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BSC 2010 - Biology I > Exam # 2 - Lecture Notes 7-9 > Flashcards

Exam # 2 - Lecture Notes 7-9 Flashcards

1
Q

T/F: Lipids are not polymers, nor macromolecules.

A

True

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2
Q

Lipids are rich in ________.

A

hydrocarbon

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3
Q

What is the defining characteristic of lipids?

A

They are hydrophobic

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4
Q

______ ______ are the simplest lipid.

A

Fatty acids

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5
Q

What is the makeup of a fatty acid?

A

A long hydrocarbon chain with a carboxyl group at one end, and a methyl group at the other end

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6
Q

If you have a carbon-carbon double bond or more than one, it makes you…..

A

unsaturated

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7
Q

Whenever you have a double-bond…you get ___ atoms locked in a plane.

A

six

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8
Q

Molecules with the same atoms arranged differently are called _______.

A

isomers

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9
Q

If the carbons are on the same side of the double bond, it’s called a ___ isomer.

A

cisc

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10
Q

If the carbons are on alternating sides of the double bond, it’s called a ___ isomer.

A

trans

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11
Q

Which fatty acid do we find in nature?

A

cis fatty acids are found in nature

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12
Q

Where do the trans fatty acids come from?

A

Human industry

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13
Q

What does the omega number tell you?

A

Tells the position of the first double bond in a fatty acid counting carbon’s from the methyl end

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14
Q

Unsaturated fats lack the ________. Double bonds mean less _______.

A

hydrogens, hydrogen

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15
Q

What is the makeup of a fat?

A

Three fatty acids + 1 glycerol

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16
Q

What is a glycerol?

A

Three carbons in a chain. Each carbon has a hydroxyl group attached (total of three hydroxyl groups)

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17
Q

The hydroxyl group on the glycerol reacts with the _______ group on the fatty acid. What results?

A

carboxyl group. DEHYDRATION and COVALENT BOND

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18
Q

What is the major function of fat?

A

To store energy

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19
Q

What are the three “energy nutrients” that you get in your diet?

A

Fat, carbs, protein

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20
Q

Fats store energy, they’re going to serve as a ______ or _______.

A

cushion or insulation

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21
Q

Most animal fats are _________ fats.

A

saturated

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22
Q

Most vegetables fats, fish fats…are _______ fats.

A

unsaturated

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23
Q

Your animals fats, which are SATURATED fats, are typically _____ at room temperature. Your plant and fish fats are UNSATURATED, typically ______ at room temperature.

A

solid, liquid

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24
Q

It’s easier to pack saturated fat because the tails are _______. It’s harder to pack unsaturated fat because that cis configuration double bond make a _____ in the tail.

A

straight, kink

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25
Q

What type of lipid surrounds of cells?

A

Phospholipid

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26
Q

What is the makeup of a phospholipid?

A

Two fatty acids + 1 glycerol + phosphate group + additional chemical group

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27
Q

The phospholipid is both hydrophobic and hydrophilic…so it’s called __________.

A

amphipathic

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28
Q

So the phospholipid in being _______ is the ideal barrier. Cell membrane.

A

amphipathic

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29
Q

A steroid contains…

A

four fused rings

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30
Q

________ is a steroid.

A

Cholesterol

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31
Q

Cholesterol is also a what, and why?

A

An alcohol because of the ol-

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32
Q

Which means it must have a what?

A

hydroxyl group

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33
Q

So cholesterol is a ______, among the ______’s it’s a _______, and this _______ also happens to be an _______.

A

lipid, lipid’s, steroid, steroid, alcohol

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34
Q

Cholesterol is an important _______ ______ for making other biological steroids.

A

starting point

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35
Q

_______, which is the stress hormone.

A

Cortisol

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36
Q

_________ is also an important component of the cell membrane of cells.

A

Cholesterol

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37
Q

Bile is _________ and helps to digest ____.

A

amphipathic, fat

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38
Q

Fat is digested in your _____ ________.

A

small intestine

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39
Q

Your _____ creates bile and cholesterol.

A

liver

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40
Q

What is bile made out of?

A

Cholesterol

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41
Q

What vitamins do is, again, provide a ______ material, a _______, to make some very special bio molecules.

A

starting, precursor

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42
Q

Protein is a polymer made from a monomer called an _____ ____.

A

amino acid

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43
Q

The polymer is called a _________, and each contains many different _____ _____.

A

polypeptide, amino acids

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44
Q

The covalent bond that joins the amino acids is called a ________ bond.

A

peptide

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45
Q

When we say protein…really what that means is one polypeptide _______ into a specific shape.

A

folded

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46
Q

Once again, ______ to build a bio molecule…and a covalent bond that results is called a ______ bond.

A

dehydration, peptide

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47
Q

A protein…which is a polypeptide….________.

A

FOLDED

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48
Q

It’s the polypeptide ______ into a particular conformation. That’s a protein.

A

FOLDED

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49
Q

Proteins are an ______ source

A

energy

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50
Q

Where do you store your protein?

A

In your muscles

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51
Q

It’s not really a store of protein…it has a function…that function is _______ _________.

A

muscle contraction

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52
Q

Your muscle contracts because it is full of ________ _______.

A

contractile proteins.

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53
Q

Mother’s milk has _____ in it…casein is a ______ protein.

A

casein, storage

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54
Q

Another function of proteins is structural support . What protein is common within your bones?

A

Collagen

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55
Q

The receptor that a hormone binds to is made out of what?

A

Protein

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56
Q

Proteins play a fundamental role in ____-____ _________ because all receptors are proteins.

A

cell to cell communication

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57
Q

Proteins are involved in ________. We just talked about muscle contraction…that is what enables movement.

A

movement

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58
Q

________ is a protein! It transports oxygen. So _______ is another function of proteins.

A

Hemoglobin, transport

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59
Q

Defense…._________. _______ is an example of an immune function that is provided with a protein.

A

antibody

60
Q

_________! ________….the molecule on which our biochemistry most depends, also made from protein.

A

Enzymes

61
Q

What two functional groups are found in every amino acid?

A

An amino group, carboxyl group

62
Q

What happens to the carboxyl group under cellular pH?

A

This weakly acidic carboxyl group, under cellular pH, will ionize and lose a proton. It will loose the hydrogen on the hydroxide. The carboxyl group (minus the H on the carboxyl) will become negatively charged, and the hydrogen that was lost will go to the amino group, giving it a positive charge

63
Q

In every amino acid is a central ______ atom.

A

carbon

64
Q

A central carbon atom that we donate as ______.

A

alpha…alpha carbon

65
Q

Also…a ________ atom is bonded to every alpha carbon.

A

hydrogen

66
Q

What is the final bond to the alpha carbon?

A

An R group, or side chain of the amino acid

67
Q

Again, how do we get twenty?

A

The the R group that varies the twenty variations

68
Q

If you have ______ or ______, it makes you polar.

A

oxygen or nitrogen

69
Q

There are a total of ____ charged amino acids.
____ of them are acidic, therefore negatively charged.
____ of them are basic, therefore positively charged.

A

5, two, five

70
Q

How is a polypeptide built from these amino acids?

Which functional groups are going to react?

A

The carboxyl group of one amino acid will react with the amino group of another amino acid

71
Q

What kind of reaction is this, again?

A

DEHYDRATION

72
Q

Amino reacts with carboxyl…dehydration…covalent bond…and that covalent bond is called a _______ bond.

A

peptide

73
Q

We ALWAYS add onto the ________.

A

carboxyl

74
Q

The backbone contains a repeating pattern of…which atoms?

A

N-C-C

75
Q

For every peptide bond, there’s also a _______ group.

A

carbonyl

76
Q

Likewise, for every peptide bond, what used to be an amino group is now just this ________ connected to this nitrogen.

A

hydrogen

77
Q

When we say “polypeptide backbone”, what is everything that is included?

A

Repeating pattern of N-C-C, carbonyl oxygens and amino hydrogens

78
Q

When dehydration occurs, you no longer have those ______ from the amino and carboxyl group.

A

charges

79
Q

At one end…we will have a free amino group…it never reacted with anything.
At the other end…we will have a free carboxyl group…also never reacted with anything.
So amino and carboxyl are the two ends of a polypeptide.
We call this the __-_______ for nitrogen…
and the __-_______ for the carboxyl.

A

N-terminus, C-terminus

80
Q

What is the enzyme that cuts the bacterial cell wall?

A

Lysozyme

81
Q

What is the primary structure for a protein?

What is the chemistry that holds it together?

A

Which amino you have and in what order.

Covalent bonding holds the amino acids together

82
Q

How does the cell do this? How do you build glycine and then proline and then glutamic acid, etc. How do you know how to do that if you’re the cell? What do you NEED to build something of such complexity?

A

YOU NEED INSTRUCTIONS. You need a CODE.

83
Q

The order of amino acids in a protein is determined by the order of ________ in the _____ of that protein.

A

nucleotides, gene

84
Q

In other words…the order of amino acids in a protein is determined by the sequence of the _____ for that protein.

A

GENE

85
Q

What are genes for?

A

They encode the structure of our proteins, which in turn, run the cell

86
Q

Genes specify the _______ ______ of the protein for the cell.

A

primary structure

87
Q

It is the precise ________ _______ that causes the protein to fold in a particular way.

A

primary structure

88
Q

Which structure causes the protein to fold in a particular way?

A

PRIMARY STRUCTURE

89
Q

Secondary structure is characterized by _________ _______ of the polypeptide.

A

localized folding

90
Q

What are the two types of localized folding?

A

1) Coils (alpha helices)

2) Sheets (beta pleated sheets)

91
Q

So we have ______ ______ between backbone atoms.

A

hydrogen bonding

92
Q

What is the chemistry of the secondary structure?

A

Hydrogen bonding

93
Q

The overall three dimensional structure formed by the entire polypeptide is called _______ structure.

A

tertiary

94
Q

Tertiary structure is going to involve the __ ______ interacting with each other to hold this chain together.

A

R groups

95
Q

The ____ is where the non-polar amino acids are.

A

core

96
Q

Non-polar amino acids cluster in the interior of proteins, and they interact wit each other by __________ ________.

A

hydrophobic interactions

97
Q

What holds the tertiary structure together?

A

ALL FOUR WEAK INTERACTIONS COLLABORATE TO HOLD TOGETHER A TERTIARY STRUCTURE

98
Q

In secondary structure, the hydrogen bonding is going to involve the _________ atoms.

A

backbone

99
Q

The tertiary structure, recall, is the entire polypeptide ________.

A

folded

100
Q

Proteins are said to be in one of two structures, which are….

A

Linear or fibrous structure

101
Q

What is it that causes a chain to become a glob?

A

It’s hiding the non-polar amino acids. The non-polar side chain is trying to hide from the water

102
Q

One amino acid…one in particular…will provide a covalent interaction…which amino acid is it?

A

Cystine

103
Q

Which chemical group is only found in cystine?

A

Sulfhydryl group

104
Q

Now full disclosure…you have to have ___ of them…not one, but ___

A

TWO

105
Q

When the protein folds, if there are two cystine’s that effectively end up in each others faces…a chemical reaction can happen, known as an ________ reaction.

A

oxidation

106
Q

All oxidations remove ________.

A

hydrogen

107
Q

You remove hydrogen…and that is one product. Then you have those two sulfur atoms which are ________ bonded together, through _______!

A

covalently, oxidation

108
Q

Two cystine’s in a protein can become covalently bonded…and this is referred to as a _______ ______

A

disulfide bond/disulfide bridge

109
Q

Which proteins have this feature?

A

It’s those proteins that leave the cell.

110
Q

When a cell makes protein…it’s for one of two reasons. What are those two reasons?

A

1) Either the cell requires that protein for it’s own functioning…in which the proteins stays in the cell to do its job
2) The protein leaves the cell, to perform its function elsewhere
* Two possibilities, stays or leaves.**

111
Q

It is those proteins that LEAVE the cell that often have this _______ _______.

A

disulfide bridge

112
Q

What’s the logic? Why would proteins that have disulfide bridges leave the cell?

A

Extra stabilization. If for example, an enzyme, leaves their cell of origin, it’s a GOOD IDEA for those enzymes to have some additional…BONDING. Yeah, to hold their structure in an unforgiving environment.
So that’s the logic, extra stabilization for proteins that could need that.

113
Q

If a protein has multiple polypeptides, we say that it has _______ structure.

A

quaternary

114
Q

How is quaternary structure held together?

A

ALL FOUR WEAK INTERACTIONS, just like tertiary structure

115
Q

Again, what is quaternary structure?

A

Two or more polypeptides coming together to form a final protein

116
Q

One more interaction may stabilize quaternary structure, what might that be?

A

Disulfide bridge

117
Q

The fourth level is also stabilized by ________ _______. Possibly…possibly…namely in proteins that what?

A

disulfide bridges. Proteins that leave the cell

118
Q

_____-_____ have disulfide bridges stabilizing their tertiary structure, as well as their quaternary structure.

A

anti-bodies

119
Q

Primary structure:
Secondary structure:
Tertiary structure:
Quaternary structure:

A

Primary structure: the order of the amino acids in the protein
Secondary structure: localized folding of the polypeptide…either into coils or into sheets
Tertiary structure: the entire polypeptide folded
Quaternary structure: perhaps…multiple polypeptides coming together

120
Q

Folding happens SPONTANEOUSLY…based on the ______ _______ of that protein.

A

primary structure

121
Q

Why is pH important to establish the shape of the protein?

A

It will dictate the charges. Some amino acids are acidic, some are basic…whether the amino acids lose protons or receive them depends upon the ambient pH

122
Q

If you should boil a protein, what might happen?

A

The weak interactions will not resist the thermal energy of the environment

123
Q

What’s it called when all the weak interactions break and the protein unfolds?

A

Denaturation

124
Q

If the protein is in an environment where there’s other protein..also denatured…it will not _______ properly.

A

renature

125
Q

When you boil an egg…you boil it…what happens to the protein? They denature…and proceed to do what?

A

Stick to other proteins. If you denature every protein by boiling…they will then stick to other protein.
It will be very difficult to uncoil an egg because there’s so many protein..so many proteins that they stick to one another

126
Q

Which protein effectively “hugs” the other protein as it’s being made by the ribosome, allowing it to fold without interacting with other proteins within the cell.

A

chaperon proteins

127
Q

What are the two types of nucleic acid?

A

DNA and RNA

128
Q

Where do you find them?

A

In the nucleus

129
Q

What are the monomers of nucleic acids?

A

Nucleotides

130
Q

How many different nucleotides are there?

A

Four

131
Q

You join nucleotides by dehydration…become covalently joined. The chain is called a ___________.

A

polynucleotide

132
Q

The covalent bond that results from dehydration is called a _____________ ______.

A

phosphodiester bond

133
Q

Two main functions of nucleic acids…
Polynucleotides…
Nucleotides…

A

Polynucleotides store information

Nucleotides store energy

134
Q

What three parts makeup the nucleotide?

A

5 carbon sugar, phosphate group, nitrogenous base

135
Q

Which sugar lacks the oxygen?

A

Deoxyribose

136
Q

If you have one ring, six atoms, you are called a _________.

A

pyrimidine

137
Q

If you have two rings, fused…one has six atoms, the other has five atoms…then you’re called a _______.

A

purine

138
Q

What are the pyrimidines?

A

Thymine, cytosine, and uracil

139
Q

What are the purines?

A

Adenine and guanine

140
Q

The nitrogenous base is joined at carbon number…?

A

one

141
Q

The phosphate of one nucleotide is joined to the _____ of the last nucleotide.

A

sugar

142
Q

So this chemistry means we’re always going to have a ________ on one end and a ____ on the other.

A

phosphate, sugar

143
Q

So the end with the phosphate is called the ____ prime end, because…

A

five prime end because there phosphate is joined to the carbon number five prime

144
Q

The end with the sugar is called the ____ prime end, because…

A

out of respect to this three prime hydroxyl

145
Q

What does the polynucleotide backbone consist of?

A

A repeating pattern of phosphate-sugar.

Two distinct ends…a five prime end and a three prime end. Held together covalently by phosphodiester bonds.

146
Q

What are the three differences between DNA and RNA?

A

1) The sugar - DNA, deoxyribose. RNA, ribose
2) The bases - Thymine only found in DNA. Uracil only found in RNA
3) The chain - DNA, two chains (helix). RNA, one chain

147
Q

Explain: DNA –> RNA –> Protein

A

This is simply saying that making a protein requires two steps.
The DNA or gene is first copied into the other type of nucleic acid called RNA. It’s the RNA that is decoded.
DNA copied into RNA.
THIS IS NOT A CHEMICAL REACTION. NOT CONVERTING DNA TO RNA. JUST COPIED
Likewise, the RNA remains in tact. It is NOT converted into protein. IT’S DECODED.

BSC 2010 - Biology I (9 decks)

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