Lecture 4 Flashcards

1
Q

All living things contain what? (4)

A

nucleic acids, proteins, carbohydrates and lipids

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2
Q

Why is carbon so special? (2)

A
  • it can bound up with 4 separate atoms
  • it can bond with another C atoms
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3
Q

Is CO2 organic?

A

NO, it’s not organic b/c there’s only one C

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4
Q

Name 3 different arrangements of carbon skeleton:

A
  • straight
  • branched
  • rings (long or short) bonds
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5
Q

What are functional groups?

A

molecular commponents attached to that carbon skeleton

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6
Q

Name all 7 functional groups you need to know and recognize

A
  • Adelhyde
  • Carbonyl
  • Carboxyl
  • Phosphate
  • Hydroxyl
  • Sulfhydryl
  • Amino
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7
Q

You also have to know what 2 other functional groups

A

Estradiol and Testosterone

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8
Q

Biological molecules are composed of WHAT that are linked to each other

A

composed of subunits

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9
Q

How do you call a single unit?

A

a monomer (comme une perle)

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10
Q

How do you call a chain/ring of monomers?

A

a polymer (like a pearl necklace)

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11
Q

How do we build chains (polymers)? (2)

A

Dehydration Synthesis or Condensation reaction

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12
Q

What is this Dehydration Synthesis?

A

Dehydration removes a water molecule, forming a new bond
= a bond forms and WATER is released

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13
Q

How do you breakdown a chain (polymer)?

A

with hydrolysis

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14
Q

What is hydrolysis?

A

it adds a water molecule, breaking a bond
= water is added and a bond is broken

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15
Q

Name all 4 main classes of biological molecules

A
  • lipids
  • carbohydrates
  • proteins
  • Nucleix acid
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16
Q

Name a carbohydrate

A

sugar

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17
Q

could sugar be complex or simple

A

BOTH

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18
Q

What is the process of cellular respiration?

A

carbohydrates broken down for energy

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19
Q

How are they stored?

A

stored as long chains

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20
Q

Stored for long-term or short-term reserves?

A

short-term reserves

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21
Q

If there is too much of glycogen, what will happen?

A

the liver will store it

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22
Q

What are the 2 main functions of carbohydrates?

A
  • they serve as a source of energy (sugars)
  • they provide structure and support (cellulose)
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23
Q

In what ratio are C, H, O?

A

CH2O -> 1:2:1

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24
Q

Are monomers complex or simple sugars?

A

simple sugars (polymers are complex sugars)

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25
What are the 2 types of simple sugars?
- monosaccharides - dissacharides
26
What are monosaccarides?
monomers of carbohydrates
27
They share the same molecular formula, which one?
C6H12O6
28
Name 3 examples of monosaccharides
- glucose - galactose - fructose
29
What are disaccharides?
2 linked monosaccharides
30
Give 3 examples of disaccharides
- sucrose (glu. + fructose) (table sugar) - lactose (glu. glactose) (milk sugar) - maltose (glu. + glucose) (brewing sugar)
31
What are complex sugars named?
polysaccharides
32
What are polysaccharides?
polymers of monosaccharides
33
Name 2 storage carbohydrates
- Starch - Glycogen
34
Starch is stored by what?
Energy storage in plants (where they convert excess glucose as starch)
35
Glycogen is stored by what?
animals stored excess glucose as glycogen
36
Name 2 structural carbohydrates
Cellulose and Chitin
37
Where can you find cellulose?
support in plants (wood) and fiber
38
Where can you find chitin?
in fungal cell walls and external skeleton of insects and other anthropods
39
TRUE OR FALSE: Herbivores eat plants and produce enzymes
FALSE they eat plants and DO NOT produce enzymes to breakdown cellulose
40
What is in their digestive system?
a house bacteria
41
Why does this bacteria have enzymes?
to breakdown cellulose
42
What is the second main class of biological molecules?
lipids
43
Do lipids have water?
little or no affinity for water
44
What are the 3 major types of lipids?
- neutral fats - phospholipids - steroids
45
TRUE OR FALSE Different structures and functions but they are hydrophobic
TRUE
46
what does hydrophobic mean?
water-fearing
47
Long term or short term?
long-term reserves of fat tissue
48
protections for vital organs from shock
TRUE
49
buoyancy
TRUE (tendency of an object to float or to rise in a fluid when submerged)
50
Does not maintain body temperature
FALSE it does
51
Fat is constructed from what?
from 2 kinds of smaller molecules
52
Define what these 2 kinds of smaller molecules are
- 1 molecule of glycerol - 1 to 3 molecules of fatty acids
53
There is a term that defines 3 fatty acids
triglyceride
54
What is the second type of lipid?
A phospholipid
55
are they a major constituent of cell membranes?
YES
56
What is the structure of a phospholipid: (4é)
- molecules similar to neutral fats - 2 molecules of fatty acids - 1 glycerol molecule - 1 phosphate molecule
57
Phospholipids are an ________ molecule
amphipathic
58
What does amphipathic mean?
it has hydrophobic and hydrophylic parts
59
Which part is hydrophobic and which part is hydrophilic?
The HEAD is hydrophylic (attracted to water) TAIL is hydrophobic (repelled from water)
60
When placed in water, they self-assemble into what?
a bi-layer (double-layer)
61
Is the head of the tail on the outside?
the hydrophilic head is outside https://d20khd7ddkh5ls.cloudfront.net/lipids_phospholipids.jpg
62
What is the third type of lipid?
steroids
63
there are 3 main functions, name them
- constituent of cell membrane (cholesterol) - components of vitamins (ex. vit. D) - components of hormones (ex. testosterone, estrogens, progesterone...)
64
Steroids are made from what?
sterol
65
What are sterols?
multiple rings of carbon atoms
66
NEED TO RECOGNIZE A STEROL RING STRUCTURE AND A CHOLESTROL
67
What are proteins known for?
proteins are the workhorses in the cell
68
name all 4 main functions of a protein:
transport proteins enzymes protein hormones
69
Proteins are made of what?
amino acids (monomers)
70
All amino acids have the same basic skeleton, tell me important info
- 20 commons a.a. used to build proteins - POLYPEPTIDES (polymer of a.a.) - PROTEIN (1 or more functional polypeptides)
71
What do amino acids contain? (5)
- carbon - hydrogen - oxygen - nitrogen - some of them also contain sulfur
72
What is the basic strucutre of an amino acid?
- 2 functional groups (amino group and carboxyl group) - 1 variable group (R)
73
Name all 9 examples of a.a.
- Glycine (Gly) - Alanine (Ala) - Valine (Val) - Leucine (Leu) - Isoleucine (Ile) - Methionine (Met) - Phenylalanine (Phe) - Tryptophan (Trp) - Proline (Pro)
74
What is a polypeptide?
a chain of amino acids
75
Name the process of water removal
Dehydration synthesis (condensation reaction)
76
Going from a carboxyl group + amino group to a peptide bond is that dehydration synthesis or hydrolysis?
Removal of h20 (water) so dehydration synthesis
77
how levels are there to build a protein? name them
4 levels of stuctures Primary Secondary Tertiary Quaternary
78
Why is the primary level so important?
b/c if the sequence and order of the a.a. is wrong, everything is wrong (which can lead to disease and abnormalities)
79
Continue the sentence: new form,
new function (form determines function)
80
What can alter the protein's conformation and ability to function?
every small change in the primary structure
81
the order of the a.a. are determined by what?
by the nucleotide (genetically determined)
82
Give an example of abnormality
a substitution of a single "wrong" a.a. in the primary structure can cause a disease sickle cell anemia where blood cells don't have the same shape (carries less oxygen = bad)
83
What happens in the secondary structure?
coiling and folding of a sequence of amino acids
84
Which 2 differents types of forms can they be coiled/folded
coiling --> alpha helix folding --> beta pleated sheet
85
The secondary structure of a protein is maintained by what type of bond?
Hydrogen bonds
86
which type of form (alpha or beta) is common in fibrous protein?
beta pleated sheet (beta-keratin)
87
are hydrogen bonds strong?
together, HB are strong but weak individually
88
Pleated sheets make up the core of what?
core of globular proteins
89
Is tertiary related with a single or many polypeptides?
a SINGLE polypeptide
90
Name 4 different kinds of bonds b/w a.a can occur within one protein
HB, ionic bonds, covalent bonds, hydrophobic interaction
91
What is quaternary structure?
the fusion of 2 or more polypeptides (bond together) into one functional macromolecule
92
Name 2 proteins and their structure
Hemoglobin --> 4 polypeptide subunits Collagen --> 3 helical polypeptides
93
What does Monomeric mean?
proteins made of a single polypeptide chain
94
What does oligomeric mean?
2 or more polypeptide chains
95
What do we call when the protein uncoils into a random shape
protein denaturation
96
so what does protein denaturation mean?
- disruption in 2 and 3 structures - temporary or permanent = break down of proteins
97
True or false: Denaturation reactions are strong enough to break a peptide bonds
FALSE
98
What can break a peptide bond
high temperature
99
Name a very important protein
a RIBOSOME
100
in which structure are ribosomes displayed?
quaternary structure
101
What does it use to make other proteins?
RNA
102
Where are ribosomes made?
in the nucleolus
103
HB a occur in which structures?
2 and 3 structures
104
what can disrupt these bonds?
alcohol