Lipids. A class of molecules that is hydrophobic Hydrophobic= water fearing Ex. Fats Oils ...
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Transcript of Lipids. A class of molecules that is hydrophobic Hydrophobic= water fearing Ex. Fats Oils ...
Lipids
Lipids
A class of molecules that is hydrophobic
Hydrophobic= water fearing Ex.
Fats Oils Steroids
Fat
Made up of Glycerol and fatty acids
Glycerol-3 carbon backbone
Fatty acid= long hydrocarbon chain
Glycerol
Fatty acid
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
Saturated Fat
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
Unsaturated Fat
Steroids
Steroid= a lipid molecule made up of four fused rings
Are lipids because they are hydrophobic
Chemical messenger Estrogen Testoterone
Steroids
Cholesterol
Cholesterol= an essential cell membrane lipid.
Starting point of steroids Good and bad uses
Proteins
Protein
Protein= a polymer made up of amino acids
20 different amino acids Uses
Hair Muscles Nutrient storage
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
Amino Acid
Carboxyl (acid)group
Aminogroup
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
Building a Protein
Amino acid DipeptideAmino acid
Peptidebond
Dehydrationreaction
Aminogroup
Carboxylgroup
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
Protein Shape
Levels of Protein Structure
Amino acids
Basic structure of protein is a long chain of amino acids.
Secondary Shape
Secondary Shape folds the amino acid chain into two shapes Alpha Helix Beta Pleated Sheet
Secondary ShapeLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
Tertiary Shape
Brings multiple polypeptides together and continues to fold them
LE 3-14cLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
Polypeptide(single subunitof transthyretin)
Quaternary Shape
Multiple polypeptides are folded together into a useable shape held together by hydrogen bonds
LE 3-14dLevels of Protein Structure
Amino acids
Hydrogenbond
Alpha helix Pleated sheet
Polypeptide(single subunitof transthyretin)
Transthyretin, withfour identicalpolypeptide subunits
Enzymes
Catalyst
A compound that speeds up chemical reactions
Enzymes
A biological catalyst A specialized protein that lowers the
activation energy of chemical reactions
Activation Energy
Amount of energy needed to start a chemical reaction
Reactants
Netchangein energy
EA withoutenzyme
Products
Progress of the reaction
En
erg
y
EA withenzyme
Substrate
Enzyme
Active site
Normal binding of substrate
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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