Ch. 3b Macromolecules F17

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Ch. 3b Warm-Up

1.

1. What are the 4 classes of

_{What are the 4 classes of}

macromolecules?

2.

2. Give an example of each

Give an example of each

type of macromolecule.

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Ch. 3b Warm-Up

1.

1. What are the 4 classes of What are the 4 classes of

macromolecules? Give an example of macromolecules? Give an example of

each. each. 2.

2. Draw and label the parts of an amino acid.Draw and label the parts of an amino acid. 3.

3. How are 2 amino acids put together? How are 2 amino acids put together? Name the process and describe what Name the process and describe what

happens. happens. 4.

4. Draw a tripeptide. (Use Google for help) Draw a tripeptide. (Use Google for help) Label the

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Peptide Bonds

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Ch. 3b Warm-Up Activity

In your family groups,

complete #1-5 on Activity

4/5.1:

“

How can you identify

organic macromolecules?

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Ch. 3b Warm-Up

1.

1. What are the 4 levels of protein What are the 4 levels of protein

structure? What bonds are formed

in each level?

2.

2. Which protein was involved in the Which protein was involved in the curds & whey lab yesterday?

curds & whey lab yesterday?

3.

3. Explain what happened to the milk Explain what happened to the milk to form the curds and whey.

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Ch. 3b: The Structure

and Function of

Macromolecules

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You Must Know

• The role of _{The role of}dehydration synthesis_{dehydration synthesis} in the in the formation of organic compounds and

formation of organic compounds and

hydrolysis

hydrolysis in the digestion of organic in the digestion of organic compounds.

compounds.

• How the sequence and subcomponents of _{How the sequence and subcomponents of}

the four groups of organic compounds

determine their properties.

• The cellular functions of carbs, lipids, _{The cellular functions of carbs, lipids,}

proteins, and nucleic acids.

• _{How changes in these organic molecules}_{How changes in these organic molecules}

would affect their function.

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You Must Know

• The 4 structural levels of proteins and how _{The 4 structural levels of proteins and how}

changes at any levels can affect the activity of

the protein.

• How proteins reach their final shape _{How proteins reach their final shape}

(

(conformation_conformation), the ), the denaturing_denaturing impact that impact that heat and pH can have on protein structure,

heat and pH can have on protein structure,

and how these changes may affect the

organism.

• Directionality influences structure and _{Directionality influences structure and}

function of polymers, such as nucleic acids (5’

and 3’ ends) and proteins (amino and carboxyl

ends).

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Monomers Polymers Macromolec_ules •Small organic

•Used for building blocks of polymers •Connects with condensation reaction (dehydration synthesis) •Long molecules of monomers •With many identical or similar blocks

linked by covalent bonds

•Giant molecules •2 or more

polymers bonded together

ie. amino acid  peptide  polypeptide

 protein

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Dehydration Synthesis

(Condensation Reaction)

Hydrolysis

Make polymers Breakdown polymers Monomers  Polymers Polymers  Monomers

A + B



AB



A + B

+ H₂O

+ +

H₂O

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Dehydration Synthesis

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Hydrolysis

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Proteomics

: Analysis of

_{: Analysis of}

proteins and sequences

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I. Proteins

• _“

_“

_{Proteios” = first or primary}

• _{50% dry weight of cells}

_{50% dry weight of cells}

• _{Contains: C, H, O, N, S}

_{Contains: C, H, O, N, S}

Myoglobin protein

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Protein Functions (+

examples)

• _{Enzymes (lactase)}_{Enzymes (lactase)}

• _{Defense (antibodies)}_{Defense (antibodies)}

• _{Storage (milk protein = casein)}_{Storage (milk protein = casein)} • _{Transport (hemoglobin)}_{Transport (hemoglobin)}

• _{Hormones (insulin)}_{Hormones (insulin)} • _Receptors_Receptors

• _{Movement (motor proteins)}_{Movement (motor proteins)} • _{Structure (keratin)}_{Structure (keratin)}

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Overview of protein

functions

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Overview of protein

functions

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Four Levels of Protein

Structure

1.

1. Primary_Primary

 Amino acid Amino acid (AA) sequence(AA) sequence  20 different AA’s20 different AA’s

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Amino Acid

• _{R group}_{R group}= side _{= side} chains

chains

• Properties_Properties::

• hydrophobichydrophobic • hydrophilichydrophilic

• ionic (acids & ionic (acids & bases)

bases)

• “_“amino” : -NHamino” : -NH2₂ • _“_“_{acid” : -COOH}_{acid” : -COOH}

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Four Levels of Protein Structure

(continued)

2.

2. SecondarySecondary

 Gains 3-D shape (folds, coils) by Gains 3-D shape (folds, coils) by H-

H-bonding bonding

 Alpha (α) helixAlpha (α) helix, , Beta (Beta (ββ) pleated ) pleated

sheet sheet

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Basic Principles of Protein

Folding

A.

A. Hydrophobic AA buried in interior Hydrophobic AA buried in interior of protein (hydrophobic

of protein (hydrophobic

interactions)

B.

B. Hydrophilic AA exposed on surface Hydrophilic AA exposed on surface of protein (hydrogen bonds)

of protein (hydrogen bonds)

C.

C. Acidic + Basic AA form salt bridges Acidic + Basic AA form salt bridges (ionic bonds).

(ionic bonds).

D.

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(continued)

3.

3. TertiaryTertiary

 Bonding between Bonding between side chainsside chains (R groups) (R groups) of of

amino acids amino acids

 H bonds, ionic bonds, disulfide bridges, H bonds, ionic bonds, disulfide bridges,

hydrophobic interactions, van der Waals hydrophobic interactions, van der Waals

interactions interactions

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(continued)

4.

4. QuaternaryQuaternary

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amino acids

amino acids  polypeptides polypeptides 

protein

Bonding (ionic & H) can create asymmetrical attractions

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Chaperonins

assist in proper

_{assist in proper}

folding of proteins

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• _Protein_Protein_{structure and function}_{structure and function} are sensitive to chemical and

are sensitive to chemical and

physical conditions

• _{Unfolds or}_{Unfolds or}_denatures_denatures_if_if_pH_pH_and_and

temperature

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change in

structure

_structure

= change

_{= change}

in

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X-ray

crystallography

used to determine

the 3-D structure

of proteins

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Genomics

: Analysis of

_{: Analysis of}

genes and genomes

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II. Nucleic Acids

Function: store hereditary info

DNA RNA

• Double-stranded helix

• N-bases: A, G, C, Thymine

Thymine

• Stores hereditary info

• Longer/larger

• Sugar: deoxyribose

• Single-stranded • N-bases: A, G, C,

Uracil

• Carry info from DNA to ribosomes • tRNA, rRNA,

mRNA, RNAi • Sugar: ribose

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Nucleotides

: monomer of

DNA/RNA

Nucleotide

Nucleotide = = SugarSugar + + PhosphatePhosphate + +

Nitrogen Base

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Nucleotide

phospha te 5-C sugar Nitrogen base

A – T G – C

Purines Pyrimidine s •Adenine •Guanine •Cytosine •Thymine (DNA) •Uracil (RNA)

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Information flow in a cell:

DNA

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III. Carbohydrates

• _Fuel_Fuel and _andbuilding material_{building material}

• Include simple sugars (fructose) and polymers _{Include simple sugars (fructose) and polymers} (starch)

(starch)

• Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH_{Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH}22OO

• monosaccharide_{monosaccharide}  disaccharide_disaccharide  polysaccharide_{polysaccharide}

• Monosaccharides_{Monosaccharides} = monomers (eg. glucose, = monomers (eg. glucose, ribose)

ribose)

• Polysaccharides_{Polysaccharides}::

 _Storage_Storage_{(plants-starch, animals-glycogen)}_{(plants-starch, animals-glycogen)}  _Structure_Structure_{(plant-cellulose, arthropod-chitin}_{(plant-cellulose, arthropod-chitin})₎

Differ in position & orientation of glycosidic linkage

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The The structure structure and and classification classification of some of some monosaccha monosaccha rides rides

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Linear and ring forms of

glucose

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Carbohydrate synthesis

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Cellulose vs. Starch

Two Forms of Glucose:

Two Forms of Glucose:  glucose & glucose &  glucose

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Cellulose vs. Starch

• _{Starch =}_{Starch =}___{glucose monomers}_{glucose monomers}

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Storage polysaccharides of

Storage polysaccharides of plantsplants ( (starchstarch) and ) and animals

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Structural polysaccharides: cellulose & chitin

(exoskeleton)

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IV. Lipids

A.

A. Fats (triglyceride): Fats (triglyceride): store energy

 Glycerol + 3 Fatty Acids  saturated, unsaturated,

polyunsaturated

B.

B. Steroids: _Steroids cholesterol and hormones

C.

C. Phospholipids: Phospholipids: lipid bilayer of _{lipid bilayer of} cell membrane

 hydrophilic head, hydrophobic

tails Hydrophilic _head

Hydrophobic tail

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Saturated Unsaturated Polyunsatura_ted

“saturated” with H Have some C=C, result in kinks

In animals In plants

Solid at room

temp. Liquid at room temp.

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The structure of a

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Hydrophobic/hydrophilic interactions make a

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