1 / 31

Short polymer

HO. HO. H. 1. 2. 3. H. Short polymer. Unlinked monomer. Dehydration removes a water molecule, forming a new bond. H 2 O. HO. 2. H. 4. 1. 3. Longer polymer. (a) Dehydration reaction in the synthesis of a polymer. HO. H. 3. 4. 2. 1. Hydrolysis adds a water

awestover
Download Presentation

Short polymer

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  1. HO HO H 1 2 3 H Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond H2O HO 2 H 4 1 3 Longer polymer (a) Dehydration reaction in the synthesis of a polymer HO H 3 4 2 1 Hydrolysis adds a water molecule, breaking a bond H2O H HO HO 2 H 1 3 (b) Hydrolysis of a polymer

  2. Trioses (C3H6O3) Pentoses (C5H10O5) Hexoses (C6H12O6) Aldoses Glyceraldehyde Ribose Glucose Galactose Ketoses Dihydroxyacetone Ribulose Fructose

  3. (a) Linear and ring forms (b) Abbreviated ring structure

  4. 1–4 glycosidic linkage Glucose Glucose Maltose (a) Dehydration reaction in the synthesis of maltose 1–2 glycosidic linkage Glucose Fructose Sucrose (b) Dehydration reaction in the synthesis of sucrose

  5. Mitochondria Chloroplast Starch Glycogen granules 0.5 µm 1 µm Glycogen Amylose Amylopectin (a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide

  6. (a)  and  glucose ring structures  Glucose  Glucose (b) Starch: 1–4 linkage of  glucose monomers (b) Cellulose: 1–4 linkage of  glucose monomers

  7. Cell walls Cellulose microfibrils in a plant cell wall Microfibril 10 µm 0.5 µm Cellulose molecules • Glucose monomer

  8. (a) (c) (b) Chitin forms the exoskeleton of arthropods. The structure of the chitin monomer. Chitin is used to make a strong and flexible surgical thread.

  9. Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol)

  10. Structural formula of a saturated fat molecule Stearic acid, a saturated fatty acid (a) Saturated fat Structural formula of an unsaturated fat molecule Oleic acid, an unsaturated fatty acid cis double bond causes bending (b) Unsaturated fat

  11. Choline Phosphate Hydrophilic head Glycerol Fatty acids Hydrophobic tails Hydrophilic head Hydrophobic tails Space-filling model Phospholipid symbol (a) (b) (c) Structural formula

  12. Hydrophilic head WATER Hydrophobic tail WATER

  13. Substrate (sucrose) Glucose Enzyme (sucrase) OH H2O Fructose H O

  14.  carbon Carboxyl group Amino group

  15. Nonpolar Glycine (Gly or G) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Alanine (Ala or A) Trypotphan (Trp or W) Methionine (Met or M) Phenylalanine (Phe or F) Proline (Pro or P) Polar Glutamine (Gln or Q) Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Electrically charged Acidic Basic Glutamic acid (Glu or E) Histidine (His or H) Aspartic acid (Asp or D) Lysine (Lys or K) Arginine (Arg or R)

  16. Peptide bond (a) Side chains Peptide bond Backbone Amino end (N-terminus) Carboxyl end (C-terminus) (b)

  17. Groove Groove (a) (b) A ribbon model of lysozyme A space-filling model of lysozyme

  18. Protein from flu virus Antibody protein

  19. Tertiary Structure Primary Structure Secondary Structure Quaternary Structure  pleated sheet +H3N Amino end Examples of amino acid subunits  helix

  20. Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond

  21. Polypeptide chain  Chains Iron Heme  Chains Hemoglobin Collagen

  22. Normal hemoglobin Sickle-cell hemoglobin Primary structure His Val Leu Glu Glu His Thr Val Primary structure Thr Pro Val Leu Pro Glu 1 2 3 4 5 6 7 1 2 3 4 5 6 7 Exposed hydrophobic region Secondary and tertiary structures Secondary and tertiary structures  subunit  subunit     Sickle-cell hemoglobin Quaternary structure Normal hemoglobin (top view) Quaternary structure     Function Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. Function Molecules do not associate with one another; each carries oxygen. 10 µm 10 µm Red blood cell shape Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. Red blood cell shape Fibers of abnormal hemoglobin deform red blood cell into sickle shape.

  23. Denaturation Denatured protein Normal protein Renaturation

  24. Correctly folded protein Polypeptide Cap Hollow cylinder Steps of Chaperonin Action: Chaperonin (fully assembled) The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide. The cap comes off, and the properly folded protein is released. 2 3 1 An unfolded poly- peptide enters the cylinder from one end.

  25. DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore Ribosome 3 Synthesis of protein Amino acids Polypeptide

  26. 5 end Nitrogenous bases Pyrimidines 5C 3C Nucleoside Nitrogenous base Thymine (T, in DNA) Uracil (U, in RNA) Cytosine (C) Purines Phosphate group Sugar (pentose) 5C Adenine (A) Guanine (G) (b) Nucleotide 3C Sugars 3 end (a) Polynucleotide, or nucleic acid Ribose (in RNA) Deoxyribose (in DNA) (c) Nucleoside components: sugars

  27. 5' end 3' end Sugar-phosphate backbones Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 3' end 5' end New strands 5' end 3' end 5' end 3' end

More Related