Marcomolecules and Bonding

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Author:
rica_ross
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226493
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Marcomolecules and Bonding
Updated:
2013-07-09 21:50:58
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Biology
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Biology GRE
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  1. Monomers
    Single Molecules
  2. Polymers
    Lots of molecules
  3. Basic forms of:
    Proteins
    Carbs
    Lipids
    Nucleic Acids
    • Proteins--> Amino Acids CHNO
    • Carbs--> Simple Sugars (glucose/fructose) CHO
    • Lipids-->Glycerol and Fatty acids  CHO
    • Nucleic Acids--> Nucleotides (phosphates, sugar, base)
  4. Amino Acids is made up of
    • Amino (NH2) Acids (COOH) Carboxyl group
    • R variable group on central C, gives shape and function
  5. Zwitterions
    Monomeric, or unbound amino acids, pH 7, term shows how amino acids act as pH buffers.

    • A overall neutral molecule can have charged/polar ends. So the positive amino end picks up an extra OH-, and negative carboxly end picks up extra H+ ions
    • --> no free H+ ions for pH changes
  6. Dehydration Synthesis
    Carboxyl carbon (COOH) binds to the amino N (NH2) of another amino acid. 

     OH- and H+ are lost from each end and form H20

    Forms a Dipeptide bond, two attached amino acides.
  7. Dipeptide Bond
    Two attached amino acids via OH- and H+
  8. Levels of Protein Structure- Primary
    Primary, Linear
  9. Levels of Protein Structure- Secondary
    alpha helixes, or beta pleated sheets
  10. Alpha Helices, and Beta Pleated Sheets
    • Alpha Helices- tightly wond coils
    • Beta Pleated Sheets- straight chains held above or below due to hydrogen bonding
  11. Levels of Protein Structure-Tertiary
    Bonding of amino acid side chains that are father apart. 

    Bonding occurs with disulfide bridges, via hydrophilic, and hydrophobic ends.
  12. Levels of Protein Structure- Quatanery
    Multi sub-unit structures and build one large protein

    Ex: Hemiglobin
  13. Lipids- Summary
    Non polar, insoluble in water, used for energy storage
  14. Fatty Acids
    long chains with COOH (carboxyl acid) group at one end

    all have formula CH3(CH2)n

    n is between 12-24 and even
  15. Saturated Fatty Acids vs Unsaturated Fatty Acids
    • Saturated- single bonded hydrocarbons
    • Unsaturated- Double bonded or have at least one double bond making them bendy/kinky
  16. Glycerides
    Esters made of glycerol, 1-3 fatty acid chains

    • with 1 fatty acid chain- monoglyceride
    • with 3 fatty acid chainrs- triglyceride
  17. Phosopholipids
    Predominate lipid in cell membranes

    glycerol plus two fatty acid chains, phosphate group attached to the R group

    Phosphate group makes one end polar and hydrophilic

    Fatty acid makes one end nonpolar and hydrophobic 

    antipatic molecule creates a lipid bilayer around cell
  18. emulsification
    amphipatic lipids (having two poles) surround a fat droplet and break it down into smaller pieces

    ex: similar to detergents and soaps
  19. Complex lipids examples, and what are they useful for?
    • lipids grouped together with other molecules
    •  ex: triglycerides, phosopolipids
    • useful for transporting various substances around the body, they get surrounded with lipid or protein barrier
  20. Chylomicrons
    surround and transport fats from intestines to other tissues
  21. Non glycerides
    includes steroids, such as cholesterol, characterized by core of four fused carbon rings
  22. Monosaccharides
    simple sugars in specific CHO ratios, either in rings or chains

    • general formula (CH20)n
    • n-#carbond in sugar ring
  23. Glucose
    C6H12O6
  24. Glycosidic Bonds, two forms
    bridge one sugar to another across an oxygen atom

    • alpha linkage- chain bendy
    • beta linkage- straight chain
  25. Glycosidic Bonds - alpha linkages
    chain/bendy, found in sugar storage molecules, chain can be broken down as required
  26. Glycosidic Bonds - Beta linkages
    straight chain, found in structural  carbohydrates such as cellulose
  27. oligosaccharide vs polysaccharide
    oligo-multiple but short 2-10 sugars

    poly- 10+ sugars
  28. Chitin
    builds exoskeletons similar to cellulose, links monosaccharides vis beta glycosidic linkages
  29. Nucleotide
    phosphate group, sugar and nitrogenous base
  30. DNA structure and bonds
    double stranded helic made up nucleotides, connected with H bonds.

    deoxyribose sugar in DNA, ribose sugar in RNA
  31. Nitrogenous base pairs
    C-D A-T in RNA there is no T so A-U
  32. Enzymes: General Function
    3D nature effects bonding and increased the rate of reaction

    can either put things together or break them apart

    usually end in -ase, and refer to what they either break apart or put together
  33. Enzymes: four principles
    • lower activation energy
    • do not get used up in reaction
    • do not affect overall change in G (delta G), just change the rate of reaction
    •      G is gibbs free energy
    • do not change equilibrium, only rate equilibrium is reached
  34. Enzyme rate/saturation
    Enzymes do not get used up in reactions, therefore you can only go so fast with x number of enzymes. when all the enzymes are being used the soln is saturated and the rate has reach Vmax, rate can no longer increase
  35. Enzyme Fit: Lock and Key
    Enzymes only work for particular substances/active site
  36. Enzyme Fit: Induced fit
    Enzymes can be flexible and accommodate multiple substances
  37. Enzyme Binding site and Catalytic Site

    Transition state
    Catalytic site- where rxn actually happens

    Binding site- temporary bond and consists of amino acids

    Transition states, substance is neither original or final product
  38. Rate of Rxn is not only influences by concentration of substrate but also
    • temperature
    • pH
  39. Regulation of Enzymes: Feedback Inhibition
    End product of enzyme Rxn works to block original enzyme. I.e. new product can also bind to enzyme active site
  40. Regulation of Enzymes: Competitive Inhibition
    certain molecules compete with substrate for active sites on enzyme 

    can be overcome by adding more substrate, will take longer to reach Vmax because competitor also is binding with enzyme.
  41. Regulation of Enzymes: Irreversible Inhibitors
    Competitive inhibitors that chemical/covalently bond to active site, enzymes permanently inactive. 

    increasing substrate does nothing to rate of rxn
  42. Regulation of Enzymes: Non Competitive Inhibitors
    Act elsewhere on enzyme and change its 3D shape, either to make the enzyme more or less effective, controls enzyme allosterically

    positive allosteric effect increases rate, negative decreases rate
  43. Regulation of Enzymes: Pseudoirreeverible
    have a higher affinity for enzyme sites, very hard to displace but not impossible

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