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Amino Acids, Peptides & Proteins

Amino Acids, Peptides & Proteins. Amino Acids Zwitterion or ampholyte Peptides Proteins Structure of Proteins Separation & purification Protein Sequencing Protein Synthesis. Our Life Is Maintained by Molecular Network Systems. Molecular network system in a cell.

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Amino Acids, Peptides & Proteins

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  1. Amino Acids, Peptides & Proteins Amino Acids Zwitterion or ampholyte Peptides Proteins Structure of Proteins Separation & purification Protein Sequencing Protein Synthesis

  2. Our Life Is Maintained by Molecular Network Systems Molecular network system in a cell

  3. Proteins Play Key Roles in a Living System • Three examples of protein functions • Catalysis:Almost all chemical reactions in a living cell are catalyzed by protein enzymes. • Transport:Some proteins transports various substances, such as oxygen, ions, and so on. • Information transfer:For example, hormones. Alcohol dehydrogenase oxidizes alcohols to aldehydes or ketones Haemoglobin carries oxygen Insulin controls the amount of sugar in the blood

  4. Estimated Functional Roles (by % of Proteins) of the Proteome in a Complex Organism

  5. Protein Functions • Transport • Regulatory • Motor • Fibrous Protein • Enzyme • Immunoglobulin

  6. 20 Amino acids Leucine (L) Isoleucine (I) Valine (V) Alanine (A) Glycine (G) Asparatic acid (D) Proline (P) Asparagine (N) Methionine (M) Tryptophan (W) Phenylalanine (F) Tyrosine (Y) Threonine (T) Serine (S) Cysteine (C) Glutamine (Q) Histidine (H) Glutamic acid (E) Arginine (R) Lysine (K) White: Hydrophobic,Green: Hydrophilic,Red: Acidic,Blue: Basic

  7. a-amino aicds • All proteins are composed of amino acids • Twenty common amino acids • All amino acids are primary amino acids except for proline • A primary amino group is attached to the a-carbon of carboxyl group • Except for Glycine, all other amino acids have at least one chiral centers • All chiral amino acids are belong to L-amino acids

  8. Amino acids vary in Size Structure Electric charge Solubility in water

  9. Classification of amino acids Classified by polarity of side chains hydrophobic: water fearing, non-polar side chains hydrophilic: water loving, polar neutral positively charged negatively charged aromatic

  10. Titration curve of amino acids Neutral side chain Acidic side chain Basic side chain

  11. Peptide Bond

  12. Peptides Dipeptide Tripeptide Tetrapeptide Oligopeptide Polypeptide Protein

  13. Peptide Bond

  14. Replace -ine by -yl but keep the last -ine ! Ala-Gly-Arg Alanylglycylarginine

  15. Structure of Proteins Primary structure Secondary structure Tertiary structure Quaternary structure

  16. Peptide & Protein Charge pI = ?

  17. pI = (8.8 + 10.8)/2 = 9.8

  18. Protein Separation/Purification • In general, proteins contain > 40 residues • Minimum needed to fold into tertiary structure • Usually 100-1000 residues; percent of each AA varies • Proteins separated based on differences in size and composition • Proteins must be pure to analyze, determine structure/function • Factors to control (to avoid denaturation or chemical degradation) • pH • Presence of enzymes • Temperature • Reactive thiol groups • Exposure to air, water

  19. Methods of Separation/Purification • Solubility (salts, solvents, pH, temperature) • Chromatography • Ion exchange • Gel filtration • Affinity • Electrophoresis

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