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Tan_Anson_Block4_MM1 (Proteins (Elements (Hydrogen, Oxygen, Nitrogen,…

- - - - Quaternary Structure
        
        Examples: Collagen(Helix) and Hemoglobin(Cluster)
        
        Overall Protein Structure
        
        2+ polypeptide chains
        
        Result of the formation of polypeptides into a cluster or helix
      - Primary Structure
        
        Most simple structure of protein
        
        Composed of 127 Amino Acids
        
        Unique sequence of amino acids
        
        Precise primary structure is determined by inherited genetic information
      - Secondary Structure
        
        Hydrogen Bonding between areas of polypeptide
        
        However, side chains are not involved
        
        Causes folding
        
        beta pleated sheet
        
        alpha helix
      - Tertiary Structure
        
        Reinforced by covalent bonds call Disulfide Bridge
        
        Can exist in one structure with other bonds
        
        formed between to cysteine monomers
        
        amino acids with sulfhydral groups (-SH)
        
        brought together closer during folding
        
        One sulfur bonds to the 2nd
        
        Overall Shape of Polypeptide due to Side Chains
        
        The skeleton of the protein
        
        Hydrogen Bonds: OH with H or polar amino acids
        
        Ionic Bonds: NH3(ammonia) slight positive with slight negative O or slightly charged amino acids
        
        3D
        
        Hydrophobic Interactions and Van der waals Interactions or non polar amino acids
        
        Non polar side chains like to cluster up in the core of structure
  - - - 20 Different Types of Amino Acids
      - Combines with other amino acids to form polypeptides by dehydration reaction
      - Single Organic Compound
      - Contains a Carboxyl group (-COOH) and a amino group (-NH2)
      - Held together by hydrogen bonds
      - Same Base but Side Chains may Differ
        
        Protein Structure differ due to side chains
        
        Causes a specific conformation
        
        Amino Acids are strung together and the bonds fold the protein
        
        Chaperone Proteins use energy from ATP to bind and release polypeptides when folding to make sure it is folded correctly
        
        Chaperone Proteins also assist when proteins undergo refolding after being denatured
  - - - When the folding becomes abnormal
    - - To regulate chemical reactions in body or acts as catalysts
    - - Structure
      - Movement
      - Defense
      - Communication
      - Transportation
      - Storage
- - - - Cellulose
        
        Beta Glucose Monomers
        
        Straight Polymers linked by H-bonds
        
        Plant Cell Wall
        
        Straight Polymers
        
        Unbranched
      - Chitin
        
        arthropod and some fungi cell wall
        
        NAglucoseamine monomers
        
        straight polymers linked by H-bonds
        
        straight polymers
        
        unbranched
        
        hardens when combined with calcium carbonate
      - Peptidoglycan
        
        unbranched
        
        bacteria cell wall
        
        straight polymers
        
        NAglucoseamine monomers with 4 amino acid side chain
        
        straight polymers linked by covalent linked by peptide bonds between amino acid side chains
    - - Plant Starches
        
        Amylopectin
        
        Alpha Glucose Monomers
        
        Helical Polymers
        
        Branched Polymers
        
        Amylose
        
        Alpha Glucose Monomers
        
        Helical Polymers
        
        Unbranched Polymers
      - Animal Glycogen
        
        Branched Polymers
        
        Helical Polymers
        
        Alpha Glucose Monomers
  - - - -Sucrose (fructose-glucose)
      - -Lactose (glucose-galactose)
      - -Maltose (glucose-glucose)
    - - -glucose
      - -fructose
      - -galactose
      - -NAglucosamine(contains nitrogen)
- - - - three fatty acids
      - one glycerol
    - - Four Carbon Rings
      - Connected to various functional groups
    - - Unsaturated
        
        Double Bonds Between Carbons(at least one)
        
        Causes Bents
        
        HydroCarbons
        
        Liquids and Oils
      - Saturated
        
        Single Carbon Bonds
        
        HydroCarbons
        
        Waxes and Solids
    - - polar head(choline and phosphate)
      - two fatty acids
      - one glycerol
  - - - Stores Energy
    - - common component of animal cell membranes
      - precursor to human hormones
    - - Major Components of Cell's Membranes(ie. Salt membrane)
    - - Energy Storage
      - Protects Internal Organs
- - - - Carbon
      - Hydrogen
      - Oxygen
    - - Phosphorous
      - Oxygen
    - - Carbon
      - Nitrogen
      - Hydrogen
      - Oxygen
  - - - Connects to the sugar's carbon 3 and 5
        
        Via Strong Covalent Ester Bonds
      - Part of Nucleic Acids Backbone
      - Oxygens are slightly negative
    - - Deoxyribose in DNA
        
        Only has a hydrogen connected to carbon number 2
      - Pentose: 5 carbons
      - Ribose in RNA
        
        Has a OH connected to carbon number 2
    - - Pyrimidines
        
        Larger that Purines
        
        Thymine(Only in DNA)
        
        Cytosine
        
        Uracil( Only in RNA)
      - Purines
        
        Smaller
        
        Adenine
        
        Guanine
  - - - tRNA
        
        involved in ordering amino acids to make the protein
      - mRNA
        
        conveys genetic information for protein production from nucleus to cytoplasm
        
        Interacts with cell's protein production system
        
        Directs production of a polypeptide
    - - biological code for production of hormones, enzymes, and protein
      - long term storage of information in body
      - Holds genetic information for development and function of body
      - Directs RNA Synthesis