Levels of protein structure.pptx
- 1. LEVELS OF PROTEIN STRUCTURE PRESENTED BY OM PRAKASH SHAH 1
- 4. PRIMARY STRUCTURE Proteins are made up of building blocks called Amino. And there are 20 different types of amino Acids present in our body. These amino acids are held togather by a covalent bond known as Peptide Bond. These Amino Acids binded in a specific sequence by the process called Translation to form a Poly-Peptide Chain. This specific sequence of Amino Acids in the Polypeptide is called the Primary Structure. Each Amino Acids in the Primary Structure are also Known as Residue. 4
- 5. PRIMARY STRUCTURE The Polypeptide Chain in a Protein Molecule has the ability to form many Hydogen Bonds. This is because each one of the Amino Acids contains two types of Functional Groups- N-H - Group - Hydohen Bond Donor. C=O - Group - Hydohen Bond Acceptor. This phenomena play an important role on the formation of secondary structure of protein. It is also important to note that the Peptide Bond of the polypeptide chain is Double Bond in nature i.e they cant rotate 5
- 7. SECONDARY STRUCTURE Once the primary structure of protein is formed, It begins to twist and turn into regular patters that make up its secondary structure. These regular patterns include- α-Helix. β Plated Sheets. β Turns. Ω Loops. This twist and turns are formed as a result of the regular pattern of the hydrogen bonds between NH and CO groups on the polypeptide chain. 7
- 8. The Alpha Helix is the Twisted structure of polypeptide chain. It contains the Back bone on inner portion of the chain and on the outer side there are the side chain. This structure is formed as a results of bond formation between the NH group and CO group. ALPHA HELIX 8
- 9. The beta pleated sheet is polypeptide chains running along side each other linked together by hydrogen bonds. It is called the pleated sheet because of the wave like appearance. This allow to form more H-bonds in the Polypeptide and thus resulting in more compact structure. BETA PLATED SHEETS 9
- 10. Beta turns, also known as beta bends or tight turns, are a type of secondary structure. Beta turns change the direction of the peptide backbone by nearly 180°, allowing the peptide chain to fold back onto itself These turns generally occur when the protein chain needs to change direction in order to connect two other elements of secondary structure. They are composed of Four Amino Acids and there is a H- Bond between the first AA and the fourth AA. BETA TURNS 10
- 12. The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain will take within its local environment. There are several factors / interaction between the amino acids that leads to the formation of this structure,namely- 1. Hydrobhobic Interaction. 2. Di-sulphide Bridge. 3. Hydrogen Bond. 4. Hydrophillic Interaction. 5. Ionic Bond. TERTIARY STRUCTURE 12
- 14. The quaternary structure of a protein is formed when two or more polypeptide (Subunit) bind togather to give a single protein having a specific function. Protein quaternary structure is the fourth (and highest) level of protein structure. Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains. Not all proteins have a quaternary structure since some proteins function as single units. Depending upon the number of subunit these proteins are named as Monomer, Dimer, Trimer, Tertramer........ QUATERNARY STRUCTURE 14
- 16. DOMAINS Domains are distinct functional and/or structural units in a protein. • It is a region of the protein's polypeptide chain that is self- stabilizing and that folds independently from the rest. • The independent folded regions are connected by a Hinge region. • This hinge region arises when small AA like Glycine are found in a repeated sequence in a poplypeptide chain. 16
- 18. • Two or more than two secondary structure (Super Secondary) combine togather during protein folding to form MOTIF. • It is a tertiary structure that arises by combing two or more than two secodary structure. • It provide function to a protein. Motifs are super secondary structure in a polypeptide chain. MOTIFS 18
- 20. • It is the process by which the Primary Structure is converted into Secondary Structure, the Secondary to Tertiary and Tertiary to Quaternary Structure. • There are two types of protein foldings that is observed depending upon the timing of folding. 1. Co-Translational folding- Ocuurs while translation is going on. 2. After translation- Occurs after the Translation process is completed. Protein folding is the process by which a protein gets its 3-Dimentional structure FOLDINGS 20
- 21. VIDEO LINKS 1. Overview of Structure of protein. 2. Primary Structure of Protein. 3. Secondary Structure of protein. 4. Tertiary Structure of Protein. 5. Quaternay Structure of Protein. 6. Motifs and Domains. 7. Protein Foldings. 21
- 22. THANK YOU FOR LISTENING DANDWASTH DHANYAWAAD 22