Chapter 2

Organic Compounds

II. Lipids

Composition: CHO – lipids have less oxygen atoms in proportion to Carbons and Hydrogens.

-less soluble in H2O (hydrophobic)

-have greasy or oily consistency

Types of Lipids:

1. Neutral fats and oils

-most abundant lipids

-consists of glycerol joined to one, two, or three fatty acids

-glycerol is a 3 carbon alcohol with 3 –OH groups

-fatty acid is a straight chain of carbon atoms with carboxyl groups

(-COOH) at one end.

-glycerol and fatty acid(s) are joined by an ester bond between the –OH of glycerol and the –COOH of the fatty acid(s) by way of dehydration.

e.g. glycerol + 1 fatty acid = monoglyceride

glycerol + 2 fatty acids = diglyceride

glycerol + 3 fatty acids = triglyceride

Saturated and Unsaturated fats and oils are triglycerides.

-saturated – contain maximum number of Hydrogen atoms.

(carbons are fully loaded with H)

-tend to be solid at room temperature

-butter, animal fats (lard)

-unsaturated – contains 1 double bond between carbons, therefore, not fully saturated with Hydrogens.

-polyunsaturated - contain more than one double bond.

-both unsaturated and polyunsaturated are oils and most are liquid at room temperature.

Note: trans fatty acids are considered unhealthy. They are found in butter substitutes.

2. Phospholipids

-consists of an organic compound (amino acid), a phosphate group, and a glycerol molecule attached to two fatty acids.

- the head of the phospholipid are the organic compound, phosphate, and the glycerol. It is also polar: (+) and (-) and hydrophilic.

-the tail is the fatty acids and hydrophobic

-the term used to describe a molecule that is both hydrophilic and hydrophobic is amphipathic.

3. Steroids

-carbon atoms arranged in 4 rings: 3 six carbon rings

4 five carbon ring

-steroids are distinguishable by extending side chains.

Types of Steroids:

1. Cholesterol – found only in animal cells and is synthesized in the liver.

- precursor to all steroids

-part of the plasma membrane: 85% synthesized internally

15% dietary

HDL (High Density Lipoproteins) and LDL (Low Density Lipoproteins) are more than just cholesterol.

-consists of cholesterol, fats, phospholipids and proteins

- name refers to ratio of lipids to proteins

e.g. HDL has lower ratio of lipids to proteins

- may prevent cardiovascular disease

-“Good Cholesterol”

LDL has higher ratio of lipids to proteins

-may cause cardiovascular disease

-“Bad Cholesterol”

2. Bile salts – emulsify fats in the intestines

3. Reproductive hormones –estradiol and testosterone

4. Cortisol – metabolic regulator of blood sugar

5. Vitamin D – aids in bone metabolism

6. Eicosanoids – hormone-like chemical signals between cells

Uses for Lipids: energy storage, cellular fuel, structural components of cells, thermal insulation.

III. Proteins

Composition: CHON and usually S

- large complex molecule formed from amino acids

-central importance in the chemistry of life

-proteins are composed of 20 different amino acids

- amino acids are joined by peptide bond (by way of dehydration)

-2 amino acids = dipeptide

-longer chain= polypeptide (10 – 2000+)

All amino acids consist of: amino group -NH2

carboxyl group -COOH

side chain -R (varies from amino acid to amino acid)

Some amino acids are polar.

Levels of Structure of Proteins

-polypeptide chains are twisted and folded to form proteins with a 3-D shape.

-conformation of protein determines functions e.g. unique shape of enzyme permits it to recognize and act on substrates.

4 Levels of Organization

1° Primary – the sequence of amino acids in a polypeptide chain.

e.g. Met-Val-Leu-Val-Trp-Gly

2° Secondary – polypeptide chain coils into alpha helix and beta pleated sheet due to H bonding.

3° Tertiary – overall shape assumed by each polypeptide chain-Protein

3-D structure determined by interactions among side chains.

1. H bonding between amino acids

2. Ionic bonding between side chains

3. Hydrophobic interactions by nonpolar side chains

4. Covalent bonding between cysteins (disulfide bonds)

4° Quaternary – 2 or more polypeptide chains or proteins together.

e.g. hemoglobin exists as four tertiary proteins

Prosthetic Group – a non amino acid component of a protein that is covalently bonded.

-has a specific function

e.g. hemoglobin –has iron ring that binds to oxygen.

glycoprotein – carbohydrate (sugar) is prosthetic group.

Enzymes – proteins that function as a catalyst

– permit biochemical reactions to occur rapidly at normal body temperature.

- they act upon substrates (other substances or molecules)

- suffix –“ase” added to substrate name to distinguish between enzymes.

e.g. amylase (amyle=starch) or carbohydrease

anhydrease (anhydr – without water) removes water

lipase –enzyme that acts on lipids

3 Characteristics of Enzymes: highly specific to substrates

very efficient – speeds up reactions

under cellular control (genes)

Enzymes have active sites – areas that aid in breaking down or forming bonds between two or more substrates.

IV. Nucleic Acids

Composition: CHONP

-transmits hereditary information

-determines protein production

-discovered in nuclei of pus cells

Polymers of Nucleotides (monomers): 5 carbon sugar – ribose

phosphate group

nitrogenous bases:

-purine – double ring structure

-pyrimidine –single ring structure

Nucleotides are covalently bonded between phosphate groups and either ribose or deoxyribose (depending on which nucleic acid) by phosphodiester bond

2 Types of Nucleic Acids

I. RNA (ribonucleic acid)

-functions in protein synthesis

-usually single stranded

-complement to DNA

Bases for RNA: purines- Adenine (A) and Guanine (G)

pyrimidines – Cytosine (C) and Uricil (U)

3 Types of RNA:

1. mRNA (messenger) - transcribes and carries information for making proteins out of the nucleus.

2. tRNA (transfer) – links with specific amino acid and brings it to mRNA.

3. rRNA (ribosmomal) – the site of protein synthesis

-catalyzes reactions; joining of amino acids into proteins.

-consists of 2 subunits (1 large and 1 small).

2. DNA (deoxyribonucleic acid)

- usually double helix

- has purines: A and G

pyrimidines: T and C

- bases are bonded to a phosphate and sugar backbone

-the sequence of bases makes up genes (hereditary material of the cell)

- contains instructions for making all proteins.