Test
502 practice test
Este test tiene tipos de pregunta que se abren en el reproductor de siempre.
Preguntas del test (68)
12.3 Carbohydrates are molecular compounds containing just three elements: Carbon, Oxygen, Nitrogen
- AVerdadero
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22.4 The simple sugar ___________ is a principal source of metabolic energy for the cell.
- Afructose
- Bsacrose
- Cstarch
- Dglucose
32.3 Disaccharide contains
- Aglucose
- Bmaltose
- Cstarch
- Dglycogen
- Efructose
- Fgalactose
- Glactose
- Hsucrose
- Icellulose
42.3 Monosaccharides contains
- Aglucose
- Bmaltose
- Cstarch
- Dglycogen
- Efructose
- Fgalactose
- Glactose
- Hsucrose
- Icellulose
52.5 Select the correct answer for the number of carbons
- A3 carbons are triose, 4 carbons are pentose, 5 carbons are hexose, 6 carbons are tetrose
- B3 carbons are pentose, 4 carbons are hexose, 5 carbons are triose, 6 carbons are tetrose
- C3 carbons are triose, 4 carbons are tetrose, 5 carbons are pentose, 6 carbons are hexose
62.4 monosaccharides are simple sugars that contain only one aldehyde or ketone groups
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72.13 Oligosaccharides consist of a few short chains of monosaccharides units joined by ___________ bond
- Ahydrogen
- Bcovalent
- Cionic
- Dphosphodiester
82.22 Asymmetric Carbon is a chiral molecule contains at least one C bonded with
- A4 different groups
- B3 different groups
- Call the same groups
- Ddouble bond
92.25 Enantiomers are chiral molecules that are mirror image
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102.27 Which of the following is incorrect
- ASucrose : glucose and Fructose
- BLactose: galactose and glucose
- CMaltose: Glucose and glucose
- DSucrose: Glucose and starch
112.35 In the digestive tract, polysaccharides and disaccharides are converted to monosaccharides by ___________ enzymes that hydrolyze the __________ bond
- AGylcosidases and hydrogen
- BGlycosidases and glycosidic
- Chydrogen and glycosidic
- Dglycosidic and hydrogen
12(3.3) All the following are roles of the Amino Acids EXCEPT:
- Athey may polymerize to form peptide most notably proteins
- Bthey serve as precursors for other small biomolecules
- Cthey may be oxidized to serve as an energy source for the cell
- Dthey serve as transporters of hydrophilic compound in blood
133.3 Amino acids contains two characteristics functional groups:
- Aamino group and carboxylic group
- Bamino group and phosphate group
- Cphosphate group and carboxylic group
14Carboxylic group has a pKa of
- A3
- B6
- C9
- D2
- E1
153.4 amino group has a pKa
- A9
- B2
- C6
- D1
163.6 The formation of a peptide bond between two amino acids is an example of a(n) ______________ reaction.
- Acleavage
- Bcondensation
- Cgroup transfer
- Disomerization
- Eoxidation reduction
173.10 Sulfur group contains which amino acids
- Amethionine and glutamine
- Bmethionine and serine
- Cserine and cysteine
- Dcysteine andmethionine
- Easoargunine and glutamine
183.9 serine and threonine: side chains contain which ______ group
- Ahydroxyl
- Bamide
- Cthiol
193.9 cysteine: side chain containing ______ group
- Ahydroxyl
- Bamide
- Cthiol
203.17 The chirality of an amino acid results from the fact that its carbon:
- Ahas no net charge
- Bis a carboxylic acid
- Cis bonded to four different chemical groups
- Dis in the L absolute configuration in naturally occurring proteins
- Eis symmetric
21Of the 20 standard amino acids, only ___________ is not optically active. The reason is that its side chain ___________
- Aalanine; is a simple methyl group
- Bglycine; is a hydrogen atom
- Cglycine; is unbranched
- Dproline; forms a covalent bond with the amino group
- Elysine; contains only nitrogen
223.18 All of the amino acids that are found in proteins, except for proline, contain a(n):
- Acarbonyl group
- Bamino group
- Cester group
- Dthiol group
23Which of the following statements about cystine is correct?
- ACystine is formed through a peptide linkage between two cysteines. E) Two cystines are released when a —CH2—S—S—CH2— disulfide bridge is reduced to —CH2—SH.
- BCystine forms when the —CH2—SH group is oxidized to form a —CH2—S— S—CH2— disulfide bridge between two cysteines.
- CCystine is formed by the oxidation of the carboxylic acid group on cysteine
- DCystine is an example of a nonstandard amino acid, derived by linking two standard amino acids.
243.26 Isoelectronic point or iso-ionic point is the PH at which the amino acid does not migrate in an electric field, which is the correct equation:
- ApI=1/2(pKa1+pKa2)
- BpI=2(pKa1+pKa2)
- CpI=(pKa1+pKa2)
253.33 Select the classifications for Fibrous protein
- Ado not have a tertiary structure
- Bspherical in shape
- Cdissolve in water to form colloidal solution
- Dlong fibers or sheets in shape
- Einsoluble in water
- Fegg albumin, serum, globulin etc
- Gperform structural functions
- Heg. keratins, collagen, elastin, and fibroin
- Ithe length of polypeptide chain is always identical in two samples of the same globular protein
- Jthe length of polypeptide chain may vary in two samples of the same fibrous protein
263.33 Select the classifications for Globular protein
- Ahave tertiary structure. Quaternary may or may not be present
- Bperform structural functions
- Cspherical in shape
- Dinsoluble in water
- Edissolve in water to form colloidal solution
- Flong fibers or sheet in shape
- Gthe length of polypeptide chain is always identical in two samples of the same globular protein
- Hdo not have a tertiary structure
- Iperforms metabolic functions
- Jegg albumin, serum globulin etc
273.35 Primary Protein is a ________ structure that refers to the sequence of ________ bond along the main chain of polymer
- Ahydrogen, linear
- Blinear, covalently
- Clinear, hydrogen
- D3d, hydrogen
283.35 secondary protein is a repeating pattern of _________ which is an example of ___________.
- Ahydrogen bond, only beta sheet
- Bhydrogen bond, only alpha helix
- Ccovalently bonded, alpha helix and beta sheet
- DHydrogen bond, alpha helix and beta sheet
293.42 What amino acid is called helix breaker?
- AProline is disfavored in an α-helix because its N is part of a cyclic structure, it cannot form appropriate bond angles to fit within α-helix called helix breaker
- Bβ-sheet is formed by 2 or more strands of amino acids; it is a coplanar alignment of backbone atoms
- CHistidine, lysine and arginine are basic aa that carry a nitrogen that can be protonated and positively charged at physiologic and lower pH
303.47 Identify which of the following refers to the arrangements of different protein subunits in a multi-protein complex
- ASecondary structure
- BQuaternary structure
- CPrimary structure
- DTertiary structure
31Unfolding of a protein is called denaturation
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323.51 which of the following is not correct about protein unfolding.
- Aunfolding is sometimes reversible for small proteins mostly
- Bdisulfide bridge are important in reestablishing the proper
- Cdenaturation results in gain of function for the protein
333.53 For the unfolding reaction of a protein G , ∆H=216 Kj/mol this means that
- AUnfolding is favored enthalpically
- BThe entropy is positive at all temperature
- CFolding is favored enthalpically
- DThe entropy is negative at all temperature
343.55 Myoglobin is a globular protein composed of a single polypeptide that has one O2 binding site
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353.62 Protein turnover
- AIs the process of recycling proteins into their constituent amino acids for reuse by the cell
- BIts is used to eliminate misfolded proteins
- CIts used to regulate the cell cycle by breaking down in a timely fashion
- DIt is used in the immune system to provide the necessary cleavage of foreign antigenic proteins for presentation and recognition by immune system cells
- EAll of the above
363.62 Two main systems used in protein degradation: lysosomal system and ubiquitin multi-subunit enzyme assembly the proteasome
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373.63 All are correct for lysosomal system EXCEPT:
- ALysosomes are membrane bound cytoplasmic organelles that form the major degradative compartment in the cell
- BIt degrades proteins, nucleic acids, whole bacteria through endocytosis, autophagy, and chaperone-mediated autophagy
- CLysosomes are extremely acidic (pH=3.8-5) which promotes denaturation of protein and nucleic acids.
- DLysosomes also contain hydrolytic enzymes that are active at high pH
383.68 there are 10 essential amino acids
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393. 68 protein are classified based on their structure or function
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40[blank_start]System[blank_end] Part of the universe that is of interest, e.g organism or cells surrounding
[blank_start]Kinetic energy[blank_end] Energy of movement
[blank_start]open system[blank_end] a system that can exchange matter/energy with surrounding
[blank_start]closed system[blank_end] A system that cannot exchange matter with surroundings
[blank_start]potential energy[blank_end] Stored energy
[blank_start]isolated system[blank_end] a system that cannot exchange matter/energy with surrounding
[blank_start]electric energy[blank_end] the energy of moving electrons or other charged particles
[blank_start]Heat or thermal energy[blank_end] The energy of the motion of molecules
[blank_start]radiant energy[blank_end] the kinetic energy of photons, or waves of light, and is critical to biology- ASystem
- Bclosed system
- Copen system
- Dradiant energy
- Epotential energy
- FKinetic energy
- Gpotential energy
- Helectric energy
- Iradiant energy
- Jclosed system
- Kopen system
- Lsystem
- Mopen system
- Nsystem
- Okinetic energy
- Pelectric energy
- Qclosed system
- Rpotential energy
- Sisolated system
- Theat or thermal energy
- Uclosed system
- Vsystem
- Wkinetic energy
- Xopen system
- Ypotential energy
- Zisolated energy
- AAheated or thermal energy
- ABpotential energy
- ACsystem
- ADkinetic energy
- AEopen system
- AFisolated system
- AGradiant energy
- AHclosed energy
- AIisolated system
- AJheat or thermal energy
- AKradiant energy
- ALelectric energy
- AMpotential energy
- ANopen system
- AOclosed system
- APelectric energy
- AQkinetic energy
- ARopen system
- ASclosed system
- ATpotential energy
- AUheat or thermal energy
- AVradiant energy
- AWHeat or thermal energy
- AXradiant energy
- AYelectric energy
- AZisolated system
- BApotential energy
- BBkinetic energy
- BCradiant energy
- BDheat or thermal energy
- BEelectric energy
- BFisolated energy
- BGpotential energy
- BHclosed system
- BIkinetic energy
41the highest potential energy is while an object is rolling down the hill.
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42The three types of kinetic energy: heat(thermal), Radiant energy, and electric.
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43What is potential energy?
- AThe energy an object has due to its motion
- BThe energy an object might have if it existed
- CThe stored energy of an object due to its position or condition
44What is kinetic energy?
- AThe energy an object has due to its motion
- BThe stored energy of an object due to its position or condition
- CThe energy an object might have if it existed
45Concertation gradient is the
- AConcentration of high solute to low solute
- BConcentration of low solute to high solute
46to predict the direction of a chemical energy, measure the potential energy called Free energy or G (Gibbs)
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47Which of the following has the most potential energy?
- AA car at the top of a hill
- BA car speeding down the hill
- CA person at the top of a hill
48Can you create or destroy energy?
- Ayes
- Bno
- Cif your Rose youll give it the hand
49Laboratory tests on the urine of a patient identified the presence of methylmalonate (-OOC–CH(CH3)–COO-). Methylmalonate is best described as which one of the following?
- AA strong acid
- BThe conjugate base of a weak acid
- CIt is 100% dissociated at its pKa.
- DIt is a major intracellular buffer.
5042. What is the pH 0.1 M HCl? [blank_start]1.26[blank_end]
- A1.26
51[blank_start]Oxidized[blank_end] the species losing electrons
[blank_start]Redox[blank_end] When one chemical species loses electron and another gains electron
[blank_start]Reduce[blank_end] The species gaining electrons- AOxidized
- Bredox
- Creduce
- DRedox
- Eoxidized
- Freduce
- GReduce
- Hoxidized
- Iredox
52What’s the formula for carbohydrate
- A(CH2O)n
- BCH3(CH2)3-CH3
- CCOOH
536.3 Enzymes are biological catalysts that act to slow down biochemical reaction
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546.5 stomach enzymes used to break protein down into peptides. works at very acidic pH(1.5)
- Apepsin
- Blactase
- Ctopoisomerase
- Dhyaluronidase
- Ezymase
556.5 a digestive enzyme that breaks lactose into glucose and galactose. low levels of lactase can result in locatose intolerance
- Apepsin
- Blactase
- Ctopoisomerase
- Dhyaluronidase
- Ezymase
566.5 a family of enzyme that act on the coiled structure of DNA. they cut the DNA to alter the coiled structure.
- Apepsin
- Blactase
- Ctopoisomerase
- Dhyaluronidase
- Ezymase
576.5 a family of enzymes that break down hyaluronic acid and increase tissue permeability
- Apepsin
- Blactase
- Ctopoisomerase
- Dhyaluronidase
- Ezymase
586.5 a naturally occuring enzyme in yeast, widely used in the baking industry to ferment sugar into ethanol and carbon dioxide
- Apepsin
- Blactase
- Ctopoisomerase
- Dhyaluronidase
- Ezymase
59 Enzyme speeds up the reaction by reducing the activation energy (∆G‡) by allowing the binding of the transition state into the active site
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606.9 The highest potential energy
- Atransition state
- Breactant
- Cproduct
61Prosthetic groups are [blank_start]tightly[blank_end] bound co-factor and co-enzyme are [blank_start]loosely[blank_end] bound co-factor
- Atightly
- Bloosely
62Enzyme cofactors that bind covalently at the active site of an enzyme are referred to as _________
- Aprosthetic group
- Bapoenzymes
- Cvitamins
- Dco-substrates
636.19 Which of the following statement is not true regarding the active site of an enzyme?
- AAn active site is normally a hollow on the surface of an enzyme
- Ban active site is normally hydrophilic in nature
- Csubstrates fit into active sites and bind to functional groups within the active site
- DAn active site contains amino acids which are important to the binding process and the catalytic mechanism
64 A catalyst can promote product formation during a chemical reaction by _____.
- Abringing reactants together.
- Bpositioning reactants in the correct orientation.
- Cstabilizing the transition state.
- Dlowering the activation energy barrier.
- Eall are correct
65The potential outcome of a reaction is usually influenced by two factors:
- Astability of product
- Brate of product
- Crate of the reaction
66If the reaction is under kinetic control (rate, irreversible conditions) and the major product is that from fastest reaction.
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67If the reaction is under thermodynamic control (equilibrium, reversible conditions) and the major product is the more stable system
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68stopped at 6-27
- A6-27
- Bok
Información
- Descripción
- Test sobre 502 practice test, creado por Abdullah Saleh el 03/09/2017.
- Autor
- Abdullah Saleh
- Idioma
- English
- Visitas
- 42
- Etiquetas
- Valoración
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