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Published byEdwina Peters Modified over 9 years ago
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Lipids
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A class of molecules that is hydrophobic Hydrophobic= water fearing Ex. Fats Oils Steroids
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Fat Made up of Glycerol and fatty acids Glycerol-3 carbon backbone Fatty acid= long hydrocarbon chain Glycerol Fatty acid
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Saturated Fat Saturated Fat= a fat that has all three fatty acid chains contain the maximum number of hydrogen atoms Only single bonds Found in most animal fat Lard butter
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Saturated Fat
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Unsaturated Fat Unsaturated Fat= A fat that has less than the maximum number of hydrogen's bonded. Some Carbon atoms are double bonded. Corn Oil Olive Oil Vegetable oil
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Unsaturated Fat
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Steroids Steroid= a lipid molecule made up of four fused rings Are lipids because they are hydrophobic Chemical messenger Estrogen Testoterone
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Steroids
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Cholesterol Cholesterol= an essential cell membrane lipid. Starting point of steroids Good and bad uses
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Proteins
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Protein Protein= a polymer made up of amino acids 20 different amino acids Uses Hair Muscles Nutrient storage
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Amino Acids Amino Acid= a monomer made up of a central carbon and four partners Three are the same and one changes to create 20 different amino acids
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Amino Acid Carboxyl (acid) group Amino group
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Building Proteins Proteins are made by connecting amino acids into a chain called a polypeptide Each amino acid is linked by a dehydration reaction Linked between the amino group and carboxyl group
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Building a Protein Amino acid Dipeptide Amino acid Peptide bond Dehydration reaction Amino group Carboxyl group
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Protein Shape A protein consists of one or more polypeptide precisely folded into a unique shape The shape is influenced by the environment Temperature and pH change will change the shape of a protein = denaturation
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Protein Shape Levels of Protein Structure Amino acids Basic structure of protein is a long chain of amino acids.
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Secondary Shape Secondary Shape folds the amino acid chain into two shapes Alpha Helix Beta Pleated Sheet
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Secondary Shape Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet
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Tertiary Shape Brings multiple polypeptides together and continues to fold them
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LE 3-14c Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin)
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Quaternary Shape Multiple polypeptides are folded together into a useable shape held together by hydrogen bonds
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LE 3-14d Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin) Transthyretin, with four identical polypeptide subunits
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Enzymes
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Catalyst A compound that speeds up chemical reactions
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Enzymes A biological catalyst A specialized protein that lowers the activation energy of chemical reactions
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Activation Energy Amount of energy needed to start a chemical reaction
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Reactants Net change in energy E A without enzyme Products Progress of the reaction Energy E A with enzyme
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Substrate Enzyme Active site Normal binding of substrate Enzyme
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LE 5-6 Enzyme available with empty active site Active site Glucose Fructose Products are released Enzyme (sucrase) Substrate (sucrose) H2OH2O Substrate is converted to products Substrate binds to enzyme with induced fit
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b. a. f. c. d. e.
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