SCID Living Process: From Molecules to Cell

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SCID 141 - Living Process: From Molecules to Cell Instructor: Kittisak Yokthongwattana, Ph.D. Department of Biochemistry, Faculty of Science, Mahidol University Amino Acids and Proteins

Amino Acids

Stereo Chemistry of Amino Acids

Different Side Chains of Amino Acids

Different Side Chains of Amino Acids

Different Side Chains of Amino Acids

Different Side Chains of Amino Acids

Different Side Chains of Amino Acids

Amino Acid Abbreviation

Amino Acid Abbreviation

Covalent Bond Formation Between Amino Acids – disulfide bond

Protonation States of Amino Acids

Protonation States of Amino Acids

Peptide Bond Formation

Polypeptide Chain – primary structure

Polypeptide Chain Folds Into Secondary Structure

 AND  ANGLES

Ramachandran plot Image from Voet and Voet, Biochemistry, 4th Edition, 2011

What do  AND  ANGLES signify? Image from Voet and Voet, Biochemistry, 4th Edition, 2011

Polypeptide Chain Folds Into Secondary Structure – alpha helix

Molecular Interaction stabilizing secondary structure is hydrogen bond Image from Lippincott, Fig. 2.6

Polypeptide Chain Folds Into Secondary Structure – alpha helix

Polypeptide Chain Folds Into Secondary Structure – Beta Sheet

Polypeptide Chain Folds Into Secondary Structure – Beta Sheet

Secondary Structures fold into tertiary structure

Intermolecular Interactions that stabilize tertiary structure Disulfide bond formation Hydrophobic interaction Images from Lippincott, Fig. 2.9, 2.10

Intermolecular Interactions that stabilize tertiary structure Ionic interaction Images from Lippincott, Fig. 2.11

Soluble Protein

Chaperone-Assisted Protein Folding – DnaK/DnaJ SYSTEM

Chaperone-Assisted Protein Folding – GroEL/GroES SYSTEM

Transmembrane protein

Transmembrane protein

Transmembrane protein

Transmembrane protein Aquaporin

Voltage-Gated K+ Channel

Example of Chloride Channel

Quaternary Structure of protein is the assembly of tertiary structures http://upload.wikimedia.org/wikipedia/commons/3/3d/1GZX_Haemoglobin.png

Disulfide bond formation also stabilizes protein quaternary structure

Protein folding signifies functions

Collagen is a triple-helix protein The stability of collagen triple helices rely on a sharp turn of the helix caused by an amino acid called hydroxyproline. Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following its de novo synthesis (as a post-translational modification). Such reaction, which requires vitamin C, takes place in the lumen of the endoplasmic reticulum. http://en.wikipedia.org/wiki/Hydroxyproline#mediaviewer/File:Hydroxyproline_structure.svg

Actin – Myosin are major proteins in myocytes

Actin – Myosin are major proteins in myocytes

Actin – Myosin are major proteins in myocytes

Myosin motor

Actin

Movement of myosin motor on Actin filament

Immunoglobulin proteins - IgG

Immunoglobulin proteins

Immunoglobulin proteins - IgM

Phagocytosis of an antibody-bound virus by a macrophage

Hemoglobin Hemoglobin Myoglobin

Heme structure within hemoglobin upon Oxygen binding

The Bohr Effect CO2 and H+ ions also are effectors of hemoglobin. In active muscle cells, oxygen is rapidly consumed and carbon dioxide and H+ ions are produced. O2 affinity decreases at lower pH. As hemoglobin moves into a tissue with lower pH, it can more easily unload oxygen. Increase in CO2 concentrations have the same effect. In combination, the effect of pH and CO2 allow nearly 90% of the oxygen bound in the lungs to be unloaded in tissues where it is required.

Structural Basis of the Bohr Effect

BPG Binding Stabilizes the T state

Sickle Cell Anemia