Cell Biology - Ch. 3

Front 1

4 components of Major Macromolecules

Back 1

- Chemical nature of monomers

- Synthesis of polymers

- Properties of polymers

- Functions

Front 2

Protein: Monofunctional

Back 2

When a protein has a specific function.

Front 3

Protein: Bifunctional

Back 3

When a protein has two distinctly different roles.

Front 4

Protein Type: Enzymes

Back 4

Fx: Selective Catalysis

(i.e. Digestive Enzyme)

Front 5

Protein Type: Structural

Back 5

Fx: Support Cellular Structures

(i.e. Collagen and Elastin)

Front 6

Protein Type: Motility

Back 6

Fx: Cell and parts movement

(i.e. Actin and Myosin)

Front 7

Protein Type: Regulatory

Back 7

Fx: Cellular Function

(i.e. Transcription factors DNABP)

Front 8

Protein Type: Transport

Back 8

Fx: Substance in and out

(i.e. trans membrane for small molecules)

Front 9

Protein Type: Hormonal

Back 9

Fx: Hormones

(i.e. Insulin, GH)

Front 10

Protein Type: Defensive

Back 10

Fx: Against Disease

(i.e. Antibodies)

Front 11

Protein Type: Storage

Back 11

Fx: Storage and release of AA

(i.e. in seed broken down for AA requirement)

Front 12

Monomer

Back 12

A monomer is another term used to classify an Amino Acid (AA).

Front 13

Are there proteins that share identical AA sequences with proteins.

Back 13

NO. No two proteins share identical AA sequences.

Front 14

30 most common small molecules in cells.

Back 14

20 - Amino Acids

5 - Aromatic Bases (purines and pyrimidines)

2 - Sugars (ribose and glucose)

3 - Lipids (choline, glycerol, palmitate)

Front 15

20 Amino Acids

Back 15

Front 16

5 Aromatic Bases

Back 16

PURINES

- Adenine

- Guanine

PYRIMIDINES

- Cytosine

- Thymine

- Uracil

Components on nucleic acids (DNA and RNA)

Front 17

2 Sugars (monosaccharides)

Back 17

Ribose - component of nucleic acids.

Glucose - energy metabolism; component of starch and glycogen.

Front 18

3 Lipids

Back 18

Choline

Glycerol

Palmitate

- Components of phospholipids

Front 19

20 Amino Acids - 9 Non-Polar

Back 19

Front 20

20 Amino Acids - 6 polar uncharged amino acids (hydrophillic)

Back 20

Front 21

20 Amino Acids - 5 polar, charged amino acids

Back 21

Front 22

Addition reactions between Amino Acids...

Back 22

Are known as Dehydration/Condensation reactions. Resulting in the formation of water and the formation of a Peptide/Amide bond.

Front 23

Steps of Amino Acid addition reactions...

Back 23

- Condensation/Dehydration reaction.

- Formation of Peptide/Amide bond.

- Directional continuation; either at N Terminus (Amino Group) and the C Terminus (Carboxyl Group)

Front 24

Requirements of Polypeptide Synthesis

Back 24

Information and Energy

- Energy needed for incoming Amino Acid

- Amino Acid linked to transfer RNA or tRNA

- messenger or mRNA is used as template

Front 25

Two Amino Acid chain

Back 25

Dipeptide

Front 26

Three Amino Acid chain

Back 26

Tripeptide

Front 27

Several Amino Acid chain

Back 27

Polypeptide

Front 28

Monomeric Proteins

Back 28

Single peptide which achieve a shape from spontaneous folding and coiling.

Front 29

Multimeric Proteins

Back 29

Two or more polypeptides

Front 30

Multimeric - Homomeric

Back 30

Identical polypeptides

Front 31

Multimeric - Heteromeric

Back 31

Two or more different polypeptides.

Front 32

How many polypeptides in Hemoglobin?

Back 32

Hemoglobin contains four polypeptides.

Front 33

What are the four subunits of Hemoglobin?

Back 33

2 - alpha globulin subunits

2 - beta globulin subunits

Front 34

Why do proteins have conformations?

Back 34

Proteins fold into a proper shape or Conformation to accomplish their biological goals.

Front 35

Conformation depends on what kind of bonds?

Back 35

Covalent Disulfid bonds

&

Non-covalent bonds

Front 36

Conformation: Disulfide Covalent Bonds

Back 36

Intramolecular Disulfide Bonds - between Cysteine residues of the same protein stabilize the conformation of polypeptide.

Front 37

Confirmation: Non-covalent Bonds

Back 37

Hydrogen Bonds

Ionic Bonds

Van der Waals Interactions

Hydrophobic Interactions

Front 38

Non-covalent Bonds: Hydrogen Bonds

Back 38

Stabilizes helical and sheet structures.

R- Groups in amino acids can act as H donor or acceptors. This allows H bonds tho form at safe distances with AA.

Carbonyl and Sulfhydryl are good acceptors. And, OH groups are good donors.

Individual H bonds are weak but many together can stabilize biopolymers.

Front 39

9 Nons (20 AA)

Back 39

Gly - Ala - Val - Leu- Ile

Met - Phe - Trp - Pro

Front 40

6 Neuts (20 AA)

Back 40

Ser - Thr - Cys - Tyr - Asn - Gln

Front 41

5 Poles (20 AA)

Back 41

Asp - Glu

Lys - Arg - His

Front 42

Non-covalent Bonds: Ionic Bonds

Back 42

R-Grpups are (+) or (-) charged.

Ionic bons are nondirectional - meaning they are not limited to discrete angles.

Loss of ionic bonds account for the denaturation of protein which are subjected to unfavorable pH.

Front 43

Non-covalent Bonds: Vaan der Wals

Back 43

Molecules with non-polar covalent bonds that contain transient negative and positive charged regions.

Electrons are unevenly and asymmetriclly distributed.

Transient attraction between two nonpolar molecules. This requires close proximity.

Table for the binding of molecules with complementary surfaces.

Front 44

Non-covalent Bonds: Hydrophobic

Back 44

Not a bond or interaction.

A term used to explain the tendency of a molecule or parts of a molecule to avoid reacting with water.

Front 45

Stability of protein structure/folding

Back 45

1. Covalent Disulfide bonds.

2. Hydrogen bonds between r- groups.

3. Iconic bonds - between charged amino acids.

4. Transient Vaan der Wals forces - nonpolar molecules.

5. Hydrophobic interactions with non-polar groups in the interior.

Front 46

4 Levels of Protein Structure

Back 46

1. Primary

2. Secondary

3. Tertiary

4. Quaternary

Front 47

The 2 Protein Categories

Back 47

1. Fibrous Proteins (small number)

2. Globular Proteins

Front 48

Fibrous Proteins (small number)

Back 48

- Fibroin

- Keratins

- Collagen

- Elastin

Front 49

Globular Proteins

Back 49

Most proteins in cellular structure and function.

Front 50

Path of Genetic Information

Back 50

1 - mRNA forms inside nucleus.

2 - mRNA leaves nucleus via nuclear pores.

3 - mRNA sticks to ribosome, initiating protein formation.

Front 51

Nucleic Acid Synthesis

Back 51

Requires energy from nucleotides and information via the DNA template.

Hydrogen bonds form between the carbonyl groups and nitrogen atoms of purines and pyrimidines bases.

Front 52

Polysaccharides (Part 1)

Back 52

Sugar and sugar derivative polymers.

Repeating Unit - six carbon sugar glucose.

Single or Two kinds of alternating patterns.

Not an informational polymer.

Structural and energy polymers.

Storage - Starch and Glycogen.

Shorter Polymers - Oligosaccharides - attached to proteins on cell surface.

Front 53

Polysaccharides (Part 2)

Back 53

Play roles - signaling by recognizing extras signaling molecules.

Six carbon sugar glucose is single repeating unit.

Differ in nature of the bond and branch chains.

Front 54

Polysaccharides (Part 3)

Back 54

Monomers - Monosaccharides

- Sugar

Aldehyde or Ketone

- Aldosugar with Terminal carbonyl group.

- Ketosugar with internal carbonyl.

Front 55

Structure of Monosaccharides (Monomers)

Back 55

Front 56

Disaccharides

Back 56

Two monomeric saccharides linked covalently.

- Maltose (Two glucose units)

- Lactose (Glucose linked to Galactose)

- Sucrose (Glucose linked to Fructose)

Disaccharides formed by condensation and by Glycosidic bond.

Front 57

How are sugars named?

Back 57

Sugars are named based on number of carbon atoms

Three Carbon - Triose

Four Carbon - Tetrose

Five Carbon - Pentose

Six Carbon - Hexose

Front 58

The Two ring forms of D-Glucose

Back 58

Alpha and Beta glucose.

Alpha can be broken down by humans.

Beta can only be broken down by bacteria.

Front 59

Common Disaccharides

Back 59

Front 60

Polysaccharides (Part 4)

Back 60

Structural and Storage

Starch - Storage in plant cells.

Glycogen - storage in animal cells.

These polymers consist of Glucose units lined together by Glycosidic bonds.

Front 61

Glycogen

Back 61

Storage polysaccharide in animal cells.

- Alpha linkage

- consists of Glucose units lined together by Glycosidic bonds.

- highly branched with linkages at every 8 to 10 glucose units to provide side chains roughly 8 to 12 glucose units long.

Front 62

Starch

Back 62

Alpha linkage

Branched - Amylose (10-30%)

Unbranched - Amylopectin (70-90%)

Branches every 12 to 25 glucose units. With long side chains, 20 to 25 glucose units long.

More than half the carbon in plants is Cellulose.

Front 63

Lipids

Back 63

• Heterogenous molecules - functionally and chemically diverse.

• NOT formed by stepwise processes.

• Resemblance by property of solubility.

• HYDROPHOBIC

• Soluble in nonpolar solvents - chloroform or ether.

• Some are Amphipathic - containing polar and nonpolar regions.

Front 64

Lipid Functions

Back 64

Energy Storage.

Membrane Structure.

Special Function.

Front 65

Lipids - Six Main Classes

Back 65

1. Fatty Acids

2. Triacylglycerols

3. Phospholipids

4. Glycolipids

5. Steroids

6. Terpenes

Front 66

Fatty Acids

Back 66

• Building blocks: long unbranched hydrocarbon chains with carboxy group at the end.

• Amphipathic - head polar and tall nonpolar.

• Number of carbon atoms vary.

• Yield energy upon oxidation.

• Saturated (No double bonds) vs Unsaturated (Double bonds present)

Front 67

Triacylglycerols

Back 67

Commonly known as Triglycerides: storage Lipids that provide energy and insulation.

Glycerol molecule with three fatty acids by ester bonds.

Front 68

Triacylglycerol - Sat. vs Unsat.

Back 68

Saturated fatty acids with triacylglycerols, semisolid at room temperature.

Unsaturated fatty acids with triacylglycerol, mostly liquid at room temp.

Front 69

Phospholipids

Back 69

Fatty acids esterfied into glycerol molecules.

Phosphatidic Acid - basic component

Amphipathic Nature - highly polar heads and two nonpolar heads.

Sphingolilids - amine alcohol sphingosine.

Ceramides - polar region flanked by two long nonpolar tails.

Front 70

Ceramides

Back 70

Polar region flanked by two long nonpolar heads

Front 71

Phospholipids - Self Organization

Back 71

Front 72

Structures of common Phosphoglycerides (Part 1)

Back 72

Phosphatidic Acid (+) R-Group

Front 73

Structures of Common Phosphoglycerides (Part 2) - Phospatidic Acid

Back 73

Front 74

Structures of Common Phosphoglycerides (Part 3) - Common R-Groups

Back 74

Serine, Ethanolamine, Choline, Inositol.

Front 75

Glycolipids - General Structure

Back 75

Front 76

Glycolipids (Part 1)

Back 76

Derivatives of sphingolipids

Glycosphingolipids

Carbohydrate attached to a sugar unit.

Carbohydrate group - one to six sugar unit, D-Glucose, D-Galactose, N-acetyl-D-galactosamine.

Front 77

Glycolipids (Part 2)

Back 77

Found in some membranes - certain plant cells and nervous system.

Front 78

Steroids (Part 1)

Back 78

Four ringed hydrocarbon

Cholesterol

Amphipathic

- OH group at the 3rd position - polar

Four rings and hydrocarbon - nonpolar

Found only in membranes.

Front 79

Steroids (Part 2)

Back 79

Steroid hormones – glucocorticoids and mineralocorticoids, Estrogens (estradiol), androgens (Testosterone).

Stigmasterol, sitosterols – Plants

Ergosterol – Fungus

Front 80

Common Steroid Hormones

Back 80

Front 81

Terpenes

Back 81

Formed from five carbon compound isoprene.

- Isoprenoids

Polyisoprenoids - found in Archea cell membrane.

Involved in activating sugar derivative and electron carriers Coenzyme Q and Plastoquinone.

Products are Vitamin A1, Cartinoids, and Dolichols, etc.

Front 82

Common Structural Motifs - β-α-β

Back 82

The α- helix is represented by blue a blue coil (left) or a blue cylinder (right).