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Amino Acid & Protein

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Amino Acid & Protein Amino Acid & Protein DR. MD. MAHBUBUR RAHMAN MBBS, M. Phil . MSc.(Biotechnology) DEPT. OF BIOCHEMISTRY RAJSHAHI MEDICAL COLLEGE At the end of the session Student will be able to • Definition of amino acid, formation of peptide bond & its property • Biomedical importance of AA • Protein cycle At the end of the session Student will be able to • Classification of AA, • Isoelectric pH and 2D electrophoresis • Protein – definition, classification & structure, • purification of protein Biomedical Importance • Monomeric unit of Protein/ Polypeptide • Amino acid and their derivatives participate in diverse cellular function • Further discussed in functional classification Biomedical Importance Peptide performs prominent role in neuroendocrine system eg. Hormone , Neurotransmitter, Transporter Human lack of capability to synthesize 10 of the 20 common A-Acid (most of them α amino acid) Diversity of Protein function Enzyme and hormone regulate metabolism muscle movement by protein (contractile protein) Collagen fiber forms bone Ig fights against infectious Bacteria & viruses Bacitracin and gramicidin act a antibiotic Bleomycin act anticancer agent Amino Acid Are organic acid having both carboxyl group and amino group attach to same carbon atom. Peptide Bond In protein, amino acids are joined covalently By peptide Bond which are amide linkage Between the α-carboxyl group of one amino acid and the α- amino group of another Characteristic of peptide bond Net charge of amino acid at neutral pH • At physiologic pH all amino acid have a negatively charged group (- COO-) and positively charged group ( - NH3).----- is called amphoteric( ampholyte) Isoelectric pH The pH at which amino bears no net charge. The pH at which amino acid are electrically neutral that is the sum of positive charge equals the sum of negative charge Optical properties of amino acid α carbon of each amino acid are attached to four different group there fore amino acid have optical isomerism. CLASSIFICATION According to their polarity and structural features. Nonpolar Aliphatic Amino Acid Aromatic Amino Acid Aliphatic polar, Uncharged Amino Acids Sulpher containing amino acid Acidic and Basic amino acid On the basis of their nutritional requirement Essential Amino Acid e.g lysin Leucine Non essential Amino Acid e.g. serine On the basis of their metabolic end product • Glucogenic amino acid e.g. Methionine and threonine • Ketogenic Amino acid e.g. Lysin and Leucine GLUCOGENIC AMINO ACID • Amino acid whose catabolism yields pyruvate or one of the intermediate of the citric acid cycle are termed glucogenic amino acid. eg Threonine, Methionine, valine Ketogenic amino acid • Amino acid whose catabolism yields either acetoacetate or one of the precursor of (acetyle co A or acetoacyl co A) are termed ketogenic amino acid. eg: lysin, Leucine Protein Proteins are macromolecules composed of amino acid linked by peptide bond. Functional classification of Protein • Enzymatic catalysis - Glucokinase • Transport and storage- Hb, albumin, Transferin • Structural element of the cytoskeleton- microtubule, Microfilament • Immunity - immunoglobulin • Hormonal – Insulin, GH, • Receptor protein- LDL receptor, • Regulatory – membrane channel Structure of Protein • Primary structure • Secondary structure • Tertiary structure • Quaternary structure Primary structure of protein Secondary Structure Tertiary structure Hemoglobin structure Quaternary structure Life cycle of protein protein purification Technique PROTEOMICS & THE PROTEOME The Goal of Proteomics Is to Identify the Entire Complement of Proteins Elaborated by a Cell Under Diverse Conditions Denaturation of protein • Results in the unfolding and disorganization of the protein structure which are not accompanied by hydrolysis of peptide bond. • Denaturing agent – Heat, Organic solvent, Mechanical mixing, Strong acid or Bases. detergents and ion of heavy metal ( lead, mercury) Classification of protein • On the basis of composition and solubility – simple protein – albumin, globulin – conjugated protein- glycoprotins – Derived protein- peptones & amino acid Classification of the basis of Shape Globular proteins Fibrous proteins Classification of the basis ofnutritional requeirment Nutriotionally rich proteins Incomplete Proteins .
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