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Bio test Biochem > bio test sep 17 > Flashcards

bio test sep 17 Flashcards

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Biology 101 flashcards
1
Q

Monomer

A
  • small molecule (reacts with similar molecule to form a bigger molecule)
  • smallest unit in a polymer
  • building blocks for biological processes (DNA, RNA, proteins , carbohydrates)
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2
Q

Monosaccharide

A

-most basic form of a carbohydrate

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3
Q

Disaccharide

A
  • two monosaccharides bonded together using a glycosidic bond to form a disaccharide
  • two sugars (double sugar)
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4
Q

Polysaccharide

A
  • two or more monosaccharides bonded together using a glycosidic bond
  • simple suagrs
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5
Q

Glycosidic bond

A

a covalent bond that bonds a carbohydrate (sugar) to another group

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6
Q

Fatty Acid

A
  • a hydrocarbon chain w carboxyl function at one end
  • affects saturation
  • the longer the chain gets, the more insoluble it becomes
  • example ; butryic acid (butter)
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7
Q

Saturated Fatty Acid

A
  • has a single Carbon bond
  • has the maximum amount of Hydron atoms possible
  • found in lauric acid (coconut oil)
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8
Q

Unsaturated Fatty Acid

A
  • has one or more double carbon bonds
    healthier than saturated
  • can be found in nervonic acid ( fish oil)
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9
Q

Fats

A
  • Fats are made up of 2 molecules (glycerol and fatty acid)

- formed by dehydration rxn

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10
Q

Tryglycerides

A
  • The most well known fat

- made up of 3 fatty acids joined to a single glycerole molecule

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11
Q

Phospholipids

A
  • MANDATORY FOR CELL FUNCTION
  • lipid that consists of 2 fatty acids
  • makes up the lipid bilayer of cell membranes
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12
Q

Steroids

A
  • inlcludes sex chromosomes (testosterone, estrogen, progesterone)
  • groups of lipids with structures on fused carbon rings
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13
Q

Waxes

A
  • provide a water resistant wax layer

- made of large long fatty acid chains

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14
Q

Nucleotide

A
  • building block of DNA

- Adenine, Thymine, Guanine, Cytosine

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15
Q

DNA

A
  • deoxyribonucleic acid
  • carries and stores hereditary materials
  • double helix structure
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16
Q

RNA

A

Ribonucleic acid
- Involved in protein synthesis in eukaryotes
- hereditary molecule found in many viruses
there are 3 types of RNA 1
1) Messanger Rna
2) Transfer RNA
3)Ribosomal RNA. (MTR)

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17
Q

Amino Acids

A
  • What proteins are made of
  • 20 amino acids
  • 12 are “non essential” they are already made by our body
  • 8 are ‘essential’ we have to obtain these through foods
  • bonded to make proteins through dehydration rxn
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18
Q

Peptide Bonds

A
  • a type of covalent chemical bond linking two amino acids together
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19
Q

Denaturation

A
  • process modifying the molecular structure of a protein

- involves breaking of weak linkages

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20
Q

Enzyme

A
  • biological catalyst that accelerate chemical reactions by lowering reaction time
  • consists of one or more polypeptide chain
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21
Q

Catalyst

A

-the process in which a chemical reaction is sped up without being altered in the process

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22
Q

Active site

A
  • the region where the substance is trying to go to form the reaction
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23
Q

substrate

A
  • a molecule upon which an enzyme acts

- temporary molecule that is formed when an enzyme comes into perfect contact with its substance

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24
Q

Cofactor

A
  • a non protein chemical compound or metallic ion that is required for an enzyme activity as a catalyst
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25
Q

Coenzyme

A
  • small molecules

- helps enzymes catalyze a reaction

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26
Q

What are the different Carbohydrates

A

1) monosaccharides
2) disaccharides
3) polysaccharides

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27
Q

functions of monosaccharides

Characteristics of monosaccharides

A
  • produce and store energy

- soluble in water

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28
Q 
function of disaccharide
characteristics of disaccharide
A
  • provides you with quick energy

- soluble in water

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29
Q 
function of. a polysaccharide 
characteristics of a polysaccharide
A
  • energy storage and structural support

- insoluble in water

30
Q

functions of lipids

A
  • serve as structural components of cell membranes
  • energy for storehouses
  • important signalling molecules
31
Q

characteristics of lipids

A
  • energy rich organic molecules
  • insoluble in water
  • no ionic charge
32
Q

five types of Lipids

A

1) Fatty Acids
2) Fats
3) Wax
4) Phospholipids
5) Steroids

33
Q

components of fatty acid

A
  • single hydrocarbon chain (carboxyl function at on end)

- As the chain increases the fatty acid becomes more insoluble

34
Q

Describe the relationship of size of fatty acid and solubitlity.

A
  • the longer the fatty acid chain, the more insoluble they become
35
Q

Saturated vs Unsaturated

A 
Saturated- single carbon bond 
- have the most hydrogens possible
-lauric acid (coconut oil)
Unsaturated- double carbon bonds
-nervonic acid (fish oil)
36
Q

components of fat : made of 2 molecules

A

-made of 2 molecule (glycerole and fatty acid)

37
Q

Describe phospholipid structure

A

-2 fatty acid chains and one phospholipid group

38
Q

describe the function of a fatty acid

A

Cell membrane

39
Q

example of fatty acid

A

lipid bilayer

40
Q

describe the structure of a steroid

A

four carbon rings

41
Q

function of a steroid

A

hormonal signalling (think estrogen progestrone and estrogen)

42
Q

characteristics of steroids

A

testosterone and cholesterole

43
Q

structure of wax

A

long fatty acid chain lined to alcohol

44
Q

function of wax

A

water resistance and protection

45
Q

example of wax

A

wax coating on leaves , fruits and stems

46
Q

what are essential amino acids

A

the 8 amino acids our bodies do not produce , it is ESSENTIAL we get them through food intake

47
Q

what are non essesntial amino acids

A

the 12 amino acids our bodies produce naturally

48
Q

how is a peptide bond formed

A
  • amino acids bond together

- forms a condensation reaction

49
Q

Describe how proteins are formed

A
  • made of amino acids

- proteins are polymers composed of amino acid monomers joined by peptide bonds in a 3D structure

50
Q

Four levels of protein structures

A

1) primary protein structure
- sequence of a chain of amino acids
2) secondary protein structure
- hydrogen bonding to the peptide backbone causes amino acids to fold
3) tertiary protein structure
- three dimensional pattern of a protein
- CRITICAL TO PROTEIN STRUCTURES
4) quaternary protein structures
- protein consisting of one amino acid chain

51
Q

how does denaturation occur in proteins?

A

disrupts the alpha helix and beta sheets in a protein and uncoils it to a random shape
- UNCOILS THE DNA OF A PROTEIN

52
Q

what is the affect of denaturation

A
  • they lose their structure therefore they cannot function
53
Q

The 7 types of proteins

A

1) structural
2) defensive
3) signal
4) carrier
5) recognition and receptor
6) enzyme
7) motile

54
Q

Identify the 5 nitrogenous bases

A

1) Adenine
2) Thymine
3) Guanine
4) Cytosine
5) Uracil

55
Q

How do nitrogenous bases pair ?

A

A +T

C+G

56
Q

What is the function of DNA ?

A
  • contains genetic instruction

- stores hereditary information

57
Q

what is the structure of DNA?

A
  • a double helix structure
58
Q

what is the relationship between DNA and nucleotides

A

DNA is made of nucelotides

59
Q

DNA relation to Nitrogenous Bases

A

nitrogenous bases are found in DNA strands in the double helix

60
Q

What is the function of RNA ?

A

carrier of genetic codes in some viruses

61
Q

Nitrogenous bases in RNA

A

Adenine , Guanine , Cytosine, Uracil

62
Q

Nucleotides and RNA relation

A

consists of ribose nucleotides forming strands

63
Q

RNA structure

A

-Single stranded

64
Q

Components of DNA

A
  • deoxyribose sugar
  • base
  • deoxyribose
65
Q

Function of enzymes

A
  • regulate chemical reactions in the body
66
Q

Uses of enzymes

A
  • digestion

- detergent

67
Q

how do enzymes speed up reactions

A
  • by lowering energy which allows rxn to occur faster
68
Q

what is the structure of enzymes

A
  • 3D shape

- shape of the active site matches the substrate like a puzzle piece

69
Q

Describe how enzyme structure allow them to speed up a reaction

A
  • the enzyme structure is constant throughout and can start over as soon as it finishes with the last product causing it to be quick
70
Q

Four factors that affect enzyme activity

A

1) Ph
2) temperature
3) enzyme concentration
4) enzyme acticity

71
Q

what is a competitive enzyme inhibition

A

the substrate and inhibitor are in competition for the spot in the enzyme

  • NO RXN OCCURS
72
Q

what is non competitive enzyme inhibition

A

the inhibitor binds to the active site and changes the shape

  • NO RXN OCCURS

Bio test Biochem (1 decks)

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