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

b.

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f.

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