Macromolecules

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Author:
hellosleepy
ID:
158817
Filename:
Macromolecules
Updated:
2012-07-18 13:24:22
Tags:
MCAT
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Description:
MCAT Biology
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  1. Fatty Acid 

    Long carbon chains with COOH end 
  2. Saturated Fatty Acids vs. Unsaturated Fatty Acids 
    Saturated = SINGLE double C=C bond

    Unsaturated = One or more C=C bonds
  3. Triglycerides

    • 3C Glycerol backbone + 3 fatty acids chains attached
    • Important energy storage molecule 
  4. Phospholipid

    3C Glycerol backbone + 2 fatty acid chains + 1 phosphate group

    Amphipathic
  5. Steroids
    • Type of lipid that regulates metabolic activities
    • Include: hormones, cholesterol, Vit D
  6. Eicosanoids
    • Type of lipid
    • Include: Prostaglandins, leukotrienes
  7. How are lipids transported in the blood stream? 
    • Via lipoproteins & Albumin 
    • Classification: VLDL(bad) --- HDL (good) 
  8. Bonds found in proteins 
    Peptide bonds
  9. Bonds found in carbohydrates
    Glycosidic bonds 
  10. Bonds found in nucleis acids 
    Phosphodiester bonds 
  11. Basic amino acids 
    • Histidine 
    • Lysine
    • Arginine  
  12. Acidic amino acids 
    • Aspartic acid/Aspartate 
    • Glutamic Acid/Glutamate 
  13. Polar amino acids 
    • Serine 
    • Threonine
    • Cysteine (forms covalent disulfide bonds)
    • Tyrosine
    • Asparagine
    • Glutamine 
  14. Nonpolar amino acids - I saw Lucy methodically probe and feel Alan, then Val tripped glycine
    • Glycine
    • Alanine
    • Valine
    • Laucine
    • Isoleucine
    • Phenylalanine
    • Tryptophan
    • Methionine (start amino acid)
    • Proline (turn-inducing & affects tertiary structure)
  15. How many amino acids are there and of those how many are essential? 
    20 amino acids total -- 10 of which are essential. 
  16. Amino acid structure 
  17. Forces creating tertiary structure
    • 1. Disulfide bonds 
    • 2. Ionic interactions between side chains
    • 3. H-bonding
    • 4. Van der Waals
    • 5. Hydrophobic side chains being pushed away from protein center
  18. Globular proteins
    • Enzymes
    • Hormones
    • Membrane pumps
    • Channels
    • Tubulin - which polymerized to form MTs in flagella & cilia
  19. Structural proteins
    • Maintain and strengthen cellular matrix 
    • Collagen  
  20. Describe the two anomeric forms of glucose
     
    1. Alpha-glucose: anomeric carbon and methoxy carbon are on opposite ends of the ring 

     2. Beta-glucose: anomeric and methoxy carbons are on same side of the ring 
  21. Types of glucose linkages 
    1. Alpha: Digested by animals - starch & glycogen 

    2. Beta: Digested by bacteria - cellulose (bacteria break beta linkages)
  22. Where are the largest amounts of glucose found?
    The mucles and liver
  23. How is glucose absorbed into most cells?
    • 1. Mostly via facilitated diffusion
    • 2. Or by secondary active transport fown the [Na+] gradient
  24. What kind of cells can absorb glucose in the absence of insulin?
    Neurons and hepatic cells
  25. Components of a nucleotide 
    • 1. 5C pentose sugar 
    • 2. Nitrogenous base
    • 3. Phosphate group 
  26. How many H-bonds are formed between the nitrogenous bases?
    • A&T form 2 H-bonds 
    • C&G form 3 H-bonds 
  27. Directionality in which a nucleic acid is written and read?
    5'--->3' (leading strand)
  28. What is ATP? 
    What about NADH?
    What about Mg2+?
    • ATP is a nucleotide 
    • NADH is a coenzyme
    • Mg+ is a cofactor (assist in enzyme fxn, minerals)
  29. Non-competitive enzymatic inhibition 
    • Binds to somewhere other than active site 
    • Does NOT change enzyme-substrate affinity
    •  Decreases reaction rate 
  30. Competitive enzymatic inhibition 
    • Binds to the active site and thus, decreases enzyme-substrate affinity 
    • Does not change reaction rate
    • Can be overcome by adding more substrate  
  31. Irreversible enzymatic inhibition 
    Covalently binds to enzymes 
  32. Types of enzymatic regulation (4)
    • 1. Proteolytic cleavage (zymogen-->active enzyme)
    • 2. Covalent modification (phosphorylation)
    • 3. Protein subunit regulation (GPCRs)
    • 4. Allosteric modulation (positive cooperativity)
    • **Allosteric modulation results in a conformational change 
  33. Kinases vs. Phosphatases
    • Kinases phosphorylate & usually deactivate 
    • Phosphatases dephosphorylate
  34. Importance of cofactors?
    Not all enzymes need cofactors 

    They are metal ions  that activate an exzyme by binding to it
  35. Coenzymes?
    They help out enzyme catalyzed reaction by carrying/delivering electrons and being oxidized or reduced 

    Include: NADH, FADH2 etc. 

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