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Dental Admisssions Test > Biology > Flashcards

Biology Flashcards

1
Q

Any substance that takes up space and has mass

A

Matter

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2
Q

Substance that has specific chemical and physical properties

A

Element

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3
Q

The smallest unit of matter that still retains all the chemical properties of an element

A

Atom

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4
Q

Whenever two or more atoms join together

A

Molecules

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5
Q

Contain carbon atoms arranged as ling chains or rings, and these carbon atoms tend to bond with hydrogen, oxygen, or nitrogen atoms

A

Organic molecules

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6
Q

Strong attractive forces that hold atoms within a molecule

A

Intramolecular forces

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7
Q

________ exist between molecules, and they are far weaker than ______

A

Intermolecular forces; intramolecular forces

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8
Q

_________ forces are significant because they determine physical properties

A

Intermolecular forces

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9
Q

Molecules that have the potential of binding to other identical molecules through chemical reactions

A

Monomers

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10
Q

Formation of polymers

A

Polymerization

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11
Q

Substances that have a large number of units (monomers) bonded together

A

Polymers

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12
Q

Macromolecules that contain carbon, hydrogen, and oxygen atoms

A

Carbohydrates

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13
Q

_______ contain roughly one carbon atom per water molecule

A

Carbohydrates

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14
Q

“One sugar”

A

Monosaccharides

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15
Q

________ have a ratio of precisely one carbon per water mater molecule

A

Monosaccharides

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16
Q

Monosaccharides will usually have anywhere from ____ to ____ carbon atoms

A

3 to 7

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17
Q

Five carbon sugars

A

Pentoses

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18
Q

Six carbon sugars

A

Hexoses

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19
Q

Whenever a linear pentose or hexose sugar converts to a ring structure, it forms a _______

A

Hydroxyl (-OH) functional group

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20
Q

A hydroxyl group that points down creates a ______ sugar

A

Alpha

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21
Q

A hydroxyl group that points up creates a ______ sugar

A

Beta

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22
Q

“Two sugars”

A

Disaccharides

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23
Q

Disaccharides form when two monosaccharide monomers join together via

A

Dehydration reaction (also known as condensation reaction)

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24
Q

Water adds to a covalent bind and splits monomers apart

A

Hydrolysis reaction

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25
Q

The bond formed between a carbohydrate and another molecule

A

Glycosidic bond

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26
Q

Contains one glucose and one fructose

A

Sucrose

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27
Q

Contains one galactose bound to one glucose

A

Lactose

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28
Q

Contains two glucose monosaccharides linked together

A

Maltose

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29
Q

Long polymers of monosaccharides

A

Polysaccharides

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30
Q

A crucial storage polysaccharide in plants, containing many glucose monomers in linear forms as well as branched forms

A

Starch

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31
Q

Linear plant starch that contains a-1,4-glycosidic bonds

A

Amylose

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32
Q

Branched form of plant starch that contains a-1,4-glycosidic bonds and a-1,6-glycosidic bonds

A

Amylopectin

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33
Q

A critical storage polysaccharide found in humans that contains many glucose monomers. It is more branched than amylopectin

A

Glycogen

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34
Q

Contains a-1,4-glycosidic bonds and a lot of a-1,6-glycosidic bonds. It is primarily stored in liver and muscle cells.

A

Glycogen

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35
Q

It is broken down to release glucose monosaccharides to cells that need energy

A

Glycogen

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36
Q

Structural polysaccharide found in plant cell walls, wood, and paper

A

Cellulose

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37
Q

A glucose polymer that contains b-1,4-glycosidic bonds

A

Cellulose

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38
Q

Cellulose forms linear strands that pack together in parallel, where adjacent strands are held together by

A

Hydrogen bonds

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39
Q

Humans cannot digest cellulose; instead, it passes through our digestive tracts as

A

Fiber

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40
Q

Virtually identical to cellulose, and it is found in the cell walls of fungi and in the robust exoskeleton of insects

A

Chitin

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41
Q

Chitin is a polymer of _______. One of the hydroxyl groups in each glucose molecule gets replaced by a functional group containing nitrogen

A

N-acetylglucosamine

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42
Q

All of the proteins that are exposed by the cell form a

A

Proteome

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43
Q

All proteins contain polymers called _______. Each polypeptide contains monomeric subunits called ________.

A

Polypeptides; Amino acids

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44
Q

Alpha carbon center which is attached to an amino group, hydrogen atom, and carbonyl group

A

Amino acid

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45
Q

At physiological PH in the human body, the amino group tends to be _______ and the carbonyl group tends to be ________

A

Protonated; Deprotonated

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46
Q

Variable group in amino acids

A

R group

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47
Q

Every amino acid monomer is attached to its neighbor via

A

Peptide bonds

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48
Q

Amino acids form peptide bonds with each other via

A

Dehydration/condensation reactions

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49
Q

A peptide bond is called _______ when it involves amino acids

A

An amide bond

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50
Q

Amine bonded to a carboxylic acid

A

Amide bond

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51
Q

Polypeptides are said to have both

A

N-terminus (amino) and C-terminus (carbonyl)

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52
Q

Specific order or sequence of a peptide, which is determined by DNA genes. All proteins have this.

A

Primary structure

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53
Q

Folds that occur in a polypeptide chain due to intermolecular interactions between atoms of the polypeptide backbone

A

Secondary structure

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54
Q

The amino acid structural features other than the R-group. The secondary structure does not involve R-group atoms

A

Polypeptide backbone

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55
Q

Most common type of intermolecular force that leads to secondary protein structure

A

Hydrogen bonding

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56
Q

Hydrogen bonds can only occur between

A

Hydrogen, fluorine, oxygen, or nitrogen

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57
Q

Two of the most common secondary protein structures

A

Beta-pleated sheets and alpha helices

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58
Q

Three dimensional structure of larger polypeptide chains, which occurs as a result of interactions between R-groups of the various amino acids

A

Tertiary structure

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59
Q

Ionic bonding, hydrogen bonding, dipole-dipole interactions, and London dispersion (van der Waal) forces

A

R-group interactions

60
Q

Another critical R-group interaction that can cause tertiary structure

A

Hydrophobic interactions

61
Q

Contain sulfur in its R-group and can create disulfide bonds with each other

A

Cysteine

62
Q

Tertiary structure interactions are usually not covalent; disulfide binds are an _______ to this

A

Exception

63
Q

Refers to large proteins that have multiple subunits which come together by the same general interactions used in creating tertiary structure

A

Quaternary structure

64
Q

While there are multiple polypeptide chains in a quaternary structure, we consider the entire structure to be

A

One protein

65
Q

_________ and ________ components are fundamental to a protein because they relate to the function of that protein

A

Structural; compositional

66
Q

Common tetramer protein with primary, secondary, tertiary, and quaternary structure

A

Hemoglobin

67
Q

whenever a functional protein loses its higher order
structures

A

Protein denaturation

68
Q

Protein denaturation can occur by

A

excess temperature, chemicals, pH changes,
and radiation, to name a few

69
Q

all of the information necessary for the
folding of those proteins (some denatured proteins) is contained directly within

A

The amino acid sequence

70
Q

Molecules that increase reaction rates

A

Catalysts

71
Q

Catalysts do not affect the __________ of a reaction

A

Spontaneity

72
Q

________ are not used up by the reactions they manipulate,
meaning the reaction does not change them in any way.

A

Catalysts

73
Q

Catalysts ________ activation energies to speed reactions.

A

Lower

74
Q

the amount of energy a chemical reaction requires to progress

A

Activation energy

75
Q

catalysts do not affect the energy of

A

Reactants or products

76
Q

biological, globular (usually) protein catalysts that speed up specific forward and reverse reactions by lowering their activation energies.

A

Enzymes

77
Q

_________ only change the energy of the transition state, not of the reactants or products.

A

Enzymes

78
Q

Enzymes catalyze reactions by binding to reactant molecules, which are called

A

Substrates

79
Q

An enzyme’s __________ is where substrates bind.

A

Active site

80
Q

An enzyme’s ___________ measures how efficient an enzyme is in converting substrate to product

A

Specificity constant

81
Q

Non-protein molecules that assist enzymes in the reactions they manipulate.

A

Cofactors

82
Q

a ribonucleic acid (RNA) molecule that is capable of acting as an enzyme by changing the speed of reactions as they progress from reactants to products.

A

Ribozyme

83
Q

Coenzymes are organic cofactors, and these usually include things like

A

Vitamins

84
Q

Enzymes that are bound to their cofactor

A

Holoenzymes

85
Q

An enzyme that is lacking (not bound to) its cofactor.

A

Apoenzyme

86
Q

Cofactors that tightly/covalently bind to their enzyme in a holoenzyme are known as

A

Prosthetic groups

87
Q

A form of enzyme regulation, where inhibitors compete with substrates for active sites.

A

Competitive inhibition

88
Q

Adding more substrate will only increase the speed of catalysis until all active sites are occupied

A

Enzyme saturation

89
Q

when an inhibitor binds to the allosteric site of an enzyme – a different location that is not the active site of enzyme catalysis.

A

Noncompetitive inhibition

90
Q

We cannot outcompete allosteric inhibitors by adding more substrate, which is why they are known as ____________________. The rate of enzyme catalysis is unaffected by
increasing the substrate concentration.

A

Noncompetitive inhibitors

91
Q

_________ store energy, provide insulation, contribute to cell membranes, and lead to the synthesis of critical hormones.

A

Lipids

92
Q

a small, organic alcohol molecule that has three carbons and three hydroxyl groups

A

Glycerol

93
Q

a long hydrocarbon tail attached to a carboxylic acid.

A

Fatty acid

94
Q

Fats are produced by

A

Dehydration/condensation reactions

95
Q

The hydroxyl groups of the glycerol molecule react with the carboxylic acids of fatty acids to produce

A

An ester linkage

96
Q

The addition of water to a fat’s ester bonds will break the fatty acids off the glycerol backbone by

A

A hydrolysis reaction

97
Q

If a fatty acid tail has no double bonds, it is

A

Saturated

98
Q

At room temperature, saturated fats are

A

Solid

99
Q

__________ fatty acids can possess one or more double bonds because they do
not have full hydrogen saturation

A

Unsaturated

100
Q

Fatty acids with one double bond

A

Monounsaturated

101
Q

Fatty acids with two or more double bonds

A

Polyunsaturated

102
Q

create kinks in the fatty acid chain because the hydrogens associated with the double bond remain on the same side.

A

Cis-unsaturated fatty acids

103
Q

cis-unsaturated fats tend to be ________ at room temperature

A

Liquid

104
Q

________ have hydrogens that go to opposite sides of the double bond, which makes them pack together tightly

A

Trans-unsaturated fatty acids

105
Q

In nature, transunsaturated fats are

A

Rare

106
Q

__________ is performed to give cheaper oils (like canola oil) the desirable room-stable properties of more expensive products, like butter.

A

Industrial hydrogenation

107
Q

___________ are a unique type of lipid (fat) found in cell membranes

A

Phospholipids

108
Q

Each phospholipid has a three-carbon glycerol backbone attached to ___________ and ___________.

A

One phosphate group; Two fatty acid tails

109
Q

Looks virtually the same as a phospholipid; however, these contain a carbohydrate molecule in place of the phosphate group.

A

Glycolipid

110
Q

A class of lipid that makes up around 30-50% of a eukaryotic cell membrane.

A

Cholesterol

111
Q

contains four hydrocarbon rings and is also amphipathic, which allows it to interact with various regions of the phospholipid bilayer.

A

Cholesterol

112
Q

Several factors influence the fluidity of a membrane, including ___________, ____________, and _____________ in the phospholipid fatty acid tails.

A

temperature, cholesterol, and the degree of unsaturation

113
Q

The ability of cholesterol to interact with the cell membrane is beneficial to the overall _______ of the membrane.

A

Fluidity

114
Q

maintains some distance between the phospholipids when it is cold, but it also holds the phospholipids together when it starts to get hot.

A

Cholesterol

115
Q

When it is cold, cells _________ fatty acid unsaturation in their membranes to ________ rigidity and maintain fluidity

A

Increase; decrease

116
Q

This organ makes cholesterol

A

Liver

117
Q

A starting material for vitamin D and a precursor to bile acids

A

Cholesterol

118
Q

The most common steroid precursor (meaning it can be made into steroids)

A

Cholesterol

119
Q

Fused structures composed of three six-membered rings (cyclohexanes) and a five membered ring (cyclopentane)

A

Steroids

120
Q

Contain a coat of phospholipids, cholesterol, and proteins. They also have a lipid core that contains more cholesterol and triglycerides.

A

Lipoproteins

121
Q

Low density of proteins. They are generally considered to be unhealthy because they deliver cholesterol to peripheral tissues via the bloodstream

A

Low-density lipoproteins (LDLs)

122
Q

High density of proteins. They are generally considered to be healthy because they take cholesterol away from peripheral tissues and deliver it to the liver. Once at the liver, the cholesterol can be used to make bile acids, which aid in fat absorption as was mentioned above. They are the “good” cholesterol.

A

High-density lipoproteins (HDLs)

123
Q

Contain long fatty acids that are connected to monohydroxy alcohols by ester linkages.

A

Waxes

124
Q

Long fatty acid carbon chains that have conjugated double bonds and six-membered rings at each end. They function as pigments that provide color to plants and animals.

A

Carotenoids

125
Q

Pentose (five-carbon) sugar attached to a nitrogenous base.

A

Nucleosides

126
Q

__________ is a pentose sugar attached to a nitrogenous base and a single phosphate group. Nucleic acids are polymers made of this.

A

Nucleotides

127
Q

A and G nitrogenous bases are known as

A

Purines

128
Q

C, U, and T are known as

A

Pyrimidines

129
Q

Purine molecules have ____ rings, while pyrimidines have just ____ ring

A

Two; One

130
Q

RNA nucleotides have _______ sugars with a hydroxyl group on the 2’ (“two prime”) carbon.

A

Ribose

131
Q

DNA nucleotides are slightly different because they have __________ sugars, meaning the 2’ carbon does not contain oxygen.

A

Deoxyribose

132
Q

RNA is _________ (less stable) than DNA because of its 2’ hydroxyl group.

A

More reactive

133
Q

Phosphate groups attach to the nucleotide sugar at the

A

5’ carbon

134
Q

The 5’ phosphates of one nucleotide connect to the __________ of another nucleotide in nucleic acid polymers.

A

3’ hydroxyl

135
Q

Create the sugar-phosphate backbone of nucleic acid polymers.

A

Phosphodiester bonds

136
Q

5’ end has a free __________ group, while the 3’ end has a free _________ group.

A

Phosphate; Hydroxyl

137
Q

Add to growing nucleic acid polymers by losing two phosphates (as pyrophosphate) to form a phosphodiester bond with the free hydroxyl at the 3’ end of the polymer - this is how nucleic acid polymerization occurs.

A

Nucleoside triphosphates

138
Q

Adenine and thymine (or uracil) make ______ H-bonds, while cytosine and guanine make ______ H-bonds.

A

Two; Three

139
Q

The cell theory

A
  1. All lifeforms have one or more cells
  2. The cell is the most simple unit of life
  3. All cells come from other cells
140
Q

Modern cell theory

A

All life is composed of one or more cells, where cells are the basic structural, functional, and organizational unit of life. Moreover, it says all cells come from pre-existing, living cells via cell
division.

141
Q

The cell theory does not apply to ______ because they are not living cells.

A

viruses

142
Q

Says that information flows from DNA to RNA to proteins. In other words, RNA is made from DNA, and proteins are made from RNA.

A

Central dogma of genetics

143
Q

The main implication of the central dogma of genetics is that information cannot
travel from _______________, or from __________________.

A

protein to protein; proteins to nucleic acids

144
Q

There is a particular case where information can travel from protein to protein. _________ are misfolded proteins that cause other proteins to misfold as well, destroying their function in the process.

A

Prions

145
Q

RNA world hypothesis

A

says that the Earth’s “primordial soup” had a lot of RNA nucleoside triphosphates, which made phosphodiester bonds with each other to create short strands of RNAs. As the strands grew longer and longer, they became more and more stable.

  1. RNA can store genetic information like DNA
  2. RNA can catalyze chemical reactions like proteins

Dental Admisssions Test (1 decks)

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