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Biochemistry Flashcards

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1
Q

Amino Acids

A

molecule with 4 groups attached to the central carbon (alpha carbon).

1) amino group
2) carboxylic acid group
3) hydrogen atom
4) R group

the r group determines the function of the amino acid.

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2
Q

Amino group

A

a functional group composed of NH3+

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3
Q

Carboxylic acid

A

a functional group composed of COOH

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4
Q

Zwitterions

A

molecules that contain both positive and negative charges on the same molecule

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5
Q

Alpha carbon

A

central carbon atom of an amino acid, bonded to the amino group, carboxyl group, and R group

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6
Q

Peptide bond

A

bond between each amino acid in a protein; catalyzed by the ribosome; forms primary structure of a protein

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7
Q

Amide bond

A

another term for peptide bond; has partial double bond character which limits rotation of the constituent groups

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8
Q

Primary structure

A

the string of amino acids connected by peptide bonds, and is defined solely by the identity of amino acids within it

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9
Q

secondary structure

A

formed through the hydrogen bonding interactions between atoms forming the backbone of the protein chain; includes alpha helices and beta sheets

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10
Q

tertiary structure

A

structure that arises from interactions between the side chains of different amino acids

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11
Q

quaternary structure

A

interactions between different protein subunits that make up a protein with more than one subunit

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12
Q

hydrophobic affect

A

a consequence of nonpolar and polar interactions; in an aqueous environment, hydrophobic residues will be attracted to each other, while they will also be repelled by the polar aqueous environment

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13
Q

protein folding

A

the process through which a protein is organized (or folded) into its proper secondary and tertiary structures

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14
Q

denaturing

A

the process through which a protein is unfolded or loses its proper 3D structure

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15
Q

chaperones

A

helper proteins that assist in folding denatured proteins back into their native state

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16
Q

Cytoskeleton

A

composition of proteins and macromolecules that provides structure for the cell; primarily composed of actin and tubulin

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17
Q

Extracellular matrix

A

composition of proteins and macromolecules that provide structure for tissue; primarily composed of collagen, elastin, and keratin

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18
Q

Actin

A

the most abundant protein in eukaryotic cells; actin monomers assemble into long polymers known as microfilaments that possess positive and negative polarity

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19
Q

Myosin

A

a motor protein that works with actin in a crossbridge cycle to contract muscle cells

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20
Q

Tubulin

A

structural monomer that assembles into heterodimers of alpha-tubulin and beta-tubulin to form microtubules

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21
Q

Collagen

A

helical fiber made of three interwoven strands and composes a large portion of the extracellular matrix in connective tissue

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22
Q

Elastin

A

provides structure to the rest of our body; when stretched, elastin fibers become more linear in shape while still preserving the cross-linked structure of the extracellular matrix

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23
Q

Keratin

A

not directly localized in the extracellular matrix, but provides cells with needed structure and stability to protect our bodies, and acts as a hard barrier from the outside world

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24
Q

Kinesin

A

a motor protein that travels towards the positive end of microtubules (towards the periphery of the cell)

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25
Q

Dynein

A

a motor protein that travels towards the negative end of microtubules (towards the nucleus of the cell)

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26
Q

GPCR

A

G-protein coupled receptor; a transmembrane signal-transducing protein system

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27
Q

G-protein

A

a trimeric protein, consisting of an alpha, beta, and gamma subunit. The alpha subunit is responsible for hydrolyzing GTP in the G-protein, while the beta and gamma subunits can have other functions in the cell

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28
Q

Pores

A

transmembrane structures embedded within the cell membrane that allows small, polar molecules to move down their respective gradients; one such example is aquaporin, which facilitates the diffusion of water

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29
Q

Ion channels

A

allows charged ions to diffuse through the cell membrane; some ion channels can be gated with ligand- or voltage-dependent sensors

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30
Q

Active transporters

A

proteins that can move ions and large molecule against their concentration gradient; rely on ATP hydrolysis for energy to move cargo

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31
Q

Peptide hormones

A

hormones that are peptides or proteins (shown below); transduce signals between organ systems and circulate in the bloodstream

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32
Q

HPG axis

A

hypothalamic-pituitary-gonadal axis; describes the sequential stimulation of hormones from the hypothalamus to the reproductive gonads

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33
Q

Innate immune system

A

nonspecific defenses against pathogens and foreign material our bodies encounter

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34
Q

Adaptive immune system

A

provides us more specific defenses against particular antigens; antibodies are key to this adaptive response

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35
Q

Variable region

A

includes paratopes on an antibody; sequences of polypeptide that provide the ability to recognize foreign substances and flag them as invasive

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36
Q

Constant region

A

region on an antibody important for recruiting other antibodies or immune system cells to help destroy the antigens

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37
Q

Catalyst

A

a substance that speeds up the rate of a reaction without being consumed itself

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38
Q

Biological catalyst

A

a molecule (can be protein or nucleic acid) that speeds up the rate of a biochemical reaction without being consumed itself

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39
Q

Activation energy

A

the input energy required to initiate a chemical reaction

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40
Q

Kinetics

A

how quickly a reaction converts reactants to products

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41
Q

Reaction rate

A

the rate at which reactants are consumed OR the rate at which products are formed

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42
Q

Regeneration

A

the ability of enzymes to reform and engage in multiple catalytic cycles

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43
Q

Lock-and-key model

A

an enzyme-substrate binding theory that poses the substrate as a “key” that fits perfectly into the enzymatic “lock” without changing conformations

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44
Q

Induced fit model

A

an enzyme-substrate binding theory that poses the substrate and enzyme undergo slight conformational changes upon binding to one another

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45
Q

One-letter amino acid code

A

a one-letter code that defines an amino acid (e.g., K is lysine)

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46
Q

Three-letter amino acid code

A

a three-letter code that defines an amino acid (e.g., Lys is lysine)

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47
Q

Michaelis-Menten

A

a plot that measures reaction velocity versus an increasing concentration of substrate while holding the enzyme concentration constant

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48
Q

Reaction velocity

A

the speed at which a certain concentration of enzymes convert substrate to product

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49
Q

Vmax

A

the maximum speed at which a certain concentration of enzymes can convert substrate to product

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50
Q

Km

A

the substrate concentration at ½ vmax and also corresponds to affinity between the enzyme and substrate

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51
Q

Saturation

A

the point at which additional substrate does not produce an increase in reaction velocity because the enzymes are already working as fast as they can

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52
Q

Catalytic efficiency

A

describes the efficiency of an enzyme by incorporating how fast the enzyme is working (kcat) and how well the enzyme can bind substrate (Km) using the following expression: kcat / Km

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53
Q

Lineweaver-Burk

A

a double reciprocal of the Michaelis-Menten plot in which (1/reaction velocity) is plotted against 1/[S]

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54
Q

Competitive inhibition

A

an inhibitor competes with substrate binding to the active site, resulting in an unchanged vmax and an increased Km

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55
Q

Uncompetitive inhibition

A

an inhibitor binds to the enzyme-substrate complex, resulting in a decreased vmax and a decreased Km

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56
Q

Mixed inhibition

A

an inhibitor binds to both the enzyme alone and the enzyme-substrate complex, resulting in a decreased vmax and an increased or decreased Km

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57
Q

Noncompetitive inhibition

A

a subclass of mixed inhibition in which an inhibitor binds to the enzyme alone 50% of the time and the enzyme-substrate complex 50% of the time, resulting in a decreased vmax and an unchanged Km

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58
Q

Cofactor/coenzyme

A

binds to the enzyme’s active site and assists in catalyzing the reaction

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59
Q

Prosthetic group

A

a cofactor or coenzyme that binds extremely tightly to the enzyme

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60
Q

Holoenzyme

A

an enzyme with its cofactors and/or coenzymes

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61
Q

Apoenzyme

A

an enzyme without its cofactors and/or coenzymes

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62
Q

Post-translational modification

A

the covalent addition of a functional group or atom to an enzyme

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63
Q

Allosteric sites

A

a site distant from the active site that can be used as a point of regulation

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64
Q

Allosteric activators

A

binds to an enzyme’s allosteric site and activates the enzyme

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65
Q

Allosteric inhibitors

A

binds to an enzyme’s allosteric site and inhibits the enzyme

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66
Q

Zymogens

A

inactive enzyme forms that must be cleaved in order to be activated

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67
Q

Feedback regulation

A

the control of flux through biological pathways by using positive and negative regulation

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68
Q

Negative regulation

A

the enzyme’s product or a product further down the pathway can inhibit the enzyme and decrease flux through the pathway

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69
Q

Feed-forward (positive) regulation

A

an enzyme’s substrate or a product upstream in the enzyme’s pathway can activate the enzyme to increase flux through the pathway

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70
Q

Cooperativity

A

the binding of substrate to a multi-subunit protein affects the binding of subsequent substrates

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71
Q

Hill’s coefficient

A

a term that describes whether a multi-subunit protein is not cooperative (=1), positively cooperative (>1), or negatively cooperative (<1)

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72
Q

Sigmoidal

A

an S-shaped curve that is characteristic of cooperative behavior

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73
Q

Double helix

A

structure of DNA; two strands of DNA wrap around each other and form a twisted ladder pattern

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74
Q

Nucleotides

A

bonded DNA pairs that include adenine, guanine, cytosine, and thymine

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75
Q

Purines

A

aromatic nitrogenous bases with two rings; include adenine and guanine

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76
Q

Pyrimidines

A

aromatic nitrogenous bases with one ring; include cytosine and thymine

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77
Q

Watson-Crick base pairing

A

bonding rules under which adenine exclusively bonds with thymine and cytosine exclusively bonds with guanine

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78
Q

Sugar phosphate backbone

A

a repeating pattern of pentose sugar and phosphate groups bonded together; in DNA, the sugar is deoxyribose

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79
Q

G-C content

A

a measure of the percentage of nucleotide bases that contain guanine or cytosine in a fragment of DNA; high G-C content indicates higher melting point

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80
Q

Melting point

A

the temperature at which hydrogen bonds between base pairs are disrupted and the two strands of DNA are dissociated

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81
Q

Chargaff’s rules

A

state that the ratio of purine nucleotides to pyrimidine nucleotides in DNA is 1 to 1. In fact, the ratio of guanine nucleotides to cytosine nucleotides and the ratio of adenine nucleotides to thymine nucleotides are also each 1 to 1

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82
Q

Antiparallel

A

describes the two strands of DNA that run in opposite directions (5’ to 3’ and 3’ to 5’)

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83
Q

Origin of replication

A

a sequence rich in adenine-thymine bonds at which the replisome is initially formed

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84
Q

Helicase

A

an enzyme that unzips DNA strands during replication

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85
Q

DNA topoisomerase

A

an enzyme that relaxes the coiling in DNA by making selective cuts in the phosphate backbone and repairing them

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86
Q

DNA primase

A

an enzyme that creates a short strand of RNA that is complementary to DNA

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87
Q

DNA polymerase

A

an enzyme that replaces RNA primers, continuously adds nucleotides to the daughter strand, and conducts proofreading during DNA synthesis

88
Q

Ligase

A

an enzyme that seals sequences of nucleotides together during DNA synthesis

89
Q

Leading strand

A

the template strand used during DNA synthesis, running in the 3’ to 5’ direction

90
Q

Lagging strand

A

the strand complementary to the lagging strand; runs in the 5’ to 3’ direction

91
Q

Okazaki fragments

A

short sequences of DNA that are produced in spurts along the lagging strand

92
Q

Mismatch repair

A

occurs in the G2 phase of the cell cycle to correct any leftover errors from synthesis

93
Q

Transcription

A

the process by which an RNA transcript is created from existing DNA; RNA polymerase creates RNA strands that are complementary to the template strand of DNA

94
Q

Translation

A

describes how proteins are created from synthesized RNA transcripts; occurs in ribosomes

95
Q

Retroviruses

A

RNA viruses that use a special enzyme known as a reverse transcriptase to create a double-stranded DNA molecule out of the RNA they possess

96
Q

Epigenetic modifications

A

physical changes on DNA that amplify or silence the expression of certain genes; include histone acetylation and deacetylation and DNA methylation and demethylation

97
Q

Imprinting

A

occurs when an inherited copy of a gene is silenced due to epigenetic modifications passed on from parent to offspring

98
Q

Nucleosome

A

a protein octamer known as a histone, and DNA

99
Q

Histone acetyltransferases (HATs)

A

enzymes that transfer acetyl groups to histones and function in the upregulation of gene expression

100
Q

DNA methyltransferases

A

enzymes that add methyl groups to DNA and function in the deactivation of genes

101
Q

Euchromatin

A

chromatin that is relatively relaxed and can easily be read

102
Q

Heterochromatin

A

chromatin that is relatively dense and cannot easily be read

103
Q

X inactivation

A

involves cells randomly silencing an X-chromosome, either from the mother or father, during early female development

104
Q

Cancer

A

characterized by uncontrolled cell proliferation, lack of response to apoptotic signals (e.g. immunity to programmed cell death), and migration to different tissues in the body

105
Q

Oncogene

A

a gene that causes cancer when mutated

106
Q

Tumor suppressor gene

A

a gene that inhibits cell cycle progression and marks cells for apoptosis

107
Q

Nondisjunction

A

failure of pairs of chromosomes to separate during meiosis; can result in chromosomal disorders such as trisomy 21 and Klinefelter syndrome

108
Q

Ribonucleic acid (RNA)

A

a form of nucleic acid that typically exists in single-stranded form; contains ribose in its phosphate backbone

109
Q

Nucleic acid

A

molecules composed of nucleotides, chained together by a sugar phosphate backbone

110
Q

Nucleotides

A

the basic building blocks of nucleic acids; includes adenine, guanine, cytosine, thymine, and uracil

111
Q

Uracil

A

uridine monophosphate; a nucleotide taking the place of thymine in RNA

112
Q

Transcription:

A

the first step of the Central Dogma; results in the transcription of genetic information from DNA’s nucleotides to RNA nucleotides

113
Q

RNA polymerase

A

an enzyme that serves as a translator to synthesize an RNA transcript

114
Q

Splicing

A

a form of posttranscriptional processing in which introns are removed and exons are ligated together

115
Q

mRNA

A

messenger RNA; carries information from the nuclear DNA to ribosomes for translation

116
Q

Alternative splicing

A

a phenomenon in which one gene can give rise to multiple proteins by retaining different combinations of RNA exons

117
Q

Translation

A

the second step of the Central Dogma; occurs in ribosomes and results in the translation of RNA nucleotides into polypeptides

118
Q

Codons

A

sequences of three nucleotides; complementary to anticodons

119
Q

tRNA

A

transfer RNA; each tRNA contains a unique anticodon loop and an amino acid it is charged with

120
Q

Degeneracy

A

a phenomenon that results in multiple nucleotide codons encoding the same amino acid

121
Q

Wobble effect

A

non-Watson Crick base pairing that allows for weak binding between the third nucleotide of the codon in mRNA and anticodon in tRNA

122
Q

rRNA

A

ribosomal RNA; main component of ribosomes; combines with special proteins to create the small and large subunits of the ribosome

123
Q

snRNPs

A

small nuclear ribonucleoproteins; complexes of small nuclear RNA (snRNA) and proteins that combine with pre-mRNA to form a spliceosome

124
Q

Fischer projection

A

a two-dimensional representation of a molecule that gives three-dimensional information; represents sugars in D- and L-configurations

125
Q

Haworth projection

A

a representation of the cyclic forms of sugars; represents sugar in their ⍺-anomer or β-anomer form

126
Q

Aldose

A

a sugar with an aldehyde group (-CHO); cyclization forms a hemiacetal

127
Q

Ketose

A

a sugar with a ketone group (-CO); cyclization forms a hemiketal

128
Q

Mutarotation

A

the ability of monosaccharides in aqueous solution to undergo spontaneous cyclization

129
Q

Pyranose

A

a sugar that contains a six-membered ring; e.g., glucose

130
Q

Furanose

A

a sugar that contains a five-membered ring; e.g., fructose

131
Q

Benedict’s reagent

A

reacts in the presence of aldoses to form a red copper precipitate

132
Q

Tollen’s reagent

A

reacts in the presence of aldehydes to form a silver, mirrorlike precipitate

133
Q

Glycogen

A

a polysaccharide used by the body as its primary form of carbohydrate-based energy storage

134
Q

Signaling lipids

A

specialized lipids involved in signal transduction pathways, or the passing of information between and within cells; include steroids and fat-soluble vitamins

135
Q

Amphipathic

A

referring to the presence of both hydrophobic and hydrophilic regions on the same molecule

136
Q

Phospholipids

A

the primary component of the phospholipid bilayer of the cell; contain a hydrophilic, polar phosphate head group joined through an ester linkage to a hydrophobic nonpolar fatty acid tail

137
Q

Triglycerides

A

lipids composed of a glycerol head group and three fatty acid tails; primarily used for energy storage and feature prominently in metabolism.

138
Q

Micelles

A

spherical structures composed of a single layer of fatty acids arranged in their lowest energy state

139
Q

Liposome

A

an empty spherical vesicle enclosed by a bilayer

140
Q

Fluid mosaic model

A

describes the structure of cell membrane components within the “sea” of relatively fluid phospholipids that make up the bilayer

141
Q

Passive transport

A

occurs when a molecule moves from an area of high concentration to an area of low concentration and no energy is required

142
Q

Active transport

A

occurs when a molecule is moving from an area of low concentration to an area of high concentration and the process requires energy; can be further categorized into primary and secondary active transport

143
Q

Amylase

A

an enzyme that begins to hydrolyze large polymeric carbohydrates into monosaccharides and disaccharides

144
Q

Glucagon

A

hormone secreted by α-cells when blood glucose levels are low

145
Q

Insulin

A

hormone released by β-cells when blood glucose levels are high

146
Q

Glycogenesis

A

pathway through which glucose is polymerized into glycogen

147
Q

Glycogenolysis

A

pathway through which glycogen is deconstructed into glucose monomers

148
Q

Glycolysis

A

metabolic process by which a glucose molecule is converted into two molecules of pyruvate

149
Q

Phosphofructokinase 1

A

catalyzes the rate-limiting step of glycolysis

150
Q

G3P dehydrogenase

A

an enzyme that catalyzes the reversible conversion of glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate, which yields two molecules of NADH per glucose molecule

151
Q

Phosphoglycerate kinase

A

an enzyme that catalyzes the reversible conversion of 1,3-bisphosphoglycerate into 3-phosphoglycerate; generates one ATP per molecule of phosphoglycerate

152
Q

Pyruvate kinase

A

an enzyme that catalyzes the irreversible conversion of phosphoenolpyruvate into pyruvate; generates one ATP per molecule of phosphoenolpyruvate

153
Q

Lactic acid cycle

A

serves to regenerate NAD⁺ under anaerobic conditions, so glycolysis can continue

154
Q

Pyruvate dehydrogenase

A

an enzyme catalyzes the irreversible conversion of pyruvate into acetyl-CoA and generates NADH and carbon dioxide as byproducts

155
Q

Citric acid cycle

A

pathway that takes place in the mitochondrial matrix and produces NADH and FADH2 from one molecule of acetyl-CoA

156
Q

Isocitrate dehydrogenase

A

an enzyme that catalyzes the rate-limiting step of the TCA cycle

157
Q

Electron transport chain

A

consists of the reactions catalyzed by four membrane-bound complexes located in the mitochondrion’s inner membrane; serves to transfer electron equivalents from NADH and FADH2 to oxygen and create a proton gradient

158
Q

Proton-motive force

A

the proton gradient established between the intermembrane space and the mitochondrial matrix

159
Q

Oxidative phosphorylation

A

a process that transfers energy that was released through the oxidation of NADH and FADH2 into a new bond: one between ADP and an inorganic phosphate molecule, resulting in the production of ATP

160
Q

Chemiosmosis

A

the spontaneous flow of hydrogen ions through the F₀ component of ATP synthase

161
Q

Decoupling agents

A

molecules that inhibit the synthesis of ATP by destroying the proton gradient present in the mitochondrion

162
Q

Pentose phosphate pathway

A

produces NADPH that can be used in fatty acid synthesis and carbohydrate products that can be used in glycolysis or nucleotide synthesis

163
Q

Palmitic acid

A

a 16-carbon saturated fatty acid

164
Q

Citrate shuttle

A

a shuttle that moves citrate to the cytoplasm from the mitochondrion

165
Q

Oxaloacetate shuttle

A

a shuttle that moves oxaloacetate to the mitochondrion from the cytoplasm

166
Q

Beta oxidation

A

the breakdown of fatty acids into acetyl-CoA

167
Q

Carnitine acyltransferase I

A

an enzyme in the carnitine shuttle that adds carnitine to fatty acids before entry into the mitochondria

168
Q

Biotin

A

vitamin B₇; an essential cofactor for fatty acid breakdown

169
Q

Ketone bodies

A

small, water-soluble compounds that can be dissolved in the bloodstream; used by the brain during ketogenesis

170
Q

Urea cycle

A

converts ammonium into urea, a compound that can be safely transported to the kidneys for excretion through urine

171
Q

Gel electrophoresis

A

an experiment used to separate different components of a mixture based on their size and charge

172
Q

Cathode

A

negatively charged side of a gel

173
Q

Anode

A

positively charged side of a gel

174
Q

PAGE (polyacrylamide gel electrophoresis)

A

the material that often makes up the gel in gel electrophoresis

175
Q

Charge density

A

the amount of charge per area of a molecule

176
Q

SDS-PAGE

A

a specific type of gel electrophoresis where sodium dodecyl sulfate (SDS) is used to denature proteins and add a constant distribution of negative charges

177
Q

Denature

A

to unfold a protein

178
Q

Reducing SDS-PAGE

A

similar to SDS-PAGE although a reducing agent is used to break disulfide bridges

179
Q

Disulfide bond

A

a covalent bond formed between two cysteine residues

180
Q

Native-PAGE

A

a type of gel electrophoresis that does not denature the proteins, which will retain their secondary, tertiary, and quaternary structure

181
Q

Isoelectric focusing

A

a type of gel electrophoresis used to separate proteins by their isoelectric point (pI)

182
Q

Isoelectric point (pI)

A

the pH at which the net charge of a protein is zero

183
Q

Northern blot:

A

a technique used after gel electrophoresis to identify a specific RNA strand

184
Q

Reporter

A

an enzyme, fluorescent or radioactive compound, or other substance that sends a readily observed or measurable signal that is used to report the presence of another substance that is difficult to visualize

185
Q

Southern blot

A

a technique used after gel electrophoresis to identify a specific DNA strand

186
Q

Western blot

A

a technique used after gel electrophoresis to identify a specific protein

187
Q

Primary antibody

A

the first antibody that binds a target protein

188
Q

Secondary antibody

A

an antibody with a fluorescent label or conjugated enzyme that binds to the primary antibody

189
Q

Sanger method

A

a technique used to determine the sequence an of DNA strand

190
Q

Primer

A

a small, single-stranded piece of DNA or RNA that binds to the 3’ end of a piece of DNA and is necessary for the initiation of DNA replication by DNA polymerase

191
Q

Reverse transcriptase

A

an enzyme that produces a strand of DNA that is complementary to an RNA strand

192
Q

Polymerase chain reaction (PCR)

A

a method used to generate a large number of copies of a piece of DNA

193
Q

cDNA library

A

a collection of host cells, usually bacteria, that is used to store genes of interest

194
Q

Indirect ELISA

A

a type of ELISA where you immobilize an antigen and determine if an antibody binds to it, followed by a secondary antibody linked to a reporter enzyme to determine if binding has occurred

195
Q

Direct ELISA

A

a type of ELISA where you immobilize an antigen and determine if an antibody binds to it, and a reporter enzyme linked to the antibody tells you if binding has occurred

196
Q

Sandwich ELISA

A

a type of ELISA where you determine the concentration of an antigen in solution by immobilizing an antibody, adding the antigen, and then adding additional antibody that is linked to a reporter enzyme

197
Q

Bacterial transformation

A

the process of a bacteria absorbing genetic information from its surroundings and inserting it into its genome

198
Q

Plasmids

A

circular pieces of DNA

199
Q

Restriction enzymes/endonucleases

A

enzymes that cut specific palindromic sequences of DNA

200
Q

Centrifugation

A

separating substances by spinning them at high speeds

201
Q

Pellet

A

the solid region at the bottom of a centrifuged tube containing dense substances

202
Q

Supernatant

A

the liquid region at the top of a centrifuged tube containing less dense substances

203
Q

Chromatography

A

a technique used to isolate a substance of interest from a larger mixture of molecules

204
Q

Mobile phase

A

the liquid containing your substance of interest in chromatography

205
Q

Stationary phase

A

the immobilized part of the column that will attract your substance of interest in chromatography

206
Q

Gel filtration (size exclusion) chromatography

A

a type of chromatography where you use beads with many small paths as your stationary phase to separate contents of a mobile phase by size

207
Q

Ion-exchange chromatography

A

a type of chromatography where you use a positively or negatively charged stationary phase to separate contents of a mobile phase by charge

208
Q

Anion-exchange chromatography

A

a form of ion-exchange chromatography that attracts negatively charged molecules

209
Q

Cation-exchange chromatography

A

a form of ion-exchange chromatography that attracts positively charged molecules

210
Q

Elute

A

breaking the interaction between your substance of interest and the stationary phase so that your substance of interest exits the column

211
Q

Affinity chromatography

A

a type of chromatography where you isolate a specific substance from the mobile phase by using a stationary phase that contains something with a high affinity for your substance of interest

212
Q

Isomerase

A

Catalyzes an isomerization reaction, which is an intramolecular rearrangement of bonds in a molecule.

example: An enzyme that converts a cis double bond into a trans double bond

213
Q

Ligase

A

Catalyzes the joining of two molecules.

example: An enzyme that seals the gap between two adjacent Okazaki fragments

214
Q

Transferase

A

Catalyzes the transfer of a functional group from one molecule to another molecule.

example: A kinase that adds a phosphate group from ATP to a protein substrate

215
Q

Lyase

A

Catalyzes the breaking of a molecule without the use of water.

example: An enzyme that breaks a bond between two nucleotides without using water

216
Q

Hydrolase

A

Catalyzes the breaking of a molecule by adding water.

example: An enzyme that breaks a bond between two nucleotides by adding water.

217
Q

Oxidoreductase

A

Catalyzes the transfer of electrons between molecules.

example: An enzyme that transfers extra electrons from an NADH electron carrier to a protein substrate.

MCAT (6 decks)

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