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BIO 148 Exam 2

Question	Answer
The idea that the sequence of bases in DNA specifies the sequence of bases in an RNA molecule, which specifies the sequence of amino acids in a protein, is _______.	The Central Dogma
The direction of synthesis of an RNA transcript is _____.	5' —> 3'
What is the process called that converts the genetic information stored in DNA to an RNA copy?	Transcription
DNA does not store the information to synthesize which of the following?	Organelles
Transcription begins at a promoter. What is a promoter?	A site in DNA to which RNA Polymerase binds
What determines which base is to be added to an RNA strand during transcription?	Base pairing between the DNA template strand and the RNA nucleotides
Which of the following terms best describes the relationship between the newly synthesized RNA molecule and the DNA template strand?	Complementary
What happens to RNA polymerase II after it has completed transcription of a gene?	It is free to bind to another promoter and begin transcription.
Where does translation take place in a eukaryotic cell?	cytoplasm
Where does transcription take place in a eukaryotic cell?	nucleus
Which nucleic acid carries the information that used during translation to make a polypeptide?	mRNA
Which nucleic base pairs with codons in the mRNA during translation?	tRNA
The codon that is used to initiate translation is the _______.	start codon
Which of the following RNAs that are involved in translation was studied by evolutionary biologists and used to initially define the three domains of life (Bacteria, Archaea and Eukarya)?	rRNA
Which of the following bonds binds amino acids together during translation?	peptide bonds
The process of using the information in mRNA to synthesize a protein is ______.	translation
What is a stop codon?	A mRNA codon that signals the end of translation.
How can a molecule with these characteristics hold all the information required to build and maintain a cell?	The information in DNA is in a code form that is based on the sequence of bases.
Beginning within the nucleus, the first step leading to the synthesis of a polypeptide is _____.	transferring of information from DNA to messenger RNA
The redundancy of the genetic code is a consequence of ______.	having more codons than amino acids
During transcription, in which direction is (1) RNA synthesized and in which direction is (2) the DNA template "read"?	(1) 5'—>3' (2) 3'—>5'
Why are ribonucleoside triphosphates the monomers required for RNA synthesis rather than ribonucleoside monophosphates?	Ribonucleoside triphosphates provide the energy for polymerization
A promoter is ______.	a sequence in DNA that brings RNA polymerase near the site for transcription
How do the the 5' UTR (5' untranslated region) and 3' UTR (3' untranslated region) become part of the mRNA?	They are part of the transcribed region of genes.
Are the 5' UTR and 3' UTR part of introns or exons in the primary transcript?	exons
During RNA processing a(n) _____ is added to the 5' end of the RNA.	modified guanine nucleotide
During RNA processing a(n) _____ is added to the 3' end of the RNA.	a long string of adenine nucleotides
The RNA segments joined to one another by spliceosomes are _____.	exons
Translation occurs in the _____.	cytoplasm
Which statement is most accurate concerning the function(s) of the 5' cap and the 3' poly(A) tail of eukaryotic mRNAs?	Both structures are important for initiating translation and extending the lifespan of the mRNA.
What name is given to the process in which pre-mRNA is edited into mRNA?	RNA processing
Polypeptides are assembled from _____.	amino acids
RNA processing converts the RNA transcript into _____.	mRNA
During the elongation phase of translation, individual tRNAs move through the three sites of the ribosome in the following sequence _____.	A—>P—>E
Just prior to the formation of a new peptide bond, the tRNA attached to the polypeptide chain occupies the _______ site of the ribosome.	P
Why does cordycepin end transcription?	It lacks a 3' OH.
How did the A site of the ribosome get its name?	It is the site occupied by incoming aminoacyl tRNAs.
Where is the start codon located?	at the downstream end of the 5' untranslated region (UTR)
Which polymers are composed of amino acids?	Proteins
Which of the following is not attached to the central carbon atom in an amino acid?	An oxygen
Which part of an amino acid is always acidic?	Carboxyl functional group
Which monomers make up RNA?	Nucleotides
Which of the following statements about the formation of polypeptides from amino acids is true?	A bond forms between the carboxyl functional group of one amino acid and the amino functional group of the other amino acid.
True or false? Enzymes in the digestive tract catalyze hydrolysis reactions.	True
Which of the following correctly orders amino acids Asp, Tyr, and Val from most hydrophobic (on the left) to most hydrophilic (on the right)?	Val, Tyr, and Asp
Which of the following parts of an amino acid vary among different amino acids?	the side chain, or R group
Which class(es) of amino acids possess side chains that would be unable to form hydrogen bonds with water?	amino acids with nonpolar side chains
During protein synthesis, the peptide bond between amino acids is formed by the process of _____.	condensation
______ structure describes the order of amino acids in the peptide chain	Primary
_________ structure describes the basic three-dimensional structures, α-helices and β-sheets.	Secondary
______ structure results from individual proteins coming together to form multi-subunit protein complexes.	Quaternary
_______structure describes how the secondary structures come together to form an individual globular protein.	Tertiary
Proteins are polymers of _____.	Amino Acids
What type of bond joins the monomers in a protein's primary structure?	Peptide
The secondary structure of a protein results from _____.	Hydrogen Bonds
Tertiary structure is NOT directly dependent on _____.	Peptide bonds
In proteins, secondary, tertiary, and quaternary levels of structure depend on primary structure. Which of the following most accurately lists elements of any protein's primary, secondary, tertiary, and quaternary structure, in that order?	Amino acid sequence, hydrogen bonding between backbone groups, overall shape of a single polypeptide, and combinations of tertiary structures
Which of the following statements about protein primary structure is true?	Primary structure is produced by the unique sequence of amino acids in a protein.
The alpha-helix is a component of __________ protein structure.	secondary
The secondary structure of proteins results because of _____ bonding between atoms in the protein's backbone.	hydrogen
What two functional groups are present on every amino acid?	an amino group and a carboxyl group
By convention, biologists write the sequence of amino acids in a polypeptide in which direction?	amino- to carboxy-terminus
Where is the information that directs different polypeptides to fold into different shapes?	in the primary structure
What is an active site?	the position in an enzyme where substrates bind
Why are proteins not considered to be a good candidate for the first living molecule?	They cannot serve as a template for replication.
Nonpolar amino acid residues are typically found in the interior of globular proteins like trypsin. Which chemical force is most directly responsible?	Hydrophobic interactions
Which of these is exhibiting kinetic energy?	a space station orbiting Earth
"Conservation of energy" refers to the fact that _____.	energy cannot be created or destroyed but can be converted from one form to another
Chemical energy is a form of _____ energy.	potential
In your body, what process converts the chemical energy found in glucose into the chemical energy found in ATP?	cellular respiration
Which of these are by-products of cellular respiration?	heat, carbon dioxide, and water
The following reaction A --> B + C + heat is a(n) _____ reaction.	exergonic
A(n) _____ reaction occurs spontaneously.	exergonic
Which of these reactions requires a net input of energy from its surroundings?	endergonic
In cells, what is usually the immediate source of energy for an endergonic reaction?	ATP
The reaction ADP + P --> ATP is a(n) _____ reaction.	endergonic
The energy for an endergonic reaction comes from a(n) _____ reaction.	exergonic
What is the fate of the phosphate group that is removed when ATP is converted to ADP?	It is acquired by a reactant in an endergonic reaction.
What is energy coupling?	the use of energy released from an exergonic reaction to drive an endergonic reaction
What type of reaction breaks the bonds that join the phosphate groups in an ATP molecule?	hydrolysis
How do cells use ATP to raise the energy level of reaction substrates?	(b) The ADP part of ATP is bound to the substrate. (c) The terminal phosphate of ATP is bound to the substrate. Sometimes it's (b), sometimes (c).
Why is ATP a good source of energy for biological reactions?	Triphosphate chains are unstable.
A reaction is said to be unfavorable if ...	(b) the free energy change for the reaction is positive. (c) equilibrium favors the reactants, not the products.
The reaction A → B is unfavorable by itself, but through energy-coupling, cells can use ATP to convert A into B. How is this done?	The unfavorable reaction is replaced by two favorable reactions.
How do cells replace the energy-rich ATP that is destroyed in energy-coupled reactions?	(a) Chloroplasts use light energy to synthesize ATP. (b) Mitochondria synthesize ATP using energy that's released by oxidizing sugars and fats.
Which statement most accurately explains why ATP hydrolysis is highly exergonic?	There is a large drop in potential energy because charge repulsion is reduced
When ATP is hydrolyzed into ADP and inorganic phosphate, _____.	free energy is released
Consider a situation in which the enzyme is operating at optimum temperature and pH, and has been saturated with substrate. What is your best option for increasing the rate of the reaction?	Increase the enzyme concentration.
In general, enzymes are what kinds of molecules?	proteins
Enzymes work by _____.	reducing EA
What name is given to the reactants in an enzymatically catalyzed reaction?	substrate
As a result of its involvement in a reaction, an enzyme _____.	is unchanged
Enzymes speed up chemical reactions by ____.	decreasing the activation energy
How do current models of enzyme function differ from Fischer's lock-and-key model?	Rather than enzymes being rigid, we now believe they undergo an induced fit upon substrate binding.
An enzyme inhibitor that is roughly the same shape as the substrate and binds at the active site is termed a(n) _____ inhibitor.	competitive
Consider the two-step metabolic pathway: A—(enzyme 1)—>B—(enzyme 2)—>C How would inactivating enzyme 1 affect the concentrations of molecules A, B, and C relative to what they would be if the pathway were fully functional?	A would increase; B and C would decrease.
The polymerization of amino acids into a protein is an example of _____.	an anabolic pathway
How does pH affect enzyme-catalyzed reactions?	The concentration of protons affects the folded structure of the enzyme.
Compare and contrast competitive inhibition and allosteric regulation.	Both are mechanisms that regulate enzymes via noncovalent modifications. Both strategies depend on the concentration of the regulatory molecule. Both strategies are often referred to as a "reversible" modifications.
Which of the following scenarios would you predict to be responsible for activating this enzyme?	The sugar binds to the enzyme and changes the conformation of the active site.
Which term describes the degree to which an element attracts electrons?	Electronegativity
Which terms describe two atoms when they form a bond in which electrons are completely transferred from one atom to the other?	Anion and cation
Which of the following statements is true of the bonds in a water molecule?	Oxygen holds electrons more tightly than hydrogen does, and the net charge is zero.
Which of the following statements is not true of most cellular redox reactions?	A hydrogen atom is transferred to the atom that loses an electron.
What kind of bond is formed when lithium and fluorine combine to form lithium fluoride?	Ionic
Gaseous hydrogen burns in the presence of oxygen to form water: 2H2 + O2 → 2H2 O + energy Which molecule is oxidized and what kind of bond is formed?	Hydrogen, polar.
Redox reactions involve the gain or loss of _____.	electrons
Which statement is true for all redox reactions?	They involve the transfer of electrons.
In mitochondrial electron transport, what is the direct role of O2?	to function as the final electron acceptor in the electron transport chain
How would anaerobic conditions (when no O2 is present) affect the rate of electron transport and ATP production during oxidative phosphorylation? (Note that you should not consider the effect on ATP synthesis in glycolysis or the citric acid cycle.)	Both electron transport and ATP synthesis would stop.
Among the products of glycolysis, which compounds contain energy that can be used by other biological reactions?	pyruvate, ATP, and NADH
Which of these equations best summarizes photosynthesis?	6 CO2 + 6 H2O → C6H12O6 + 6 O2
The light reactions of photosynthesis use _____ and produce _____.	water ... NADPH
The long-accepted hypothesis that information in cells flows in one direction: DNA codes for RNA, which codes for proteins.	Central Dogma
stretch of DNA base pairs (and associated regulatory regions) that code for a protein	Gene
The process by which RNA is made from a DNA template.	Transcription
An RNA molecule that carries encoded information, transcribed from DNA, that specifies the amino acid sequence of a polypeptide.	mRNA
The process by which proteins and peptides are synthesized from messenger RNA.	Translation
Chains of amino acids folded into a specific 3D shape	Proteins
The set of all 64 codons and the particular amino acids that each specifies.	Genetic Code
A code in which a “word” of three letters encodes one piece of information. The genetic code is a triplet code because a codon is three nucleotides long and encodes one amino acid.	Triplet Code
A reading frame is one of three ways of reading a nucleotide sequence, where each “word” is three nucleotides long and there are no overlapping words or spaces between words. Important for understanding translation.	Reading Frame
An AUG sequence in mRNA where translation begins. AUG codes for the first amino acid of a protein and it sets the reading frame that the ribosome will use for translation	Start codon
One of three sequences mRNA (UAG, UGA, or UAA) that cause termination of translation.	Stop codon
Overall process by which the information encoded in genes is converted into an active product, most commonly a protein. Gene expression includes transcription and translation (as well as other post-translational processes beyond the score of this topic).	Gene Expression
The association between specific nitrogenous bases of nucleic acids stabilized by hydrogen bonding. Adenine pairs only with thymine (in DNA) or uracil (in RNA), and guanine pairs only with cytosine.	Complementary base pairing
The strand of DNA that RNA polymerase transcribes to create RNA. The template strand will be complementary to the RNA that is synthesized.	Template strand for transcription
The strand of DNA that is complementary to the template strand. Its sequence is the same as that of the mRNA that is produced by transcription, except that thymine in DNA corresponds to uracil in RNA.	Coding (non-template) strand
One of a class of enzymes that catalyze synthesis of RNA from ribonucleotides, using a DNA template	RNA Polymerase
The short DNA sequence in a gene to which RNA polymerase binds. The promoter determines exactly where transcription will start and in which direction transcription will proceed. All genes have a promoter.	Promoter
In genetics, opposite to the direction of transcription of a gene. For example, you could indicate that a certain DNA sequence is upstream of a gene.	Upstream of a gene
: In genetics, the same direction as transcription. For example, you could indicate that a certain DNA sequence is downstream of a gene.	Downstream of a gene
the process by which the primary RNA transcript is altered before leaving the nucleus to be translated. Includes addition of a 5’ cap, poly-A tail, and splicing.	RNA processing
: In eukaryotes, a newly transcribed messenger RNA molecule that has not yet been processed	Primary transcript
A chemical grouping, consisting of 7-methylguanylate and three phosphate groups that is added to the 5’ end of newly transcribed messenger RNA molecules.	5’ cap
In eukaryotes, a sequence of 100–250 adenine nucleotides added to the 3’ end of newly transcribed messenger RNA molecules	Poly-A tail
The process by which introns are removed from primary RNA transcripts and the remaining exons are connected together.	Splicing
region of a eukaryotic gene that is transcribed into RNA but is later removed, so it is not translated into a peptide or protein	Intron
A region of a eukaryotic gene that is translated into a peptide or protein	Exon
A sequence of three nucleotides in RNA that codes for a certain amino acid or that initiates or terminates protein synthesis.	Codon
A large complex structure that synthesizes proteins by using the genetic information encoded in messenger RNA strands. Consists of two subunits, each composed of ribosomal RNA and proteins.	Ribosome
A RNA molecule that forms part of the structure of a ribosome	rRNA
One of a class of RNA molecules that have an anticodon at one end and an amino acid binding site at the other. Each tRNA picks up a specific amino acid and binds to the corresponding codon in messenger RNA during translation.	tRNA
The sequence of three bases (triplet) in a transfer RNA molecule that can bind to a mRNA codon with a complementary sequence.	anticodon
covalent bond between two amino acids. Forms with the carboxyl group of one amino acid reacts with the amino group of another amino acid.	Peptide bond
A molecule consisting of adenine, a sugar, and three phosphate groups that can be hydrolyzed to release energy. Universally used by cells to store and transfer energy.	ATP
All the chemical reactions occurring in a living cell or organism	Metabolism
Any set of chemical reactions that breaks down larger, complex molecules into smaller ones, releasing energy in the process.	Catabolic pathway
Any set of chemical reactions that synthesizes larger molecules from smaller ones. Generally requires an input of energy.	Anabolic pathway
In cellular metabolism, the mechanism by which energy released from an exergonic reaction (commonly, hydrolysis of ATP) is used to drive an endergonic reaction.	Energetic coupling
the loss of electrons from an atom during a redox reaction, either by donation of an electron to another atom or by the shared electrons in covalent bonds moving farther from the atomic nucleus.	Oxidation
An atom's gain of electrons during a redox reaction, either by acceptance of an electron from another atom or by the electrons in covalent bonds moving closer to the atomic nucleus.	Reduction
tendency of an atom or molecule to attract electrons	Electronegativity
a common pathway for the production of ATP, involving transfer of electrons from compounds with high potential energy to an electron transport chain.	Cellular Respiration
Any chemical reaction that involves the transfer of one or more electrons from one reactant to another. Also called reduction-oxidation reaction	Redox reaction
Six-carbon monosaccharide whose oxidation in cellular respiration is the major source of ATP in animal cells.	Glucose
A series of 10 chemical reactions that oxidize glucose to produce pyruvate and ATP. Used by all organisms as part of fermentation or cellular respiration.	Glycolysis
oxidized and reduced forms on nicatinamide adenine dinucleotide . A nonprotein electron carrier.	NAD+/NADH
Production of ATP by transfer of a phosphate group from an intermediate substrate directly to ADP. Occurs in glycolysis and in the Krebs cycle.	Substrate level phosphorylation
Central compartment of a mitochondrion, which is lined by the inner membrane; contains the enzymes and substrates of the Krebs cycle and mitochondrial DNA.	Mitochondrial matrix
A large enzyme complex, located in the inner mitochondrial membrane, that is responsible for conversion of pyruvate to acetyl CoA during cellular respiration.	Pyruvate dehydrogenase
A series of eight chemical reactions that starts with citrate (citric acid, when protonated) and ends with oxaloacetate, which reacts with acetyl CoA to form citrate—forming a cycle that is part of the pathway that oxidizes glucose to CO2.	The Citric Acid (Kreb’s) Cycle
Oxidized and reduced forms, respectively, of flavin adenine dinucleotide. A nonprotein electron carrier that functions in the citric acid cycle and oxidative phosphorylation.	FAD/ FADH2
: Any set of membrane-bound protein complexes and smaller soluble electron carriers involved in a series of redox reactions in which the pot. energy of electrons transferred from reduced donors is decreased and used to pump protons across membrane.	Electron Transport chain
A soluble iron-containing protein that shuttles electrons between membrane-bound complexes in the mitochondrial electron transport chain.	Cytochrome
A large membrane-bound protein complex in chloroplasts, mitochondria, and some bacteria that uses the energy of protons flowing through it to synthesize ATP.	ATP synthase
The combined effect of a proton gradient and an electric potential gradient across a membrane, which can drive protons across the membrane. Used by mitochondria and chloroplasts to power ATP synthesis via the mechanism of chemiosmosis.	Proton motive force
An energetic coupling mechanism whereby energy stored in an electrochemical proton gradient (proton-motive force) is used to drive an energy-requiring process such as production of ATP.	Chemiosmosis
production of ATP molecules from the redox reactions of an electron transport chain.	Oxidative Phosphorylation
Referring to any metabolic process, cell, or organism that uses oxygen as an electron acceptor.	Aerobic respiration
Referring to any metabolic process, cell, or organism that uses an electron acceptor other than oxygen, such as nitrate or sulfate.	Anaerobic respiration
Catabolic pathway in which pyruvate produced by glycolysis is converted to ethanol or lactic acid in the absence of oxygen.	Fermentation
Any organism that can synthesize reduced organic compounds from simple inorganic sources such as CO2 or CH4. Most plants and some bacteria and archaea are autotrophs	Autotroph
Any organism that cannot synthesize reduced organic compounds and must obtain them from eating other organisms.	Heterotroph:
an organism that produces ATP through photosynthesis	Phototroph
organisms that obtain energy by the oxidation of electron donors in their environments	Chemotroph
The complex biological process that converts the energy of light into chemical energy stored in glucose and other organic molecules. Occurs in plants, algae, and some bacteria.	Photosynthesis
A chlorophyll-containing organelle that is bounded by a double membrane and in which photosynthesis occurs; found in most plant and algal cells. Also the location of amino acid, fatty acid, purine, and pyrimidine synthesis.	Chloroplast:
A flattened, membrane-bound vesicle inside a plant chloroplast that functions in converting light energy to chemical energy	Thylakoid
the space between the inner and outer thylakoid membranes	Intermembrane space
the interior space of the thylakoid	Thylakoid lumen
The fluid matrix of a chloroplast in which the thylakoids are embedded, this is the site where the Calvin cycle reactions occur	Stroma
stacks of thylakoids	Grana
A discrete packet of light energy; a particle of light.	Photon
The distance between two successive crests in any regular wave, such as light waves	Wavelength
The amount of light of different wavelengths absorbed by a pigment. Usually depicted as a graph of light absorbed versus wavelength	Absorption spectrum
Any of several closely related green pigments, found in chloroplasts and photosynthetic protists, that absorb light during photosynthesis.	Chlorophyll
Any of a class of accessory pigments, found in chloroplasts, that absorb wavelengths of light not absorbed by chlorophyll; typically appear yellow, orange, or red..	Carotenoids
Part of a photosystem, containing an array of chlorophyll molecules and accessory pigments, that receives energy from light and directs the energy to a central reaction center during photosynthesis.	Antenna complex
One of two types of units, consisting of a central reaction center surrounded by antenna complexes, that is responsible for the light-dependent reactions of photosynthesis.	Photosystem
An energetic coupling mechanism whereby energy stored in an electrochemical proton gradient (proton-motive force) is used to drive an energy-requiring process such as production of ATP.	Chemiosmosis
Referring to any process or reaction that produces oxygen.	Oxygenic
Production of ATP molecules using the energy released as light-excited electrons flow through an electron transport chain during photosynthesis. Involves generation of a proton-motive force during electron transport and its use to drive ATP synthesis.	Photophosphorylation
In photosynthesis, the set of light-independent reactions that use NADPH and ATP formed in the light-dependent reactions to drive the fixation of atmospheric CO2 and reduction of the fixed carbon, ultimately producing sugars.	The Calvin Cycle
A five-carbon compound that combines with CO2 in the first step of the Calvin cycle during photosynthesis.	RuBP
a permanent change in a sequence of DNA (from Topic 3)	Mutation
In genetics, referring to any mutation or allele that reduces an individual's fitness	Deleterious
A mutation that results in a change in a single nucleotide pair in a DNA molecule.	Point mutation
A mutation that does not affect the amino acid sequence of the protein encoded by a DNA sequence	Silent mutation
A point mutation (change in a single base pair) that causes a change in the amino acid sequence of a protein	Missense mutation
A mutation that introduces a stop codon into a DNA sequence	Nonsense mutation
A mutation that changes the reading frame of a sequence of DNA	Frameshift mutation
The division of a sequence of DNA or RNA into a particular series of three-nucleotide codons	Reading frame
A macromolecule consisting of one or more polypeptide chains composed of 50 or more amino acids linked together. Each protein has a unique sequence of amino acids and, in its native state, a characteristic three-dimensional shape.	Protein
A small organic molecule with a central carbon atom bonded to an amino group (–NH3), a carboxyl group (–COOH), a hydrogen atom, and a side group. Proteins are polymers of 20 common amino acids.	Amino acid
The covalent bond (C–N) bond formed by a condensation reaction between two amino acids	Peptide bond
The sequence of amino acids in a peptide or protein	Primary structure
The end of a polypeptide with a free amino group (translated first)	N terminus (or amino terminus)
The end of a polypeptide with a free carboxyl group	C terminus (or carboxyl terminus)
In proteins, localized folding of a polypeptide chain into regular structures (e.g., a-helix and b-pleated sheet) stabilized by hydrogen bonding between atoms of the backbone	Secondary structure
A protein secondary structure in which the polypeptide backbone coils into a spiral shape stabilized by hydrogen bonds between atoms.	Alpha helix
A protein secondary structure in which the polypeptide backbone folds into a sheetlike shape stabilized by hydrogen bonding	Beta-pleated sheet
The overall three-dimensional shape of a single polypeptide chain, resulting from multiple interactions among the amino acid side chains and the peptide backbone	Tertiary structure
A weak electrical attraction between two hydrophobic side chains. Often contributes to tertiary structure in proteins	Van der Waals interactions
Not interacting readily with water. Hydrophobic compounds are typically nonpolar compounds that lack charged or electronegative atoms and often contain many C – C and C – H bonds	Hydrophobic
A covalent bond between two sulfur atoms, typically in the side groups of some amino acids (e.g., cysteine). Often contributes to tertiary structure of proteins.	Disulfide bond
The overall three-dimensional shape of a protein containing two or more polypeptide chains (subunits	Quaternary structure
A protein catalyst used by living organisms to speed up and control biological reactions	Enzyme
Any substance that increases the rate of a chemical reaction without itself undergoing any permanent chemical change.	Catalyst:
energy required to initiate a chemical reaction	Activation energy
A high-energy intermediate state of the reactants during a chemical reaction that must be achieved for the reaction to proceed	Transition state
the difference in free energy between the reactants and products of a reaction	ΔG
The portion of an enzyme molecule where substrates (reactant molecules) bind and react.	Active site
Change in the shape of the active site of an enzyme, as the result of the initial weak binding of a substrate, so that it binds substrate more tightly	Induced fit
A small organic molecule that is a required cofactor for an enzyme-catalyzed reaction. Often donates or receives electrons or functional groups during the reaction.	Coenzyme
: For a protein, loss of its three-dimensional structure and biological activity due to breakage of hydrogen bonds and disulfide bonds, usually caused by treatment with excess heat or extreme pH conditions.	Denaturation

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