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Biology > Biological Molecules > Flashcards

Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is a monomer?

A

Monomers are small units which larger molecules are made up of

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2
Q

Examples of monomers

A

Monosaccharides, amino acids and nucleotides

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3
Q

What is a polymer?

A

A polymer is a molecule made out of a large chain of monomers joined together

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4
Q

What is a condensation reaction

A

A condensation reaction joins two molecules together with the formation ofa hydrogen bond and eliminates water molecules

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5
Q

What is a hydrolysis reaction?

A

A hydrolysis reaction is a break of the chemical bond between two molecules and uses water molecules

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6
Q

What are carbohydrates made out of?

A

They are made out of monosaccharides

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7
Q

What are the most common type of monosaccharide

A

Glucose, fructose and galactose

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8
Q

What bond is formed from a condensation reaction in carbohydrates?

A

A glycosidic bond is formed

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9
Q

Types of dissaccharides

A

Sucrose= glucose + fructose
Maltose= glucose + glucose
Lactose= glucose + galactose

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10
Q

Isotopes of glucose

A

Alpha glucose, beta glucose

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11
Q

Structure of alpha glucose

A

In alpha glucose the hydroxyl group is known the same side. This means the alpha glucose is more reactive to enzymes meaning it is easier to break down.

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12
Q

Structure of beta glucose

A

Beta glucose has the hydroxyl groups on opposite size of the molecule which makes the molecule more stable

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13
Q

Polysaccharides of a-glucose

A

Glycogen and starch

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14
Q

Polysaccharide of B-glucose

A

Cellulose

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15
Q

What types of sugar is glucose made out of?

A

Hexose sugar which has 6 carbon atoms

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16
Q

Starch

A

Monosaccharide: a-glucose
Structure: mixture of amylose and amylopectin. Amylose- long unbranched forms coiled shape. Amylopectin- long branched chain due to 1-6 glycosidic bonds.
Properties: amylose= coiled shape makes it compact to store I’m small spaces. Amylopectin= branched chain increases surface area for enzymes to hydrolyse glycosidic bonds- glucose released faster.
Uses: plant uses starch to store excess glucose. Starch can also be hydrolysed.

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17
Q

Glycogen

A

Monosaccharide: a-glucose
Structure: long branched chain with lots of side branches. 1-6 glycosidic bonds
Properties: lots of branches increases the surface area so allows enzymes to hydrolyse glycosidic bonds allowing glucose to be released fast. compact molecule- good for storage.
Uses: animals store excess glucose as glycogen in muscles and the liver. Glycogen can be hydrolysed and turned in glucose to be released when glucose is needed for respiration.

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18
Q

Cellulose

A

Monosaccharide: B-glucose
Structure: long unbranded chain. Glycosidic bonds are 1-4. Linked with hydrogen bonds between glucose molecules in each chain to for thicker erodes called microfibrils
Properties: hydrogen bonds and microfibrils makes it very strong however still flexible.
Uses: major structural component in cell walls of plants, provides support and allows cells to become turgid

19
Q

What biochemical test is used to look for reducing/ non-reducing sugars

A

The Benedict’s test

20
Q

What are the two groups of lipids?

A

triglyerides and phospholipid

21
Q

How is a triglyceride formed

A

It is formed from 1 glycerol molecule and 3 fatty acids

22
Q

How is a phospholipid formed

A

1glycerol molecule, 2 fatty acids and a phosphate group

23
Q

What is a triglyceride

A

Triglycerides can either be saturated with no double bonds between the carbon or it can be unsaturated where there is a double bond between a carbon group. Ester bonds are formed by condensation reaction between the 3 OH groups on the glycerol and 3 fatty acids

24
Q

What are phospholipids

A

Phospholipids have ester bonds between the 2 of the OH on the glycerol and 2 fatty acids and a phosphate group binded to the other OH on the glycerol

25
Q

What are triglycerides good for

A

They are a good energy store as there is a lot of energy released into the cells after being carried in the blood.

26
Q

What practical is used to test for a lipid

A

The emulsion test- take the sample and mix 5cm³ of ethanol. Add 5cm³ of water. If a milking white emulsion forms in it there are lipids present

27
Q

What are proteins made up of

A

Amino acids

28
Q

How to amino acids make proteins

A

They are joined together by peptide bonds to form a polypeptide protein

29
Q

What is the structure of an amino acid

A

They have an alpha carbon, hydrogen, a carboxyl group (COOH), an amino group (H²N) and an R group

30
Q

What is an R group

A

An r group has a specific side chain which is attached to the alpha carbon. This allows amino acids to be grouped according to chemical properties.

31
Q

What is a primary structure

A

A primary structure is the sequence of the amino acids

32
Q

What is a secondary structure

A

The folding of the polypeptide chain either alpha helix or beta pleted sheets

33
Q

What is a tertiary structure

A

The 3D shape of the polypeptide due to hydrogen, covalent bonds and disulfite bridges

34
Q

How do 2 amino acids form a peptide bond

A

Whe one of the amino acids carboxyl groups reacts with the other amino acids amino group they go through a condensation reaction, eliminating water molecules and bonding them together. Creates a dipeptide

35
Q

How to test for proteins

A

Buiret test, will turn purple if present

36
Q

Define an enzyme

A

They are biological catalysts which lower activation energy by finding a different pathway

37
Q

What is the enzyme model called

A

The induced fit model

38
Q

How does the induced fit model work

A

. The matching substrate will find the correct enzyme active site
. Binds to the active site to create an enzyme-substrate complex
. This results in a conformative change so the substrate fits perfectly into the active site of the enzyme.
. Substrate then broken down to form products and pushed out due to energy built up inside the enzyme

39
Q

What factors effect rate of reaction

A

Concentration, temperature, pH

40
Q

How does increased concentration of enzymes or substrate impact enzymes

A

Increasing enzymes or substrate will initially increase the amount of enzyme substrate complexes as it means there are more active sites to be filled or more substrate to fill enzymes. Overtime it will plateau as there will be another limiting factor such as not enough substrate to fill extra active sites or not enough active sites to fit all of the substrate

41
Q

How does pH impact enzymes

A

Above or below the optimum level of pH, the H+ ions and OH- ions will disrupt the bonds holding the enzymes 3D structure causing them to denature

42
Q

How does temperature impact enzymes

A

As the temperature increases so will rate of reaction however then it reacts over 45 degrees the active sites will denature and change shape due to being to hot so rate of enzymes will dramatically decrease

43
Q

What is a competitive inhibitor

A

They have a similar shape to the substrate molecule. They block the active site so that the substrate cannot bind so there is no enzyme-substrate complexes.

44
Q

What is a non-competitive inhibitor

A

They do not bind to the active site however they bind to the allosteric site. This binds and changes the shape of the active site so the substrate cannot bind so no enzyme substrate complexes.

Biology (10 decks)

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