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Biology 2311-- Fall 2022 > Exam 1 > Flashcards

Exam 1 Flashcards

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1
Q

What are the four major classes of organic molecules in living organisms?

A

Carbohydrates, lipids, proteins, and nucleic acids

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2
Q

What is an important characteristic of covalent bonds?

A

They store a lot of energy

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3
Q

What are hydrocarbons?

A

Molecules consisting of carbon and hydrogen atoms

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4
Q

Are hydrocarbons polar or nonpolar?

A

Nonpolar, and when functional groups are added, they confer chemical properties to the molecule.

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5
Q

When are triple bonds found in hydrocarbons?

A

Only in two-carbon hydrocarbons such as ethyne

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6
Q

When are single and double bonds found in hydrocarbons?

A

In linear and ring hydrocarbons

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7
Q

What are some general structures of hydrocarbons?

A

Linear unbranched chain, linear branched chain, or a structure with one or more rings

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8
Q

Match the bond type to the molecule: single, double, triple and ethane, ethene, and ethyne

A

Ethane- single, ethene- double, ethyne- triple

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9
Q

Which functional groups are most commonly found in biological reactions?

A

Hydroxyl, carbonyl, carboxyl, amino, phosphate, and sulfhydryl groups, which are linked by covalent bonds to other atoms in the molecule (usually represented by R)

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10
Q

Are lipids polar or nonpolar?

A

Primarily nonpolar and water-insoluble

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11
Q

List the three common types of lipid molecules and their function

A

Neutral lipids- stored and used as an energy source
Phospholipids- form cell membranes
Steroids- serve as hormones regulating cellular activities

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12
Q

True or false: neutral lipids have no charged groups (nonpolar)

A

True

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13
Q

What are the two types of neutral lipids?

A

Oils (liquid at biological temperatures) and fats (semisolid)

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14
Q

What is a fatty acid? Is it polar or nonpolar?

A

A fatty acid has a single hydrocarbon chain with a carboxyl (COOH) group at one end. The carboxyl group gives organic molecules acidic properties because the -OH group releases the H as a proton in aqueous solutions, turning it into an ionized form. Fatty acids are nonpolar.

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15
Q

How are triglycerides formed?

A

Formed through a process called dehydration synthesis between 3-carbon glycerol (an alcohol) and three fatty acid side chains. A covalent bond called the ester linkage forms between the COOH fatty acid and the OH of glycerol, which eliminates the polar group of glycerol and forms a nonpolar molecule

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16
Q

What is the hydroxyl group and what are some of its properties/applications?

A

Hydroxyl (–OH) can be found in molecules like alcohols. It is polar and hydrogen bonds with water, which facilitates dissolving of organic molecules. It allows an alcohol to link with other molecules through dehydration synthesis reactions.

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17
Q

Where is the ester linkage in triglycerides located?

A

Between the O in glycerol and the C in the fatty acid

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18
Q

How many molecules of water are formed through formation of triglycerides?

A

3

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19
Q

What roles do triglycerides play?

A

Serve as energy reserves in animals because they can store more than 2x the calories per gram as carbohydrates.
A layer of fatty tissue under skin acts as insulation in mammals and birds.
Triglycerides also help make bird feathers waterproof

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20
Q

What is a typical number of carbons in a fatty acid?

A

14 to 22; as chain length increases, the fatty acid becomes less water soluble and more oily

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21
Q

What is a saturated fatty acid? Where are they found?

A

A fatty acid that binds the maximum number of hydrogen atoms, meaning only single bonds exist between carbon atoms. These fatty acids can be found in solid animal fats such as butter

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22
Q

What are mono and polyunsaturated fats?

A

Fatty acids with one double bond are mono; acids with 2 or more are polyunsaturated.

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23
Q

Why are unsaturated fatty acids usually fluid at biological temperatures?

A

The presence of double bonds causes “bends” in the structure that mean the molecules cannot pack as tightly together.

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24
Q

Which are healthier- saturated or unsaturated fats?

A

Unsaturated fats.

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25
Q

What are examples of unsaturated fats?

A

Vegetable oils.

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26
Q

Is stearic acid saturated or unsaturated? (no bends)

A

Saturated

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27
Q

Is oleic acid saturated or unsaturated?

A

Unsaturated

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28
Q

What are trans fats?

A

Trans fats are formed through adding hydrogen to vegetable oil, which makes the liquid into a solid fat. This is called hydrogenation. Trans fats are also found in products such as milk, butter, cheese, meats, etc. in trans fats. In the process of hydrogenation, cis fatty acid configurations are transformed into trans fat configurations and this gives them more qualities of saturated fat but they are not a good source of energy and they are harder to process

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29
Q

Why are trans fats bad?

A

They raise the level of LDL cholesterol in the blood, which increases the risk of heart disease.

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30
Q

How can LDLs contribute to heart disease?

A

Atherosclerosis occurs due to buildup of plaques in coronary arteries; these plaques form from a buildup of excess cholesterol.

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31
Q

What is the structure of phospholipids?

A

Glycerol, 2 fatty acids as the nonpolar tails, a phosphate group as part of the polar head

Order goes polar unit–phosphate group– glycerol then the two nonpolar fatty acids

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32
Q

What type of fatty acid composes the tails?

A

One saturated, one unsaturated

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33
Q

What is the function of phospholipids?

A

They help form cell membranes; the polar ends are exposed to water and their nonpolar ends collect in a region that excludes water

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34
Q

What is a micelle?

A

Micelles are lipid molecules that orient with their polar head toward water and their nonpolar tails away from water in a circle

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35
Q

What is the structure of a phospholipid bilayer?

A

2 molecules thick- polar groups face water and hydrocarbon chains form nonpolar, hydrophobic regions in the interior

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36
Q

What are waxes?

A

Fatty acids combine with long-chain alcohols or hydrocarbon structures to form waxes, which are harder and less greasy than fats

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37
Q

What are the functions of waxes?

A

Help animals keep skin, hair, or feathers protected, lubricated, and pliable; plants also secrete waxes that form a protective exterior layer to reduce water loss and resist infection.

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38
Q

What are steroids?

A

Lipids with structures based on 3 hexane carbon rings and 1 pentane carbon ring. They control development, behavior, and many internal biochemical processes. The sex hormones that control differentiation of sexes and sexual behavior is one example.

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39
Q

What makes sterols unique?

A

They have a single polar OH group at one end of the ring framework and a nonpolar hydrocarbon chain at the other end

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40
Q

What role does cholesterol play?

A

It is an important part of animal cell membranes; sterols called phytosterols also occur in plant cell membranes

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41
Q

What are some structural differences between estradiol (an estrogen) and testosterone?

A

Estradiol has 3 double bonds in first ring an an OH group. In the pentane ring it has a CH3 and an OH group. Testosterone has an =O instead of -OH and an extra CH3 between the first two rings

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42
Q

What is the name for CH3?

A

Methyl

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43
Q

What do chlorophylls and carotenoids do?

A

They are pigments that absorb light and help convert it to chemical energy in plants

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44
Q

True or false: lipid groups combine w/ carbs to form glycolipids and w/ proteins to form lipoproteins with important strucural and functional roles in cell membranes

A

true

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45
Q

Define isomers

A

Molecules with the same molecular or empirical formula but different molecular structures

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46
Q

What are structural isomers?

A

Same chemical formula but the arrangement of atoms are different, such as glucose and fructose

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47
Q

What are stereoisomers?

A

They differ in how the groups are attached, auch as in mirror image molecules and L and D sugars

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48
Q

What is the carbonyl group?

A

Has C double bonded to O, usually found in aldehydes and ketones. Molecules with carbonyl groups are major building blocks for carbohydrates and participate in the reactions supplying energy for cellular activities.

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49
Q

Carboxyl

A

C double bonded to O and bonded to OH, gives organic molecules acidic properties because -OH releases the hydrogen as a proton in aqueous solutions, converting it into an ionized form. Found in carboxylic acids.

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50
Q

Amino

A

NH2, acts as an organic base by accepting a proton. Found in amines and amino acids.

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51
Q

Phosphate

A

P bonded to 3 O and double bonded to an O, found in organic phosphates such as glyceraldehyde-3 phosphate and nucleic acids. They react as weak acids because one or both OH groups release H. Can also bridge two organic building blocks. Added to or removed from molecules as part of reactions that conserve or release energy or to alter activity.

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52
Q

Sulfhydryl

A

Found in thiols. -SH. Easily converted into a covalent linkage where it loses hydrogen atoms. Two sulfhydryl groups form a disulfide linkage.
R-SH+ HS-R = R-S-S-R+ 2H + 2e-

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53
Q

Define enatiomers

A

Mirror image molecules

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54
Q

Are glucose and fructose structural or steroisomers?

A

Structural

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55
Q

Are galactose and glucose stereo or structural isomers?

A

Stereo

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56
Q

Describe and illustrate the dehydration synthesis process

A

In dehydration synthesis, water is removed and largr molecules are formed. The OH bonds join together to form a water molecule, leaving an O to join the monomers.

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57
Q

Describe and illustrate the hydrolysis process

A

Hydrolysis involves the breakdown of large molecules through the addition of water. Polymers are broken down into monomers through the addition of water.

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58
Q

What is a carbohydrate?

A

Molecules with a 1:2:1 ratio of carbon, hydrogen, and oxygen. The empirical formula is CH2O.

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59
Q

What is a key factor about C-H bonds?

A

They hold a lot of energy

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60
Q

How many C atoms do monosaccharides have?

A

3-7

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61
Q

What are two monosaccharides called?

A

Disaccharide

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62
Q

What are polysaccharides?

A

Carbohydrate polymers with more than 10 linked monosaccharide monomers

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63
Q

What function do carbohydrates serve?

A

They can act as energy storage molecules; glycogen and starch are some examples. They can also be structural saccharides, such as cellulose.

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64
Q

What are the simplest carbs?

A

Monosaccharides

65
Q

T or F: All monosaccharides occur in linear form

A

True

66
Q

Give some examples of common hexoses. Why do we care about these?

A

Glucose, fructose, and galactose. these 6 carbon sugars play important roles

67
Q

Why are isomers important in sugars

A

Enzymes can recognize different structural and steroisomers of the basic 6-carbon skeleton which alloes it to distinguish between glucose, fructose, and galactose.

68
Q

If a monosaccharide has 3 or 5 carbons, what is it called?

A

Triose and pentose.

69
Q

How are glucose rings formed?

A

Monosaccharides with 5+ carbons can fold back through an interaction between two functional groups. The hydroxide on the 5th carbon combines with the carbonyl group on the first carbon, crearing C OH2.

70
Q

Distinguish alpha and beta glucose.

A

Alpha= below the plane, beta= above the plane. They are enatiomers (mirror images)

71
Q

How are disaccharides formed?

A

Monosaccharides covalently synthesized via dehydration.

72
Q

How is maltose formed?

A

A glycosidic bond between two alpha-glucose molecules with oxygen as a bridge between the 1 carbon and 4 carbon creating an alpha 1->4 linkage

73
Q

How is sucrose formed?

A

Alpha 1-2 linkage between glucose and fructose.

74
Q

Draw structures of glucose, fructose, and galactose

A

Use slides

75
Q

How is lactose formed?

A

beta 1-4 linkages between galactose and glucose.

76
Q

What polysaccharide do plants use for energy?

A

Starch such as amylose, which is formed from alpha 1-4 glucose lincages which creates a coiled structure

77
Q

What do animals use for energy?

A

Glycogen, which is formed from glucose alpha 1-4 chains and side branches are linked by alpha 1-6 linkages (side chain starts on third linear glucose)

78
Q

What do plants use for structural support?

A

Cellulose, which is made from glucose units joined end to end by beta 1-4 linkages. Thousands of cellulose chains line up in an arrangement reinforced by H bonds between the chains to form cellulose microfibrils in plant cells.

79
Q

What do arthropods and fungi use for structural support

A

chitin, which contains glucose and nitrogen groups. It uses beta 1-4 linkages.

80
Q

What functional group do ketones and aldehydes fit in?

A

Carbonyl

81
Q

Distinguish ketones and aldehydes

A

Ketones have a C=O connected to two R groups, while Aldehydes have a C=O connected to an R and an H

82
Q

Polymer is to nucleic acid as monomer is to:

A

Nucleotide

83
Q

What is the name of the bond that connects nucleotides?

A

Phosphodiester

84
Q

What are the components of a nucleotide?

A

Nitrogenous base, 5-carbon sugar, and a phosphate group

85
Q

What is the 5-carbon sugar in a deoxyribonucleotide and in a ribonucleotide?

A

deoxyribose and ribose

86
Q

What are the purines?

A

adenine, guanine

87
Q

what are the pyrimidines?

A

cytosine, uracil, thymine

88
Q

Is it purines or pyrimidines that have two rings?

A

Purines

89
Q

What is a nucleoside?

A

structures that only have a nitrogenous base and a 5 carbon sugar

90
Q

What are nucleotides in terms of nucleosides?

A

Nucleoside phosphates

91
Q

What are some examples of nucleotides?

A

ATP, ADP, AMP (3,2,1 phosphate groups respectively)

92
Q

Describe some structural characteristics of uracil

A

one carbon ring with two carboxyl groups

93
Q

Structural characteristics of thymine

A

One ring, two carboxyl groups, and a methyl group

94
Q

Structural characteristics of cytosine

A

Amino group and carboxyl group

95
Q

Structural characteristics of adenine

A

purine so two rings, amino group

96
Q

Structural characteristics of guanine

A

Two rings, amino and carboxyl group

97
Q

How do you distinguish between deoxyribose and ribose?

A

Look at the 2’ carbon- either H or OH will be bonded depending on whether ribose or deoxyribose

98
Q

Where do the phosphate bonds occur in nucleotides?

A

Phosphate groups bond to the 5’ carbon in the sugar

99
Q

Describe the phosphodiester bond

A

5’ Ch2-o-p-o-c (hydrolysis reaction); a bridging phosphate group between the 5’ and 3’ of next carbon

100
Q

Describe the structure of DNA

A

the sugar phosphate backbone consists of alternating sugars and phosphates where 5’ connects with phosphate group to 3’ of next sugar; in the other strand this same thing occurs in opposite direction.

101
Q

How do nucleotides pair up?

A

A-T or A-U in RNA and C-G

102
Q

How many bonds between A and T and C and G?

A

2 and 3 respectively

103
Q

Describe how each nucleotide bonds to eachother

A

CNC from hexane face eachother; for AT it is NHO and NHN in order; for GC it is OHN NHN NHO

104
Q

Can one nucleotide chain determine another?

A

Yes, that of its partner chain in the double helix

105
Q

Can RNA fold back on itself and create hybrid nucleic acids with DNA?

A

Yes, this is where uracil comes into play

106
Q

What does Atp do?

A

Main energy currency of cell

107
Q

NAD+ and FAD+

A

main electron carriers

108
Q

Describe the process of DNA replication

A
  1. Parent strand with 2 complementary strands of base paired nucleotides
  2. Two strands unwind from eachother
  3. Each old strand serves as a template for addition of new ones
  4. New and old strands join together, creating two new exact copies of old one
109
Q

List the functions of proteins

A

Structural support, enzymes, movement, transport, recognition and receptor molecules, regulation of protein and DNA, hormones, antibodies, toxins, and venoms.

110
Q

What monomers are proteins composed of?

A

Amino acids

111
Q

What functional groups do amino acids contain?

A

Amino (NH2) and carboxyl (COOH) groups

112
Q

Give the function an example of a structural support protein

A

Microtubule fibers and microfilament fibers inside cells, collagen, and cell wall proteins of plant cells

113
Q

Examples and function of enzymatic proteins

A

Increase the rate of biological reactions; DNA polymerase, rubisco, digestive enzymes

114
Q

Membrane transport proteins

A

Speed up transport across cell membranes; ion transporters move ions like Na+ and K+ into the cells, aquaporins, glucose transporters

115
Q

Motile proteins

A

Produce cellular movements; myosin acts on microfilaments to produce muscle movements; kinesin acts on microtubules involved in cell division

116
Q

Regulatory proteins

A

Promote or inhibit the activity of other cellular molecules. Nuclear regulatory proteins turn genes on or off to control the activity of DNA; protein kinases add phosphate groups to other proteins to modify activity.

117
Q

Receptor proteins

A

Hormone receptors bind hormones at the cell surface or within cells and trigger cellular responses; cellular adhesion molecules help hold cells together

118
Q

Hormonal proteins

A

Carry regulatory signals between cells; insulin regulates sugar levels; growth hormones regulate cell division and growth

119
Q

Defensive proteins

A

Defend against invading molecules and organisms; antibodies recognize and bind and eliminate foreign bodies

120
Q

Storage proteins

A

Hold amino acids and other substances in storage forms; ovalbumin is a storage protein of eggs and apoplipoproteins hold cholesterol for transport

121
Q

How many amino acids and how many classes of amino acids are there?

A

20 amino acids split into five classes based on side groups: nonpolar, polar, charged, negatively charged, and positively charged amino acids

122
Q

Why is cysteine an important amino acid?

A

Cysteine has a CH2-SH side group, which contains a sulfhydryl side group which can produce disulfide linkages that help form the 3D shape of the protein.

123
Q

How is proline different?

A

It has a ring structure that includes the central carbon atom. The central carbon binds to a -COOH and =NH (imino) group on the other side

124
Q

Can R groups interact with other amino acids and atoms?

A

Yes

125
Q

How can amino acids act as acids or bases?

A

The amino group can be basic by accepting a H+, and carboxyl can be acidic by donating a H+

126
Q

What is the bond between amino acids called?

A

Peptide bonds, which form polypeptides (the subunit of proteins)

127
Q

How is a peptide bond formed?

A

Dehydration synthesis between amino of one acid and carboxyl of the other

128
Q

What are the N and C terminal ends of a polypeptide chain?

A

The C terminal is the carboxyl side and new amino acids are only added to this side. The N terminal is the amino side.

129
Q

List the nonpolar amino acids

A

Alanine, valine, isoleucine, leucine, glycine, phenylalanine, tryptophan, methionine, proline (AVLIG FWMP)

130
Q

List the uncharged polar amino acids

A

cysteine, serine, threonine, tyrosine, asparagine, glutamine (CS TYNQ)

131
Q

List the negatively charged (acidic) polar amino acids

A

aspartic acid and glutamic acid (DE)

132
Q

List the positiviely charged (basic) polar amino acids

A

Lysine, Arginine, Histidine (KRH)

133
Q

Glycine

A

nonpolar, R group is H

134
Q

Alanine

A

nonpolar, R group is methyl

135
Q

Phenylalanine

A

nonpolar, R group is CH2 and benzene

136
Q

Methionine

A

nonpolar, R group has methyl and sulfur

137
Q

Serine

A

uncharged, hydroxyl group attached to a CH2

138
Q

Threonine

A

uncharged, hydroxyl and methyl

139
Q

tyrosine

A

uncharged, benzene ring with a hydroxyl group

140
Q

glutamine

A

uncharged, 2 carbons then amino group attached to a carbon

141
Q

cysteine

A

SH group, uncharged

142
Q

glutamic acid

A

polar negative acidic, same structure as glutamine but instead of amino group, O-

143
Q

histidine

A

positive, basic, polar, pentane ring structure

144
Q

Describe the 4 levels of protein structure

A

Primary structure- unique sequence of amino acids forming the polypeptide
Secondary structure- produced by twists and turns of amino acid chain
Tertiary structure- overall 3D shape, formed by folding of amino acid chain with its secondary structure
Quaternary structure- formed from more than 1 polypeptide chain

145
Q

What is the importance of amino acid order? Give an example

A

Changing even one acid can completely alter the structure, function, and higher levels of structure; substitution of a single amino acid in hemoglobin creates sickle cell disease

146
Q

Describe secondary structures

A

formed from primary structure, alpha helix is twisted into right hand spiral and beta sheet zigzags in flat plane. Amino acid chemical groups extend outward from the spiral, helices form rigid, rod-like structures, stabilized by regularly spaced H bonds. hydrogen bonds stabilize sheets too.

147
Q

What is a random coil?

A

has an irregularly folded arrangement; they provide flexible sites that allow the secondary structures to fold back on themselves and can also act as hinges to move parts of proteins.

148
Q

describe tertiary structure

A

gives a protein its overall conformation; influenced by secondary structures, disulfide linkages, and hydrogen bonds. attractions between polar and nonpolar groups, etc. Determines a protein’s function, and arrangement and distribution of chemical groups determines chemical activity and solubility

149
Q

How do cysteine sulfide linkages form?

A

Oxidation of sulfhydryl groups

150
Q

What groups influence structure?

A

Basic, acidic, hydrophilic/phobic, sulfur containing

151
Q

What is protein denaturation?

A

Unfolding of proteins due to temp, ph, chemicals so that it loses structure and function. can be reversible for some proteins

152
Q

What did christian anfisen’s experiment do?

A

He took native ribonuclease and added chemicals that broke the 4 disulfide linkages present, then taking away the chemicals and reacting with oxygen in air reformed them with 95% recovert

153
Q

Chaperonins

A

guide proteins called chaperonins or chaperone proteins bind temporarily with new proteins and allow them to fold correctly. unfolded polypeptide enters chaperonin cylinder, then cap goes on top, creating an enclosure, then protein folds and cap comes off

154
Q

Quaternary structure

A

two or more polypetide chains- H-bonds, polar and polar, and disulfide; chaperonins allow for individual associations of amino acids

155
Q

Functional domains

A

Subdivisions of proteins; in proteins with multiple functions, individual functions are located in different domains, and domains with similar functions are found in different proteins.

156
Q

What are motifs?

A

3D arrangement of amino acid chains within and between domains produces highly specialized regions called motifs which have similar structures/sequences among proteins.

157
Q

Give an example of a protein with domains

A

DNA polymerase- has a dna polymerase site that assembles DNA and a site that corrects mistakes during assembly (exonuclease site)

158
Q

List protein combinations

A

link with lipids to form lipoproteins, found in membranes; link with carbs to form glycoproteins, which function as enzymes, antibodies, reception and recognition molecules, and extracellular supports. Link with nucleic acids to form nucleoproteins, which form structures like chromosomes.

Biology 2311-- Fall 2022 (12 decks)

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