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biology 1 mindmaps, unit 6 Energy, Enzymes, and metabolism, Unit 3…

- - - - lock and key model
      - induced fit phenomenon
  - - - competitie
      - non competitive
    - - Vmax
      - Michaelis constant Km
    - - prosthetic groups
      - cofactors
      - coenzymes
  - - - anabolic
        
        energy drive exergonic reactions
        
        synthesis of macromolecules or micromolecules
      - catabolic
        
        recycles
        
        energy drive endergonic reactions
- - - - occurs if change in Gibbs energy is negative
      - exergonic is spontaneous
      - endergonic is nonspontaneous
  - - - used for cell reactions
- - - - oxidation
      - reduction
    - - is an energy intermediate
      - used for ATP synthesis
      - donates electrons
        
        reducing agent
- - - - structural isomers
      - stereoisomers
        
        Enantiomers
        
        Cis/ trans
- - - - hexoses
        
        fructose
        
        galactose
        
        glucose
      - linear or ring structure
        
        glucose isomers
        
        alpha and beta
        
        D and L enantiomers
      - pentoses
        
        deoxyribose
        
        ribose
    - - made of 2 monosaccharides
      - sucrose/ maltose/ lactose
    - - long polymers (glycosidic bonds)
      - energy storage
        
        starch (moderatly branched)
        
        glycogen (highly branched and globular)
      - structural
        
        cellulose/ chitin/ glycosaminoglycans (flat sheets)
  - - - glycerol, 2 fatty acids, and 1 phosphate
      - Amphipathic
        
        phosphate head polar / hydrophilic
        
        fatty acid tail nonpolar / hydrophobic
    - - triglycerides
      - glycerol and 3 fatty acid chains
      - Ester bonds
    - - high energy storage
      - saturated (solid)
      - unsaturated (liquid)
        
        cis is natural
        
        trans is artificial (solid)
    - - rings of carbon (like cholesterol)
      - hydrophobic
      - specific biological properties
  - - - 20 amino acids
      - variable side chains
    - - carboxyl group+ amino acid = peptide + water
      - N terminus and C terminus
      - polymers of amino acids
      - structure
        
        primary
        
        amino acid sequence
        
        secondary
        
        hydrogen bonds
        
        alpha helix
        
        beta pleated sheets
        
        random coiled region
        
        tertiary
        
        ionic bonds
        
        van-der wall forces
        
        disulfide bridges
        
        hydrophilic / hydrophobic interactions
        
        hydrogen bonds
        
        3D structure
        
        quaternary
        
        multiple polypeptides
  - - - A pentose sugar
      - nitrogen base (AGCT-U)
      - phosphate group
      - polymers have sugar phosphate backbone
    - - DNA
        
        thymine
        
        2 strands (double helix held be hydrogen bonds
        
        deoxyribonucleic acid
      - RNA
        
        Uracil
        
        ribonucleic acid
        
        single strand
        
        Several forms
- - - - stacks
      - vasicles
    - - Rough ER (for protiens)
      - smooth ER (for lipids and processing)
    - - contractile vacoul
      - phagocytic vacoul
      - central vacoul
  - - - intermediate fillaments
      - Actin filaments (microfilaments)
      - microtubules
    - - caries cargo
      - moves filament
      - bends fillament
- - - - transmembrane gradient
      - ion electrochemical gradient
    - - plants: turgid - flaccid - plasmolysed
      - freshwater protists have contractile vacuoles to control water pressure
      - animals: crenation - normal - lysis
    - - isotonic
      - hypertonic
      - hypotonic
  - - - symporter (cotransporter)
      - antiporter
      - uniporter
- - - - new aminoacyl tRNA enters A cite
      - polypeptide removed from the tRNA in P cite and bind to tRNA in A cite
      - codon anticodon recognition
      - translocation of ribosome by 1 codon towards 5'-3'
      - uncharged tRNA exits from E cite
    - - ribosome reaches a stop codon (UAA, UAG, UGA)
      - stop codon not recognized by tRNA, but by a release factor protein
      - release factor dissociates ribosome, and hydrolysis bond between the polypeptide and the last tRNA
    - - guanosine cap at 5' recognized by cap binding protein in eukaryotes
      - start codon recognized by aminocyl tRNA (AUG)
        
        forms a complex
        
        both enter the ribosome in the p cite
      - ribosomal binding sequence in prokaryotes