protein and amino acids with classification.pptx

Proteins and aminoacids with classification

1. Proteins & AMINO ACIDS with classification

2. Biomolecule consisting of chains of amino acid residues are called proteins. Occurrence: Almost every part of the cell About 50% of cellular dry weight Elemental Composition: PROTEINS

3. Classification Primary structure Secondary structure Tertiary structure Quaternary structure

4. Protein Protein is generally used for a polypeptide containing More than 50 amino acids

5. Peptide bond Formation of peptide bond: The amino group of amino acid combine with the carboxyl Group of another amino acids then, a peptide bond is formed.

6. Characteristics of peptide bonds The peptide bond is rigid and planar with partial
double bond in character. It generally exists intrans configuration. Both –C=O and –NH groups of peptide bonds are polar and are involved in hydrogen bond formation

7. Primary structure The Primary structure of proteins is the exact ordering of amino acids forming their chains. The exact sequence of the proteins is very important as it determines the final fold and therefore the function of the protein.

8. Secondary structure The proteins do not exist in just simple chains of polypeptides. These polypeptide chains usually fold due to the interaction between the amine and carboxyl group of the peptide link. They are found to exist in two different types of structures α – helix and β – pleated sheet structures. .

9. Alpha– Helix: A-Helix is the most common spiral structure of protein 1. The a-helix is a tightly packed coiled structure with amino acid side chain 2. The a-helix is stabilized by extensive hydrogen bonding.lt is formed between H atom attached to pep tide N, and O atom attached to peptide. The hydrogen bonds are individually weak. 3. All the peptide bonds, except the first and
last in a polypeptide chain, participate in
hydrogen bonding.
4. Each turn of a-helix contains 3.5 amino
acids and travels a distance of 0.54 nm. The
spacing of each amino acid is 0.15 nm.
5. a-Helix is a stable conformation formed
spontaneously with the lowest energy.

10. Beta pleated sheet In this arrangement, the polypeptide chains are stretched out beside one another and then bonded by intermolecular H-bonds This is the second type of structure (hence alpha
after beta) proposed by Pauling and Corey. Beta -Pleated sheets (or simply beta-sheets) are
composed of two or more segments of fully
extended peptide chain

11. Supersecondary structure The type of protein which is intermediate between the secondary and tertiary structure is called Supersecondary structure . It is connected through loops & bend at specific pattern This is the second type of structure (hence p after a) proposed by Pauling and Corey. p-Pleated sheets (or simply p-sheets) are composed of two or more segments of fully extended peptide chain

12. Tertiary structure The tertiary structure of proteins represents overall folding of the polypeptide chains, further folding of the secondary structure.
It gives rise to two major molecular shapes called fibrous and globular.
The main forces which stabilize the secondary and tertiary structures of proteins are hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.

13. Quaternary structure The spatial arrangement of various tertiary structures gives rise to the quaternary structure. Some of the proteins are composed of two or more polypeptide chains referred to as sub-units. The spatial arrangement of these subunits with respect to each other is known as quaternary structure. Example Hemoglobin Insulin

14. FUNCTIONS OF PROTEINS: Proteins functions may be broadly classified as Structural functions Dynamic functions Structural functions: 1. Collagen: Found in connective tissue, bones, and skin, providing strength, flexibility, and structure. 2. Keratin: Found in skin, hair, nails, and the epithelial lining of organs, providing strength and rigidity. 3. Elastin: Found in connective tissue, allowing for elasticity and flexibility in blood vessels, lungs, and skin. 4. Laminin: Found in the basement membrane, providing a scaffold for cell attachment and tissue organization. 5. Fibronectin: Found in connective tissue, promoting cell adhesion and migration. 6. Actin: Found in muscle cells, providing structural support and contraction.

15. 7. Tubulin: Found in microtubules, providing structural support and transport within cells. 8. Desmin : Found in muscle cells, providing structural support and maintaining cell shape. 9. Vimentin: Found in mesenchymal cells, providing structural support and maintaining cell shape. 10. Cytokeratin: Found in epithelial cells, providing structural support and maintaining cell shape. Dynamic Functions 1. Enzymatic activity: Catalyzing chemical reactions and metabolic processes. 2. Transportation: Carrying molecules, ions, and cells throughout the body. 3. Signal transduction: Transmitting and receiving signals for cellular communication. 4. Mechanical support: Providing structure and mechanical strength to cells and tissues. 5. Regulation: Controlling gene expression, metabolism, and cellular processes. 6. Defense: Participating in immune responses and protecting against pathogens. 7. Transport of molecules: Carrying molecules across cell membranes. 8. Cell-cell interactions: Mediating interactions between cells. 9. Muscle contraction: Facilitating movement and muscle contraction.

16. 10. Hormone regulation: Regulating hormone production and signaling. 11. Apoptosis: Regulating programmed cell death. 12. Intracellular transport: Moving materials within cells. 13. Cytoskeleton dynamics: Maintaining cell shape and mechanical integrity. 14. Cell migration: Facilitating cell movement and migration. 15 . Protein degradation: Regulating protein turnover and degradation.

17. AMINO ACIDS Amino acids are a group of organic compounds containing two functional groups amino and carboxyl STANDARD AMINO ACIDS 300 amino acids occur in nature- Of these, only 20-known as standard amino acids are repeatedly found in the structure of proteins GENERAL STRUCTURE OF AMINO ACIDS The amino acids are termed as α -amino acids, if both the carboxyl and amino groups are attached to the same carbon atom.

18. CLASSIFICATION OF AMINO ACIDS There are different ways of classifying the amino acid Amino acid classification based on the structure Amino acid with aliphatic sidechains:

19. 2. Amino acid containing -OH group

20. 3. Sulfur Containing amino acids

21. 4. Acidic amino acids and their amides

22. 5. Basic amino acids

23. 6. Aromatic amino acids

24. 7. Imino acids

25. B. Classification of amino acids based on polarity Classified into 4 groups based on their polarity Non-polar amino acids: Also referred to as hydrophobic (water hating). Have no charge on the 'R' group. The amino acids included in this group are - alanine, leucine, isoleucine, valine, methionine, phenylalanine, tryptophan and proline 2. Polar amino acids with no charge on 'R’ group Carry no charge on the ‘R’ group Possess groups such as hydroxyl, sulfhydryl and amide. Participate in hydrogen bonding of protein structure. The amino acids in this group are glycine, serine, threonine, cysteine, glutamine, asparagine and tyrosine.

26. 3. Polar amino acids with positive 'R' group Amino acids lysine, arginine and histidine are included in this group . 4. Polar amino acids with negative 'R’ group The dicarboxylic monoamino acidsaspartic acid and glutamic acid are considered in this group C. Nutritional classification of amino acids : Based on the nutritional requirements amino acids are grouped into two classes Essential or indispensable amino acids The amino acids which cannot be synthesized by the body and, therefore, need to be supplied through the diet are called essential amino acids. They are required for proper growth and maintenance of the individual. The ten amino acids listed below are essential for humans (and also rats) : Arginine, Valine, Histidine, lsoleucine , Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan.

27. Arginine and histidine can be synthesized by adults and not by growing children, hence these are considered as semi-essential amino acids 2. Non-essential or dispensabte amino acids Body can synthesize about 10 amino acids hence they need not be consumed in the Diet glycine, alanine, serine, cystein e, aspartate,a sparagni e, glutamate, glutamine, tyrosine and proline D. Amino acid classification based on their metabolic fate From metabolic view point, amino acids are divided into three groups Glycogenic amino acids These amino acids can serve as precursors for the formation of glucose or glycogen. e.g. alanine, aspartate, glycine, methionine etc.

28. 2. Ketogenic amino acids Fat can be synthesized from these amino acids. Two amino acids leucine and lysine are exclusively ketogenic 3. Glycogenic and ketogenic amino acids The four amino acids isoleucine, phenyl - alanine, tryptophan, tyrosine are pre-cursors for synthesis of glucose as well as fat.