lipids. a class of molecules that is hydrophobic hydrophobic= water fearing ex. fats oils ...
TRANSCRIPT
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Lipids
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Lipids
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
Aminogroup
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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 DipeptideAmino acid
Peptidebond
Dehydrationreaction
Aminogroup
Carboxylgroup
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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 ShapeLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
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Tertiary Shape
Brings multiple polypeptides together and continues to fold them
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LE 3-14cLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
Polypeptide(single subunitof 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 3-14dLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
Polypeptide(single subunitof transthyretin)
Transthyretin, withfour identicalpolypeptide 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
Netchangein energy
EA withoutenzyme
Products
Progress of the reaction
En
erg
y
EA withenzyme
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Substrate
Enzyme
Active site
Normal binding of substrate
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LE 5-6
Enzyme availablewith empty activesite
Active site
Glucose
Fructose
Products arereleased
Enzyme(sucrase)
Substrate(sucrose)
H2O
Substrate isconverted toproducts
Substrate bindsto enzyme withinduced fit
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