Carbon Molecules, Proteins, and DNA

Emphasis: Proteins and DNA

Importance of Carbon
Carbon permeates the world of life—from the energy-requiring activities and structural organization of cells, to physical and chemical conditions that span the globe and influence ecosystems everywhere.

Organic Compounds
Hydrogen and other elements covalently bonded to carbon Carbohydrates Lipids Proteins Nucleic Acids

Carbon’s Bonding Behavior
 Outer shell of carbon

has 4 electrons; can hold 8
 Each carbon atom

can form covalent bonds with up to 4 atoms

Methane: Simplest Organic Compound
H H C H Structural formula H Ball-and-stick model

Space-filling model Figure 3.2 Page 36

Bonding Arrangements
 Carbon atoms can

form chains or rings
 Other atoms project

from the carbon backbone
Glucose (ball-and-stick model)
In-text figure Page 36

Hemoglobin Molecular Models

Ball-and-stick model

Space-filling model

Figure 3.3

Ribbon model

Page 37

Functional Groups
 Atoms or clusters of atoms that are covalently

bonded to carbon backbone
 Give organic compounds their different

properties

Examples of Functional Groups
Methyl group
Hydroxyl group Amino group Carboxyl group Phosphate group Sulfhydryl group

- CH3
- OH - NH3+ - COOH - PO4- SH

Memorize!

Condensation Reactions
 Form polymers from subunits  Enzymes remove -OH from one molecule, H

from another, form bond between two molecules
 Discarded atoms can join to form water

Amino Acid Structure
Amino group Acid

Central carbon

Carboxyl group Amino group R group
Radical

tryptophan (trp)

Protein Synthesis
 Peptide bond

Condensation reaction links amino group of one amino acid with carboxyl group of next

Water forms as a by-product Fig. 3.18a Page 45

Peptide bond forms. Water forms as a by-product.

Another peptide bond forms. Water forms as a by-product.

Another peptide bond forms. Water forms as a by-product.

Another peptide bond forms. Water forms as a by-product. newly forming polypeptide chain

Primary Structure
 Sequence of amino acids
 Unique for each protein  Two linked amino acids = dipeptide  Three or more = polypeptide  Backbone of polypeptide has N atoms:

-N-C-C-N-C-C-N-C-C-N-

Second and Third Levels
 Hydrogen bonding

produces helix or sheet
 Domain formation

Tertiary structure Secondary structure Figure 3.19a Page 46

Fourth Level Structure
Some proteins are
made up of more than one polypeptide chain

Figure 3.20 Page 47

HLA-A2 quaternary structure

Hemoglobin
alpha chain beta chain

beta chain

alpha chain

One Wrong Amino Acid
 Single amino acid change in beta chain can

cause sickle-cell anemia

HbS
valine histidine leucine proline threonine valine glutamate

Fig. 3.21c,d Page 48

Sickle Cell Anemia
 Caused by two mutated copies (HbS) of Hb

gene  Low oxygen causes red blood cells to clump  Clumping prevents normal blood flow  Over time, may damage tissues and organs throughout the body  “The gene defect is a known mutation of a single nucleotide (A to T) of the β-globin gene, which results in glutamic acid being substituted by valine at position 6”.

http://en.wikipedia.org/wiki/Sickle-cell_disease

Nucleotide Structure
 Sugar
 At least one

ATP

phosphate group
 Nitrogen-containing

base

Figure 3.23a Page 50

Nucleotide Functions
 Energy carriers

 Coenzymes
 Chemical messengers

 Building blocks for nucleic

acids

DNA
 Double-stranded  Sugar-phosphate

backbone  Covalent bonds in backbone  H bonds between bases

DNA Structure Video
 http://www.youtube.com/watch?v=qy8dk5iS1f

0

RNA
 Usually single strands
 Four types of nucleotides  Unlike DNA, contains the base uracil in place of

thymine
 Three types are key players in protein synthesis

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