The Molecules Of Life Flashcards

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1
Q

What is a organic molecule?

A

Are carbon bases molecules. (Molecules that have a carbon atom present). And these carbon based compounds make up who we are.

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2
Q

What is organic chemistry?

A

Is the study of carbon compounds.

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3
Q

What are the bonding patterns of carbon?

A

It has four valence electrons. (Becomes stable through covalent bonding. Sharing electrons)
The bonds are arranged in a triangular pyramid(tetrahedron).
Are the backbone of biological molecules because they can form long chains or rings.
When carbons bond with a hydrogen they form compounds called hydrocarbons. Non polar compounds eg. Waxes oil.

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4
Q

What are carbohydrates /saccharides?

A

Are sugars and starches, they are used for energy production, storage and for structural reinforcement. It is the most abundant molecule in the world.

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5
Q

What are you two simple sugars/ carbohydrates

A

Monosaccharides- are monomers (single units of sugar. And provide immediate energy. Eg: gylceraldehyde, ribose, deoxyribose, fructose and glucose.
Note: ribose and deoxyribose are parts of RNA and DNA respectively and are five carbon sugars.

Disaccharides - when two simple sugars (two monosaccharides) joins together. And are formed through a condensation reaction(removal of water to form bond).
Eg. Maltose, sucrose and lactose
Note: most of the sweet things we eat are disaccharides.

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6
Q

What are complex carbohydrates?

A

Polysaccharides are complex carbohydrates (they are made up of more than 10 monosaccharides linked together.
They are all polymers of glucose

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7
Q

Give an example of a polysaccharide that is used for structure?

A

Cellulose are found in plant cell walls and this is what gives them structure.
Chitin - covers insects and crustaceans.
We do not have the enzymes needed to digest these polymers, however some animals (cows and termites) have bacteria in their guts that are able to digest cellulose.

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8
Q

Examples of carbohydrates that are used for food.

A

Starches (plants ) - animals have the enzymes needed to digest this.

Glycogen(animas) - is stored in our livers and muscles as a rest source of glucose.

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9
Q

What are lipids

A

Are non polar (hydrophobic) complement of cells. And a mostly carbon and hydrogen.
They are primarily used for energy storage and as structural component of cell membranes.

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10
Q

Types of lipids

A

Fats(energy storage), waxes(waterproofing), phospholipids(cell membrane) and steroids(hormones)

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11
Q

Two compounds that are formed by a condensation type reaction(removal of water to form bonds)

A

Disaccharides(two sugars joining together and fats ( between fatty acids and glycerol)

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12
Q

What is formed when 3 fatty acids are attached to a molecule of glycerol?

A

Triglycerides (dietary fats)

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13
Q

What is formed when 2 fatty acids are attached to a molecule of glycerol?

A

Phospholipids

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14
Q

Phospholipids in cell membranes

A

Cell membranes are made up of a bi layer of lipids the head group ( hydrophilic end - choline and phosphate) faces out while the fatty acid(hydrophobic end) forms the interior of the membrane. This allows for a few molecules (like water and gas) to pass through . This is what keeps the inside of a cell separated form the outside.

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15
Q

What are proteins

A

Polymers of amino acids
Consists of one of more polypeptide chains

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16
Q

How do proteins differ from one another

A

Size : number of amino acids (proteins usually have 200 to 1000 amino acids)
Sequence of amino acids(there composition)

17
Q

Two functions of proteins

A

Structural proteins- collagen in hair, skin, keratin in hair
Enzymes: all metabolic processes(the breaking building transformation and rearrangement of compounds are done by enzymes (proteins)
Transports proteins - oxygen in the blood is carried by hemoglobin( made up of proteins)
Everything expect for water and a few gases are transported through proteins.

18
Q

What is the most important macromolecules?

A

Proteins are considered the most important organisms compounds because of the different function they carry out.

19
Q

What makes up amino acids?

A

A amino group(basic), carbonyl group(acid), R-group(functional group) and a hydrogen all bonding with a carbon molecule.

20
Q

What are Your four levels of protein structure

A

Your four levels of protein structure are primary, secondary, tertiary and quaternary.

21
Q

What occurs in your primary protein structure

A

In your primary proteins structure you would have a sequence of amino acids.
A polypeptide or protein is a chain of amino acids. 

22
Q

What occurs in your secondary protein structure

A

secondary protein structure occurs when the sequence of amino acids are linked by hydrogen bonds. These hydrogen bonds which occur between carboxyl and amino groups causes the protein to Fold up and gives it an alpha helix or beta pleated sheet. 

23
Q

What occurs in your tertiary proteins structure 

A

Due to the interactions between your R-groups of amino acids proteins tend to fold up into tertiary structures. At this level proteins are functional

24
Q

What occurs at your quaternary protein structure

A

The quaternary protein structure forms when proteins are composed of more than one polypeptide these polypeptide bind spontaneously into a single protein.

25
Q

What are nucleic acids

A

Nucleic acids are polymers of nucleotides.
DNA and RNA are both nucleic acid DNA houses are genes which contain instructions for making proteins and RNA participates in protein synthesis

26
Q

What are the three parts of a nucleotide

A

A nucleotide has a five carbon sugar either ribose or deoxyribose.
One or more negatively charged phosphate groups attach to a five carbon of pentose sugar.
A nitrogenous base.

27
Q

What is denaturation

A

Is the destruction of the 3-D dimensional shape of a protein this can be reversible or irreversible.

28
Q

Explain why protein structure is essential to its function

A

So when proteins do not take on a globular shape this can cause them to not function well.This is what happens in sickle cell Amenia. This disease is caused by the substitution of a single amino acid by another amino acid in the primary structure of a protein. This causes the protein to have a long and fibrous shape instead of a globular shape.