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Organic Molecules:, membranes - Coggle Diagram

- - - - Pentoses ::
        5 carbon
      - Hexose 6 carbon
        Eg: Glucose (C6H12O6)
    - - two monosaccharides
      - Joined by dehydration reaction
      - Glycosidic bond between molecules
    - - long polymers
      - joined by many dehydration reactions
      - Uses
        
        Energy storage ; starch and glycogen
        
        Structural – cellulose (plant)
  - - - Deoxyribonucleotide (dna)
      - Ribonucleotide (rna)
      - Sugar-phosphate backbone
  - - - Amino acids polymer
      - joined by dehydration
        reaction
      - peptide bond between monomer
    - - Amino acid sequence
      - Encoded directly
        by genes
    - - α helices
      - Random coiled regions
      - β pleated sheets
      - folding due to hydrogen bonding between atoms in the polypeptide backbone
    - - final level of structure for a single polypeptide
      - 3D shape
      - 5 different types of bonds
        
        hydrophobic interactions
        
        ionic bond
        
        disulfide bridges
        
        hydrogen bond
        
        vanderwaal forces
    - - two or more polypeptides interacting
        
        Specific binding at surface
        
        Hydrogen bonds
        
        Ionic bonds and other polar interactions
        
        Hydrophobic effects
        
        Van der Waals forces
        
        several copies
        of the same polypeptide
        
        multimeric
    - - can be shared between proteins
      - carry out specific biological functions
  - - - non polar and insoluble
      - composed of hydrogen, carbon and some oxygen
    - - fats
        
        functions
        
        energy storage
        
        hydrolysis releases energy from breaking of ester bonds
        
        structural
        
        synthesis
        
        3 fatty acids
        
        Saturated- single C-C bonds
        
        Unsaturated- one or more C=C double bonds
        
        1 glycerol
        
        joined by ester bond
      - phospholipids (amphipathic)
        
        polar phosphate head
        
        non polar fatty acid tail
      - steroids
        
        Four interconnected rings of carbon atoms
        
        insoluble in water
        
        eg: cholestrol
        
        Tiny differences in structure can lead to extremely different biological properties
- - - - Transmembrane
      - Lipid-anchored
    - - non covalenty bound to either
        
        polar phospholipid heads
        
        integral membrane proteins
- - - - Metabolic intermediates remain
      - Waste products exit
      - Essential molecules enter
  - - - requires channel protein
      - Phospholipid bilayer forms Barrier to hydrophilic molecules and ions due to hydrophobic interior
  - - - Form an open passageway for the direct diffusion of ions or molecules across the membrane
    - - Conformational change transports solute across membrane
      - against concentration gradient, using ATP
      - 3 types
  - - - Uses a pre-existing gradient to drive transport
    - - Directly uses energy to transport solute via protein pump
    - - Na+/K+-ATPase
        
        Actively transports Na+ and K+ against their gradients using the energy from ATP hydrolysis
        
        Antiporter – ions move in opposite directions
        Electrogenic pump – exports one net positive (+) charge
      - endocytosis and exocytosis
        
        endocytosis
        
        Plasma membrane invaginates (folds inward) to form a vesicle that brings substances into the cell
        
        3 types
        
        Receptor-mediated endocytosis
        
        Pinocytosis
        
        Phagocytosis
        
        exocytosis
        
        Material inside the cell packaged into vesicles and excreted into the extracellular medium
- - - - diffuse laterally to nuclear envelope
      - via vesicles to Golgi, lysosomes, vacuoles, or plasma membrane
      - Lipid exchange proteins – extract lipid from one membrane for insertion in another
  - - - Process of covalently attaching a carbohydrate to a protein or lipid
      - Glycolipid – carbohydrate to lipid
      - Glycoprotein – carbohydrate to protein
      - Often play a role in cell surface recognition
      - Helps protect proteins from damage
    - - Attachment of carbohydrate to nitrogen atom of asparagine side chain
    - - O-linked Glycosylation
        
        Addition of sugars to oxygen atom of serine or threonine side chains
        
        Occurs only in Golgi
- - - - spontaneously
    - - requires ATP
      - catalyzed by flippase
    - - group of lipids floats together as a unit
      - High concentration of cholesterol
      - Unique set of membrane proteins
    - - Length of fatty acyl tails
        
        the shorter the more fluid
      - Presence of double bonds makes it more fluid
      - Presence of cholesterol
        
        stabilize membranes
        
        Effects vary depending on temperature
  - - - maybe attached to molecules outside the cell
        
        like immobile fibers in the extracellular matrix
      - some are bound to components of cytoskeleton