Biochemistry (ABI 102) – Flashcards
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The most abundant molecule in the human body is...
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Water
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What are the four most abundant elements in a human body?
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Carbon, Nitrogen, Oxygen, Hydrogen
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Which three cellular components are present in both prokaryotes and eukaryotes? A. ribosomes, chloroplasts, mitochondria B. nucleus, ribosomes, RNA C. RNA, DNA, ribosomes D. endoplasmic reticulum, DNA, RNA E. mitochondria, DNA, RNA
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C. RNA, DNA, ribosomes
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The bulk of aerobic metabolism in eukaryotic cells takes place in the...
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Mitochondria
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Which cellular compartment or organelle is involved in the synthesis of proteins and lipids?
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Endoplasmic Reticulum
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True or False? Carbon, nitrogen, oxygen, hydrogen and calcium are the five most prevalent elements found in the human body.
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True
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Condensation Reaction
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A chemical reaction in which two or more molecules combine to produce water and another simple molecule
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Hydrolysis Reaction
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A chemical reaction that breaks apart a larger molecule by adding a molecule of water
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Brønsted-Lowry Acid
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Proton donor
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Brønsted-Lowry Base
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Proton acceptor
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Hydrophobic Effect
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the observed tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules; occurs because interactions between the hydrophobic molecules allow water molecules to bond more freely, increasing the entropy of the system and decreasing the surface area of the non polar molecules
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Amphiphilic / Amphipathic
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Of or relating to a molecule having a polar, water-soluble group attached to a nonpolar, water-insoluble hydrocarbon chain.
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The angle of H2O is...
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104.5º
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Interactions Between Permanent Dipoles
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interspecific interactions
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Dipole-Induced Dipole Interactions
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dipole moment of polar molecule and polarizability of non-polar molecule
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London Dispersion Forces
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Occur between two instantaneous dipoles; the weakest dipole-dipole force (vs. hydrogen bonds which are the strongest dipole-dipole forces).
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Dialysis
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a procedure to remove waste products from the blood of patients whose kidneys no longer function; blood taken out of the body and urea and creatinine are removed from the blood by diffusion
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Buffer
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A solution that minimizes changes in pH when extraneous acids or bases are added to the solution; pH and pka must be within 1 of each other to be effective
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Good's Buffers
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1. pka from 6-8 2. Soluble in water 3. Membrane impermeability 4. Minimal salt effect (won't interact with other ions) 5. Minimal effect from temp or concentration 6. Well defined or non existent mineral cations 7. Biochemically inert (won't break down) 8. Chemical stability 9. Optical absorbance (? ; 230 nm) 10. Ease of preparation
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The lower the pka, the _____ (stronger/weaker) the acid
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The lower the pka, the stronger the acid
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The lower the pka, the ________ (more/less) H+ is dissociated
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The lower the pka, the MORE H+ is dissociated
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As pka increases, molecules tend to ____ (lose / gain) acidic hydrogen ions
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As pka increases, molecules tend to lose acidic hydrogen ions
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Metabolic Acidosis
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Characterized by a DECREASE in HCO?? level in the serum, leading to an increase in H? concentration and a decrease in pH (below 7.35), , and hyperventilation and a resulting drop in CO2 levels.
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Metabolic Alkalosis
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Characterized by an INCREASE in the HCO?? levels in the serum, leading to a decrease in the H? concentration and an increase in the pH (increase above 7.45), and hypoventilation (too little breathing) and a resulting accumulation of CO2.
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Respiratory Acidosis
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Characterized by excessive RETENTION of CO2 due to hypoventilation; therefore, an increased HCO?? concentration produces an increase in H+ ions and a decrease in the pH (decreases below 7.35).
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Respiratory Alkalosis
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Characterized by a decrease in HCO?? level in the serum, leading to an increase in H? concentration and an increase in pH (above 7.35), , and hyperventilation and a resulting drop in CO2 levels.
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A red blood cell has an internal salt concentration of ~150mM. The cell is placed in a beaker of 500mM salt. Assuming that the cell membrane is permeable to water but not to ions, water will move from the _____ (lower / higher) field with incorrect answer salt concentration to the _________ (lower / higher) field with incorrect answer salt concentration. If the membrane were permeable to ions, the solutes would diffuse _____ (into / out of) field with correct answer the cell
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A red blood cell has an internal salt concentration of ~150mM. The cell is placed in a beaker of 500mM salt. Assuming that the cell membrane is permeable to water but not to ions, water will move from the HIGHER field with incorrect answer salt concentration to the LOWER field with incorrect answer salt concentration. If the membrane were permeable to ions, the solutes would diffuse INTO field with correct answer the cell
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Which of the following correctly lists bonding interactions in terms of their increasing strength: A) Hydrogen bonds ; ionic interactions ; covalent interactions ; Van der Waals interactions B) Covalent bonds ; hydrogen bonds ; ionic interactions ; Van der Waals interactions C) Van der Waals interactions ; hydrogen bonding ; ionic interactions ; covalent bonds D) Van der Waals interactions ; ionic interactions ; hydrogen bonding ; covalent bonds
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C) Van der Waals interactions ; hydrogen bonding ; ionic interactions ; covalent bonds
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Which of the following statements about water is FALSE? A) Substances with polar functional groups are generally soluble in water. B) The hydrophobic effect is driven largely by the entropy of the non-polar substance. C) Water will act as a hydrogen bond acceptor with hydroxyl groups. D) Water carries a dipole because of the geometry of the two oxygen-hydrogen bonds. E) A network of electrostatic interactions exists between the molecules in water.
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B) The hydrophobic effect is driven largely by the entropy of the non-polar substance.
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The insolubility of nonpolar molecules in water is due to the large _______, which is the result of water molecules forming an ordered network surrounding nonpolar molecules.
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Negative entropy
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Osmotic pressure is a function of A) humidity B) solute size C) solute concentration D) van der Waals forces E) solute vapor pressure
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C) solute concentration
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The pH of coffee is 5.6. The pH of grapefruit juice is 2.6. This means that the proton concentration in coffee is A) 3000 times higher than in grapefruit juice B) 3000 times lower than in grapefruit juice C) a thousand times higher than in grapefruit juice D) a thousand times lower than in grapefruit juice E) 3 times the proton concentration of grapefruit juice
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D) a thousand times lower than in grapefruit juice.
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Open System
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A system in which both energy and matter are exchanged with the surroundings.
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Closed System
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A system in which energy, but not matter, is exchanged with its surroundings.
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Isolated System
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A system that exchanges neither matter nor energy with its surroundings.
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Living organisms are _____ systems. Why?
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Open systems because they take nutrients, release waste, and generate work and heat
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Avogadro's Number
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6.02 x 10^23
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First Law of Thermodynamics
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Energy can be transferred and transformed, but it cannot be created or destroyed.
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q = heat absorbed ____ system ____ surroundings
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q = heat absorbed BY system FROM surroundings
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w = work done ____ system ____ surroundings
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w = work dome ON system BY surroundings
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Explain what happens to water as it freezes
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As water cools towards 4ºC, it actually becomes more dense. Then as it reaches 0ºC, its density decreases as its structure opens with freezing. This allows the frozen water / ice to float in water.
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Amino Acid G
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Glycine
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Amino Acid A
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Alanine
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Amino Acid V
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Valine
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Amino Acid L
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Leucine
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Amino Acid I
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Isoleucine
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Amino Acid M
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Methionine
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Amino Acid P
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Proline
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Amino Acid F
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Phenylalanine
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Amino Acid W
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Tryptophan
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Amino Acid S
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Serine
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Amino Acid T
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Threonine
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Amino Acid N
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Asparagine
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Amino Acid Q
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Glutamine
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Amino Acid Y
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Tyrosine
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Amino Acid C
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Cysteine
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Amino Acid K
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Lysine
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Amino Acid R
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Arginine
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Amino Acid H
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Histidine
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Amino Acid D
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Aspartic acid
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Amino Acid E
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Glutamic acid
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Glycine
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G
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Alanine
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A
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Valine
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V
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Leucine
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L
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Isoleucine
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I
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Methionine
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M
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Proline
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P
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Phenylalanine
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F
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Tryptophan
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W
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Serine
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S
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Threonine
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T
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Asparagine
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N
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Glutamine
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Q
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Tyrosine
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Y
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Cysteine
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C
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Lysine
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K
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Arginine
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R
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Histidine
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H
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Aspartic acid
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D
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Glutamic acid
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E
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Enthalpy (H) Equation
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H = U + PV
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Hess's Law
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Regardless of the multiple stages or steps of a reaction, the total enthalpy change for the reaction is the sum of all changes
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Second Law of Thermodynamics
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says that the entropy (disorder) of the universe is increasing. One corollary of the Second Law of thermodynamics is the concept that, in most energy transformations, a significant fraction of energy is lost to the universe as heat.
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Entropy (S)
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a measure of the number of specific ways in which a thermodynamic system can be arranged, commonly known as disorder In a constant energy process (?U = 0) ?S ; 0
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Gibbs Free Energy
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the change in free energy for a process, combines enthalpy, entropy, and temperature Negative - spontaneous = 0 process at equilibrium
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Conversion from C° to K
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K = C° + 273.15
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?G° Equation
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?G° = -RT ln Keq R = 8.314 J/mol•K
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Concentration of water according to biochemists
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55.5M
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Zwitterions
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molecules with both a positive and negative charge that cancel each other out
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When pH ; pka the molecule is...
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PROTINATED
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When pH ; pka the molecule is...
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UNPROTINATED
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Isoelectric Point
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When the molecule is electrically neutral, pI=pH
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Electrophoresis
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The movement of suspended particles through a fluid or gel under the action of an electromotive force applied to electrodes in contact with the suspension.
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Chirality
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If an objects mirror image cannot be superimposed on the original object; lacks internal plane of symmetry
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Enantiomers
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Non-superimposable mirror image
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Amino acid residues of all proteins have the __ configuration
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L configuration
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Essential amino acids
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Amino acids that are needed, but cannot be made by the body; they must be eaten in foods Phe, Val, Thr, Trp, Ile, Met, His, Leu, Lys PVT TIM HaLL
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Primary Structure of Protein
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Amino acid sequence of its polypeptide chains
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For a protein of n residues there are ___ possible sequences
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20^n
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Neutral Drift
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Random mutations in time that do not affect function
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Invariant Residues
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Position has to be a particular, amino acid can't be replaced
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Conservatively Substituted
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Position can be occupied by the same type of amino acid
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Hypervariable
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DNA segment that shows a high degree of variability between members of a population; only functions as a placeholder
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Orthologous Proteins
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Proteins from different species that have homologous amino acid sequences (and often a similar function.) They arose from a common ancestral gene during evolution.
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Gene Duplication
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The generation of extra copies of a gene in a genome over evolutionary time. A mechanism by which genomes can acquire new functions.
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Paralogous Genes
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Genes that are found in the same genome as a result of gene duplication but one has gained a new function.
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A phylogenetic tree depicts ___________ of proteins. A) folding patterns B) hypervariable residues C) invariable residues D) evolutionary relationships E) gene sequences
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D) evolutionary relationships
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A protein that has had few changes in its amino acid sequence over evolutionary history is labeled A) a fibrinopeptide B) evolutionarily conserved C) random D) a product of pseudogenes E) phylogenetic
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B) evolutionarily conserved
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A fast way for nature to generate new proteins is: A) generation of pseudogenes. B) mutation by neutral drift. C) shuffling protein domains or motifs. D) hypervariable positions. E) liberal substitution.
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C) shuffling protein domains or motifs.
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Proteins are often constructed from multiple segments of 40-200 amino acid residues, commonly called A) pseudogenes B) hypervariable residues C) protolytic fragments D) domains E) subunits
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D) domains
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The amino acid sequence of which type of protein is likely to have changed the least during evolution? A) A protein that makes no important interactions with other proteins B) A protein fragment with no known function C) A protein that has extensive interactions with other proteins and with DNA D) A protein that has some interactions with other proteins
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C) A protein that has extensive interactions with other proteins and with DNA
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The _____ structure of a protein is the amino acid sequence of its polypeptide chain, or chains if the protein consists of more than one polypeptide.
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Primary
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True or False. Only a tiny fraction of all possible proteins exist (i.e. of all combinations of protein sequence possible, evolution has produced only a tiny fraction of the theoretical possibilities).
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True
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True or False. In an evolutionary time frame, the rate at which mutations are accepted into a protein depends upon the function of the protein.
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True
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Which one of the following statements about peptide bonds is FALSE. Peptide bonds are: A) rigid and planar, with partial double-bond character B) involved in forming the primary structure of proteins C) charged D) amides E) covalent
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C) charged
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Which level of protein structure is defined as "the hydrogen bonded arrangement of the polypeptide backbone"? A) Primary B) Secondary C) Tertiary D) Quaternary
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B) Secondary
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A rigid, planar structure between at least two amino acids consisting of about 40% double bond character is characteristic of a _______________.
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Peptide group
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Which of the following is FALSE with respect to ?-sheets? A) ?-sheets may be parallel or anti-parallel. B) Strands in a ?-sheet are connected by irregular loops. C) ?-sheets are stabilized by non-covalent forces. D) Amino acid side chains protrude from one side of the ?-sheet
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D) Amino acid side chains protrude from one side of the ?-sheet
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Repeating values of ? and ? make up predictable orientations of amino acid with a chain, this predictable orientation forms _________________
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Regular secondary structure
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The strength of Entry field with _________ comes from close packing of glycine residues and the characteristics of hydroxyproline allowing formation of a left-handed helical conformation which combines with two other left-handed structures to form a right-handed triplet helix.
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collagen
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Helix-Entry field with _________ is the phenomenon in which side chains of residues just outside -helices make hydrogen bonds to the backbone groups of the four terminal residues of the helix.
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capping
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Which of the following describes the entire three-dimensional structure of a single polypeptide? A) Tertiary structure B) Secondary structure C) Quaternary structure D) Primary structure
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A) Tertiary structure
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What is the primary driving force in the formation of protein tertiary structure? A) The exclusion of non-polar substances from aqueous solution. B) The formation of van der Waals interactions between neighbouring groups. C) Energy released when additional ion pairs are formed. D) Energy released when additional hydrogen bonds are formed.
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A) The exclusion of non-polar substances from aqueous solution.
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Which of the following statements about quaternary structure is TRUE? A) Quaternary structure requires covalent interactions between polypeptide chains. B) Quaternary structure is defined as the precise, 3-D arrangement of polypeptide backbones in proteins with more than one subunit. C) Quaternary structure exists in monomeric proteins. D) Quaternary structure is stabilized by the same types of noncovalent interactions as tertiary structure
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D) Quaternary structure is stabilized by the same types of noncovalent interactions as tertiary structure
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The overall arrangement of the regular structural elements such as the alpha helix and the ? sheet in the protein are considered the protein's _________
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tertiary structure
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The __________ of an amino acid can be used to predict whether an amino acid side chain folds towards the inside or outside of a globular protein.
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hydropathy
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What is the major factor that "drives" the folding of proteins into their tertiary structure? A) Placement of polar amino acid residues on the surface of the protein. B) Placement of hydrophobic amino acid residues within the interior of the protein. C) Formation of the maximum number of hydrophilic interactions. D) Formation of the maximum number of ionic interactions.
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B) Placement of hydrophobic amino acid residues within the interior of the protein.
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Secondary Structure
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The local spatial arrangement of a polypeptide's backbone atoms without regard for its side chain
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Tertiary Structure
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the three-dimensional form of an entire polypeptide, including its side chains
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Quaternary Structure
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the spatial arrangement of protein subunits
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? (Psi) Angle
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angle in polypeptide backbone, torsion angle around the C?-C bond
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? (Phi) Angle
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angle in polypeptide backbone, torsion angle around the C?-N bond
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Ramachandran Diagram
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A steric countour duagram that depicts allowed ranges of the angles phi and psi for amino acid residues in polypeptide cahins. For each residue, its confirmation in the main chain of polypeptide can be completely defined by the psi and phi angles
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?-helix
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A protein secondary structure - a right-handed spiral held in place by hydrogen bonds between adjacent C=O and NH groups The side chains project outward and down which avoids steric hindrance Tightly packed - van der Waals contact
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?-pleated sheet
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An element of secondary structure, marked by peptide chains lying alongside one another, forming rows or strands H-bonding occurs between polypeptide chains Anti-parallel or parallel (slightly less stable) Side chains extend to opposite sides of sheets
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Globular Proteins
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These proteins are small spheres with little to no water inside. They have hydrophobic amino acids in the inside and hydrophilic R groups on the outside Water soluble, characterized by compact and highly folded structure
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Fibrous Proteins
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These form extended sheets or strands, making them tough, durable, and generally insoluble in water; form fibers
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Keratin
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fibrous protein, mechanically durable and relatively unreactive, two alpha helices coiling around each other, heptad repeat Lots of keratin causes curly hair