Theme 5 Dan Molecules Flashcards

(37 cards)

1
Q

Monomer

A

One molecule, single most basic unit

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2
Q

Dimer

A

2 monomers chemically bonded together

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3
Q

Polymer

A

A long chain of monomers chemically bonded together

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4
Q

Anabolism

A

The synthesis of complex molecules from simple molecules by a condensation reaction (building larger molecules)

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5
Q

Catabolism

A

Breaking down large molecules. The synthesis of simple molecules from complex molecules by a hydrogen reaction

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6
Q

Covalent bonding (electrons)

A

Shares electrons

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7
Q

Ionic bonding (electrons)

A

Gains or looses electrons

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8
Q

Hydrogen bonding

A

Electrostatic force of attraction between a hydrogen atom which is covalently bonded to a more electronegative atom.

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9
Q

Condensation reaction

A

Joins two molecules together involving the elimination of a molecule of water

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10
Q

Hydrolysis reaction

A

Breaks a chemical bond between two molecules involving the use of water molecules.

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11
Q

Isomeric monosaccharides

A

Same chemical formula, different structure

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12
Q

Glycosidic bond

A

Bonding carbohydrates

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13
Q

How many amino acids are there

A

20

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14
Q

What are the monomers that make up polymers of proteins

A

Amino acids

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15
Q

What is the structure of an amino acid

A

Central carbon atom to which are attached four chemical groups
Amino group (-NH2)
Carboxyl group (-COOH)
A hydrogen atom (H)
R (side) group (all 20 have a different R)

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16
Q

What do proteins form into?

17
Q

What does the primary structure determine

18
Q

Describe the primary structure of protein

A

Amino acids joined together by peptide bonds assembled by ribosomes

19
Q

Describe the secondary structure of protein?

A

Hydrogen bonds cause polypeptides to twist and form either an alpha helix or beta sheets.

20
Q

Describe the tertiary structure of proteins

A

The alpha helixes of the secondary structure can be twisted and folded again and is held together by different bonds (such as ionic bonds and disulphide bridges) and areas that are hydrophilic and hydrophobic

21
Q

Describe the quaternary structure of proteins

A

The structure of proteins which are composed of two or more smaller protein chains such as alpha chains, beta chains, heme group etc

22
Q

What are the two main lipids?
What do they contain?
Are they soluble in water?

A

Triglycerides and phospholipids
Carbon, hydrogen and oxygen
No

23
Q

What are the 4 roles of lipids in the body?

A

Protection
Insulation
Energy
Phospholipids

24
Q

What is triglycerides?
Shape
Group of?
What bond?
What reaction?

A

A group of 3 fatty acids combined with glycerol formed by an ester bond in a condensation reaction E shaped

25
What are phospholipids? Made of? Shape
One molecule of glycerol, two fatty acid chains and one phosphate molecule. They have a hydrophilic head and two hydrophobic tails
26
Example of globular proteins
Enzymes and hormones
27
What does denaturing proteins mean?
Changing the shape from the original structure and it is not reversable
28
Creating proteins : transcription
A copy is made of the genetic code of the DNA inside the nucleus
29
Creating proteins: translocation
The code is translated from DNA instructions into amino acids sequenced by the ribosome
30
What are 3 functions of proteins in the body
Blood clotting, transport of oxygen, immunity and creating antibodies.
31
Difference between essential and non- essential amino acids
The body creates non-essential amino acids, it needs to digest non essential amino acids.
32
What is the bond for carbohydrates
Glycosidic bond
33
What is the bond for protiens
Peptide bond
34
What is the bond for lipids
Ester bond
35
Describe the lock and key model
Shape of active site does not change when substrate binds
36
Describe the induced fit model
Tertiary structure of the enzyme changes as the substrate approaches so the active site moulds around the substrate. (Not the same shape but the enzyme changes shape to fit in the active site)
37
What are the 3 principles of collision theory
Molecules collide Molecules must collide with enough energy to break and reform bonds Molecules must be in the correct spatial orientation