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Biomolecules Review > Biomolecules test > Flashcards

Biomolecules test Flashcards

1
Q

Types of carbs

A

Monosaccharides and disaccharides and polysaccharides

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2
Q

Monosaccharides : functions and characteristics

A

Quick energy source, simple sugars, straight chain or ring form

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3
Q

Disaccharides : function and characteristics

A

Quick energy source, 2 monosaccharides joined by a dehydration reaction. Examples: sucrose, lactose and maltose

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4
Q

Polysaccharides

A

Long chain or monosaccharides pinked by glysosidic bonds. Used for energy storage, structural support, cell to cell communication
Examples: starch cellulose

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5
Q

How’re glysosidic bonds formed?

A

Covalent bonds, bond between 2 monosaccharides- glucose and fructose producing the disaccharide, sucrose.
Can be broken in digestion.

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6
Q

Lipids : functions and characteristics

A

Long term energy source, energy storage, form cell membranes, hormones, vitamins.
Non polar and hydrophobic.

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7
Q

Five types of lipids

A
  1. Fatty acids
  2. Fats
  3. Phospholipids
  4. Steroids
  5. Waxes
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8
Q

Components of fatty acids

A

Single hydrocarbon chain with a carboxyl functional group at one end.

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9
Q

Fatty acids and water solubility

A

The more the chain length grows, the less water soluble it becomes. (More hydrophobic).

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10
Q

Difference between a saturated fatty acid and an unsaturated fatty acid

A

Saturated fatty acids have all the Hydrogens bonded while the unsaturated ones don’t. Also, unsaturated fatty acids can have more than one carbon double bond.

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11
Q

Monounsaturated

A

Only one carbon double bond

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12
Q

Polyunsaturated

A

Two or more carbon double bonds.

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13
Q

Components of fats

A

Fatty acids and glycerol

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14
Q

Components of triglycerides

A

3 fatty acids and a glycerol joined through dehydration reactions.

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15
Q

Characteristics of saturated fats

A

Single bonds in the hydrocarbon chain
Only one carbon double bond
Solids at room temp
Butter

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16
Q

Characteristics of unsaturated fats

A

Unsaturated fat’s do not have everything bonded in their hydrocarbon chains they have double bonds in hydrocarbon chains.
Liquid at room temperature
Olive oil, nuts

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17
Q

Characteristics and functions of phospholipids

A

Made from a phosphate group, two fatty acids and a glycerol.
Hydrophilic head and two hydrophobic tails joined by alcohol residue.

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18
Q

Phospholipids function

A

Cell membrane, lipid bilayer.

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19
Q

Steroids function

A

Cell to cell communication - hormonal signalling, cell response to its environment and growth.
Example - testosterone and cholesterol.

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20
Q

Steroids characteristics

A

-hydrophobic
Group of lipids with structures theatre composed of 4 CARBON RINGS.
Sterols are most common

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21
Q

Steroids structure

A

Four hydrocarbon rings

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22
Q

Waxes function

A

Waxes function as a protective barrier for plants and fruits. And a water resistant barrier. They have a waxy coating on birds to keep their feathers dry.

23
Q

Waxes characteristics

A

Biggest lipids former when long fatty acid chains are linked to alcohols or carbon rings.
Hydrophobic, extremely non polar, soft solid

24
Q

Waxes structure

A

Long fatty acid chains linked to alcohol or carbon rings

25
Q

Amino acids structure

A

An amino acid joined to a hydrocarbon and a carboxyl group and a side chain.

26
Q

Essential and non essential amino acids

A

There are 12 non essential amino acids that are formed by our cells.
8 essential amino acids thatre derived from the food we eat.

27
Q

How is a Peptide bond formed

A

By a dehydration synthesis reaction

28
Q

How is a protein formed

A

Amino acids - peptides - dipeptides - polypeptides + 50amino acids - protein

29
Q

Once foldin occurs…

A

The protein is able to function.

30
Q

4 levels of structure of proteins

A

Primary
Secondary
Tertiary
Quaternary - 2 or more polypeptides that come together to form the final functional protein.

31
Q

How can denaturation occur in proteins. Effect?

A

Denaturation can occur from too high or low of a temperature or pH level.
The effect is a protein that will not function properly and therefore cannot be used.

32
Q

Seven types of protein

A

Structural - framework support - hair
Enzymes - catalyst - amylase
Motile - movement - actin and myosin
Recognition and receptors - cell markers - mHc
Carrier - transport of materials - hemoglobin
Signal - messenger - hormones
Defensive - infection fighters - antibodies

33
Q

Nucleotide structure

A

Phosphate group, pentode sugar, nitrogenous based and can also have an amino group.

34
Q

Five nitrogenous bases

A 
Adenine
Guanine 
Cytosine 
Thymine 
Uracil
A-T, G-C
35
Q

DNA function

A

Deoxyribonucleic acid

Stores hereditary information responsible for inherited traits in eukaryotes and prokaryotes and many viruses.

36
Q

DNA STRICTIRE

A

Double helix

37
Q

DNA nucleotides

A

Chains of nucleotides called polynucleic chains with one nucleotide linked to the next by 1 bridging phosphate group between the 5 carbon of one sugar the the 3 carbon of the next sugar in line.

38
Q

DNA in nitrogenous bases

A

(A,c,g,t)

39
Q

DNA components

A

Phosphate group, pentose sugar, nitrogenous base (a,c,g,t)

40
Q

RNA function

A

Ribonucleic acids

Hereditary molecule of some viruses

41
Q

RNA structure

A

Half a ladder - single stranded

42
Q

RNA nucleotides

A

5 carbon ribose sugar
Phosphate molecule
1 of four nitrogenous bases

43
Q

RNA 4 nitrogenous bases

A

Adenine, guanine, cytosine or uracil.

44
Q

Function of enzymes

A

Enzymes speed up chemical reactions without being consumed or changed - catalyst
Regulate reactions so they perform at the right pace

45
Q

Enzyme uses

A

Digestion - nutrient(polymers) breakdown
Detergents- breakdown of stains
Brewing- make chemical reaction faster

46
Q

How do enzymes speed up reactions?

A

They lower the amount of energy needed to start the reaction.

47
Q

Four factors that affect enzyme activity

A
  1. Enzyme and substrate concentration
  2. Enzyme inhibitors
  3. pH
  4. Temperature
48
Q

Competitive inhibition

A

Where the substrate and inhibitor both want the active site but the inhibitor gets it.

49
Q

Non competitive inhibition

A

The inhibitor wants the spot of the cofactor (coenzyme) and changes the shape of the enzyme so the substrate ain’t fit.

50
Q

Cofactor

A

Non protein group (sugar, ion, element) that binds precisely to enzyme.

51
Q

Coenzyme

A

Organic molecule that acts as a cofactor of an enzyme.

Vitamin B3

52
Q

Active site

A

The site the substrate wants to bind to. Competitive Inhibitor also will bond here.

53
Q

Substrate

A

Reacts with reagent to create a product. Speeds up chemical reaction

54
Q

Catalyst

A

Accelerated chemical reaction without being affected.

Biomolecules Review (1 decks)

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