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Biomolecules - Proteins & Amino acids
- 1. Presented By, Revathi Gnanavelou,M.Pharm, Pharmaceutical Chemistry SVCP BioMolecules
- 2. ❑Macromolecules ❑Made up ofAmino acids ❑Heteropolymers of straight chain amino acids joined together b/w one ends of –COOH group with other end of amino group of successive amino acids by peptide bond
- 3. ❑Condensation of productsof many amino acids ➔ Polypeptide ❑Monomeric & Multimeric ➔ single / multi polypeptide chain ❑Function of proteins ➔ depends on its structures, chemical nature, nutritional requirement, metabolic fate etc.,
- 4. PROTEIN Based on size& Shape Based on Foundational Properties Based on solubility & Physical characteristics Fibrous Eg: Collagen Globular Eg: Hemoglobin Myoglobin Defense Eg: Immunoglobulin Contractile Eg: Skeletal muscle Respiratory Eg: Hemoglobin Structural Eg: skin, bones, nails Enzymes Hormones Simple Protein They are are hydrolyzed to amino acid residue Conjugated Protein In addition to amino acid – contain non- protein group Derived Protein formed from native protein by heat 10 Derived Eg: Metaprotein proteans 20 Derived Eg: Peptides Peptones
- 5. CHEMICAL NATURE OFPROTEINS • Proteins react with acids or enzymes ➔ form peptides + free amino acids Hydrolysis • Non-Covalent bonds break with the help of heat ➔ Denaturation • Molecular weight ranging from 5000 to 3,000,000 • They provide structural support to cells
- 6. •Protein exist assimple long chain of amino acid sequence •Eg: Insulin Primary Structure •Long chain proteins folded & arranged in a helix shape by formation of hydrogen bonds •Pleated sheet ( α & ß helix (stable) ) Eg: Silk fibres Secondary Structure •Long polypeptide chain formed with ionic or hydrophobic bonds or disulphide bridges help of folding & coiling - more stabilized •Eg: Myoglobin Tertiary structure •Protein molecule formed with more than one polypeptide or subunits of its own •Eg: Haemoglobin, insulin Quarternary structure
- 8. PRIMARY STRUCTURE ❖ Linearsequence of amino acids in a polypeptide chain is its primary structure. ❖ Amino acids joined by peptide bond ❖ Non-functional Eg: Pancreatic hormone insulin has two polypeptide chains, A and B, and they are linked together.
- 9. INSULIN • Insulin isa protein composed of two chains, an A chain ( 21 amino acids) and B chain (30 amino acids), which are linked together by sulfur atoms. • Insulin is derived from a 74-amino-acid prohormone molecule called proinsulin.
- 10. SECONDARY STRUCTURE Linear sequenceof amino acids which contain hydrogen bonds • Alpha Helix 1. Amino acids joined by peptide bonds 2. Hydrogen bonds formed between amino acids of same chain Eg: Keratin • Beta helix 1. Two or more polypeptide chain segment line up side by side 2. H-bonds formed b/w amino acids of two chains Eg: silk fibres
- 12. TERTIARY STRUCTURE • Coiledor folded chains formed • More bonds formed due to interaction b/w R-groups of polypeptide chain • Types of Bonding 1. Disulphide bridge (-S-S-) 2. H-Bonding (C=O…H-N) 3. Salt bridge (COO-…+NH3) 4. Hydrophobic interactions 5. Vander waals forces
- 13. Red iron-containing proteinpigment in muscles Heart attack or severe muscle damage, myoglobin is released into your blood ➔ increases in your blood 2 to 3 hours after the first symptoms of muscle damage. captures oxygen that muscle cells use for energy.
- 14. QUARTERNARY STRUCTURE • Composedof two or more polypeptide chains • Types of Bonding 1. Disulphide bridge (-S-S-) 2. H-Bonding (C=O…H-N) 3. Salt bridge (COO-…+NH3) 4. Hydrophobic interactions 5. Vander waals forces
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- 19. FUNCTIONS OF PROTEINS MajorSource of energy • Building blocks • Structural component of cell Enzymes • Proteinous in nature • Catalyze rxns in body Antibodies • Proteins protect body from invasion of microbes • Maintains Osmotic pressure Buffers • Transport nutrients • Structure of cell formed by structure of proteins
- 20. BIOLOGICAL ROLE OFPROTEINS
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- 22. CLASSIFICATION OF AMINOACID AMINO ACIDS Hydrophilic Amino acids (POLAR) Neutral Amino acids Tyrosine, Aspargine, Serine (TAS) Acidic Amino acids Glutamic acid, Aspartic acid (GA) Hydrophobic Amino acids (NON-POLAR) Aliphatic Amino acids Valine, Alanine, Glycine (VAG) Aromatic Amino acid Phenylalanine, Tryptophan (PT) Basic Amino acids Histidine, Arginine, Lysine (HAL)
- 23. STRUCTURES OF AMINOACIDS
- 24. CHEMICAL NATURE OFAMINO ACID • Organic Biomolecules • Made up of amine (-NH2) & Carboxylic (-COOH) functional group • Forms salt with bases and esters by reaction with alcohol • Undergo decarboxylation to form amines • React with ammonia to form amides like glutamine, aspargamine • More soluble in water than ether • Less acidic than carboxylic acids and less basic than amines • Have larger dipole moment than simple acids & amines
- 25. React with ammoniato form amides like glutamine, aspargamine
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- 29. FUNCTIONS OF AMINOACIDS • Building block of proteins • Acts as precursors for biosynthesis of other secondary metabolites • Used as neurotransmitters like γ-amino butyric acid & dopamine are derived from glutamic acid & tyrosine • Function as thyroid hormone like thyroxine derived from tyrosine
- 30. BIOLOGICAL ROLE OFAMINO ACIDS ➢Molecules That form a part of enzyme ➢Precursors for synthesis of various molecules such as heme ➢Responsible in many functions of metabolism ➢Building block of proteins ➢Mixture of amino acids available in cell derived from degradation of protein termed as amino acid pool ➢Constant turnover of proteins because proteins and amino acids are not stored in the body ➢Eg: Biosynthesis of tissue proteins ➢Haemoglobin ➢Myoglobin