which have more than one polypeptide chain is a quaternary structure and that is represented by three dimensional arrangement Beta pleated sheet and Ω loop These twists are formed of as a regular pattern of hydrogen bonds between NH and C O groups on thee polypeptide chain This is called a zigzag pleated sheet and are formed by hydrogen bonds In secondary structure there are hydrogen bonds forming between the peptide groups In the secondary structure the major bond is the hydrogen bond apart from the peptide bond and disulphate bond In secondary structure the structure is referred to the plated sheet that a proteinchain can form because of hydrogen bonding When the process is finished that whole shape of the polypeptide is refereed as tertiary structure So after the polypeptide chains form they are now called proteins This happens in the r groups of amino acids in the chain 6 Each amino acid consists of a central atom with an amino acid group a carboxyl group and a hydrogen atom Peptide bon is formed when a water molecule is taken on during a reaction between NH2 of one amino acid and COOH of another amino acid Disulphide bond occurs only in certain amino and specific group which is referred as a sulfhydryl group When the SH groups of two cysteine residues are covalently linked as a dithiol by oxidation that is when disulphide bonds arise Hydrogen bond is a bond between a hydrogen atom and an electronegative atom like oxygen nitrogen In amino acids the electromagnetic attract interactions between polar molecules 

So the bond is weak when hydrogen is stuck to a highlyelectronegative atom like N or O Task 2 Tertiary structure there are hydrophobic bonds hydrogen bonds ionic bonds Van der Walls forces Di sulphite bonds As amino acids interact the protein may fold upon itself In the Quaternary structure there are hydrophobic bonds hydrogen bonds ionic bonds Van der walls forced an disulphide bonds Ionic bond is a bond between oppositely charged amino acids of an aspartic acid which is a base acidic amino acid it is a negatively charged whereas lysine is a positively charged amino acid Van der walls force is a weak electrical force between atoms Also it is the sum total of all non covalent bonds between electrically equal molecules They hold molecules together Hydrophobic These blue molecules in the figure are hydrophilic regions and the red ones are the hydrophobic regions The hydrophobic is also referred as water hating amino acids Hydrophobic interactions actually the bond between two no polar groups The structure of the side chain can closely associate and are protected from interaction with solvent water So each type of a protein has a three dimensional structure this shows the order of the amino acids in its chain A protein can be unfolded or denatured by exploring with certain solvents which causes disturbance to the no covalent interactions that hold the folded chain together This causes the protein to transfer into a flexible polypeptide chain which loses its original shape When the denaturing solvent is removed the protein often refolds automatically

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