Organic Nutrients: The Building Blocks of Life 1. Carbohydrates 2.Lipids 3.Proteins 4.Nucleic Acids.

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Organic Nutrients: The Building Blocks of Life 1. Carbohydrates 2.Lipids 3.Proteins 4.Nucleic Acids

Protein A. Monomer: Amino Acids B. Polymer: Polypeptides (amino acids linked by peptide bonds) Nucleic Acid Atoms Names Structure Examples Functions Carbon Hydrogen Oxygen Nitrogen Sulfur Nutrient End in: “in” pepsin “gen” collagen “ase” lipase Long chains of amino acids Structural 1. Collagen 2. Keratin Globular 1. Enzymes 2. Transport 3. Hormones 4. Actin/Myosin 5. Antibodies 6. Gene Regulatory Cell Parts 1. Cytoskeleton 2. Connective tissue 1. Chemical Rx 2. Transports 3. Signals 4. Movement 5. Defense 6. Activate DNA Same as above End in “ine” example: glycine leucine 20 different types Amine (NH2) + Carboxyl Acid (COOH) + “R” group Glycine Leucine Proline Histidine (20) Building blocks of proteins Same as above Primary ---> Secondary-> Tertiary ----> Quaternary  Amino acid chain + H bonds interactions + R group interactions + Many chains bond together Forms a-helices & pleated sheets Shapes proteins into active form (Native Structure) C, O, H, N, P Genes Chromosomes Monomers: Nucleotides Polymer: DNA RNA Carries genetic information (how to make proteins) Protein and life Summary

OR IS IT? Let’s take a new, ‘fresh’ perspective on food

Secondary Protein Structure Slide 2

Quaternary Structure 3 intertwining chains Collagen 2 Alpha Chains & 2 Beta Chains Hemoglobin Slide 2

Nucleotide Monomers for DNA Polymer

“R” Group Interactions Slide 2 Tertiary R Group Interactions

Slide 2 Denatured Protein Denaturing Conditions 1.pH changes 2.Temperature 3.Water Concentration 4.Salinity (All of the above interfere with H bonds and ionic interactions) The 4 Levels of Protein Structure Protein unravels and loses its native shape, thereby becoming biologically inactivePrimary Secondary Tertiary Quaternary Folding can be “autocatalytic” or helped by local environmentslocal environments

Protein Unfolding: Denaturation 1.pH changes * 2.Temperature * 3.Water Concentration * *Note: Condition will interfere with H bonds, Ionic and Hydrophilic interaction The covalent peptide bonds stay intact Slide 9

Amino Acid Structure Slide 2

Globular Protein Structural ProteinCollagen Slide 2

An Amino Acid Sequence Becomes a 3 Dimensional Shape Protein Folding:

Chaperonins Aid in Proper Protein Folding How a chaperonin opens and closesSlide 9

Slide 2