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3-2
4. All the following statements about molecular chaperones are true except
a. They play a role in the proper folding of proteins.
b. They are located in every cellular compartment.
c. They are found only in mammals.
d. They bind a wide range of proteins.
Ans: c
Ans: d
Ans: c
Ans: a
Ans: d
b. ubiquitinylation
c. acetylation
d. glycosylation
e. all of the above
Ans: b
Ans: a
11. Proteases that attack selected peptide bonds within a polypeptide chain are synthesized and secreted as inactive
forms called
a. carboxypeptidases.
b. aminopeptidases.
c. zymogens.
d. a and b.
e. none of the above
Ans: c
Ans: e
13. Protein kinase A is converted from an inactive state to an active state by binding
a. ATP.
b. calcium.
c. cAMP.
d. a and c.
e. all of the above
Ans: c
14. Kinases, which are responsible for the activation or inactivation of a number of proteins, serve to add phosphate
groups onto
a. tryptophan residues.
b. serine residues.
c. cysteine residues.
3-4
d. a and c.
e. none of the above
Ans: b
Ans: a
16. Which of the following methods can separate proteins based on their mass?
a. centrifugation
b. ion exchange chromatography
c. SDS polyacrylamide gel electrophoresis
d. a and c
e. all of the above
Ans: d
17. In two-dimensional gel electrophoresis proteins are first resolved by ______________________ and then by
____________________.
a. IEF; SDS-PAGE
b. SDS-PAGE; affinity chromatography
c. SDS-PAGE; ion exchange
d. IEF; gel filtration
e. SDS-PAGE; Western blot analysis
Ans: a
Ans: b
19. Starting with 1 mCi (milliCurie) of a phosphorus-32-labeled compound, how long would it take until only 0.125
mCi remains?
a. 14.3 days
b. 28.6 days
c. 42.9 days
d. 57.2 days
Ans: c
3-5
Ans: c
21. Describe the types of bonds/interactions that hold together or stabilize the primary, secondary, tertiary, and
quaternary structures of proteins.
Ans: The primary structure of a protein is linked by covalent peptide bonds. The secondary structure is stabilized by
hydrogen bonds between atoms of the peptide backbone. The tertiary structure is stabilized by hydrophobic
interactions between the nonpolar side groups and hydrogen bonds between polar side groups. The quaternary
structure is held together by noncovalent bonds between protein subunits.
22. Many proteins contain one or more motifs built from particular combinations of secondary structure. Describe
the three common structural motifs discussed in this chapter.
Ans: The three structural motifs described in this chapter include the coiled coil motif, the helix-loop-helix motif, and
the zinc finger motif. The coiled-coil motif consists of two or more helices wrapped around one another. The
helix-loop-helix motif consists of two helices connected by a loop that contains certain hydrophilic residues at
invariant positions in the loop. The zinc-finger motif consists of an helix and two strands held together by
a zinc ion in a fingerlike bundle.
23. Describe the mechanism by which the bacterial chaperonin GroEL promotes protein folding.
Ans: The bacterial chaperonin GroEL forms a barrel-shaped complex of 14 identical subunits. A partially folded or
misfolded polypeptide is inserted into the GroEL barrel, where it binds to the inner wall and folds into its native
conformation. In an ATP-dependent step, the GroEL barrel expands to a more open state, which results in
release of the folded protein.
24. What role does aberrant protein folding play in the development of a disease such as Alzheimer’s disease?
Ans: Misfolding of a protein marks it for degradation by proteolytic cleavage. In Alzheimer’s disease, misfolding
and subsequent proteolytic degradation of the amyloid precursor protein generates a short fragment called -
amyloid protein, which changes from an -helical to a -sheet conformation. This aberrant structure aggregates
into highly stable filaments called amyloid plaques that accumulate in the brains of Alzheimer’s patients.
25. Describe the general mechanism by which a multisubunit protein can be activated by binding an allosteric
effector molecule.
Ans: A multisubunit protein often contains both regulatory and catalytic subunits. In the absence of the allosteric
effector molecule the active site of the enzyme is masked by the regulatory subunit. Upon binding the allosteric
effector molecule a conformational change occurs, which releases suppression of the catalytic subunit by the
regulatory subunit.
Ans: The activity of proteins can be modulated by binding of a ligand. Cooperativity describes a phenomenon in
which the binding of one ligand molecule affects the binding of subsequent ligand molecules. This allows a
protein molecule to respond more efficiently to small changes in ligand concentration. In positive cooperativity,
the binding of one ligand molecule enhances the binding of subsequent ligand molecules.
Ans: In the first dimension, proteins are separated by isoelectric focusing, which separates proteins on the basis of
their charge. In the second dimension, the proteins, which have been separated by charge, are then separated by
their molecular weight (mass). The advantage of the two-dimensional technique is its ability to separate proteins
more effectively. For example, two proteins with the same molecular weight could not be separated by one-
dimensional SDS polyacrylamide gel electrophoresis. However, if these proteins differed in charge, then the
two-dimensional gel would be able to separate these proteins into unique spots.
28. How can gel filtration chromatography separate proteins based on their mass?
Ans: In gel filtration chromatography, a column of porous beads made from acrylamide, dextran, or agarose is poured
into a column. Proteins flow around the spherical beads. Because the surface of the beads contains large
depressions, smaller proteins will penetrate into the depressions more easily than larger proteins and thus will
travel more slowly through the column than larger proteins.
29. What is Western blotting? How can this technique be used to detect proteins?
Ans: Western blotting or immunoblotting is a method for identifying proteins separated on a gel using a specific
antibody. The proteins are first separated by polyacrylamide gel electrophoresis and then transferred from the
gel to a membrane. The membrane is incubated with a primary antibody specific for the desired protein. After
unbound antibody is washed away, the presence of the bound primary antibody is detected with a secondary
enzyme-linked antibody. The presence of the antibody-enzyme complex can then be detected using a
chromogenic substrate.
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pues es deleite halagüeño
–y en la experiencia me fundo–
buscar dentro del gran mundo
otro mundo más pequeño.
Mira, ¡qué hechiceras! Van
desnudas. ¡Y son muy bellas!
¡Cuán tapadas van aquellas!
Viejas o feas serán.
Amable procura ser,
y cortés y lisonjero:
eso no cuesta dinero,
y produce gran placer.
Una música sonó:
¡qué espantosa cencerrada!
Pasemos: te daré entrada
tan luego como entre yo.
Mira, ¡cuán vasto lugar!
Sus límites no se ven;
cien antorchas y otras cien
lanzan fulgor singular;
y una inmensa multitud
que vivaz júbilo inflama,
danza y ríe, come y ama:
¿quieres mayor beatitud?
Fausto
Mefistófeles
Un General
Nada de la gratitud
de las naciones esperes;
siempre van, cual las mujeres,
detrás de la juventud.
Un Ministro
Un Advenedizo
Un Autor
La Bruja prendera
Mefistófeles
Fausto
Mefistófeles
La tromba asciende,
y aquel que impulsar pretende
es impulsado a la vez.
Mira.
Fausto
Mefistófeles
Es Lilith, la hermosa.
Fausto
¿Lilith?
Mefistófeles
La primera esposa
de Adán. ¡Guárdate bien de ella!
Guárdate de sus cabellos
que su adorno y gloria son:
si prenden un corazón,
para siempre queda entre ellos.
Fausto
Mefistófeles
Es imposible parar
en aquesta danza loca:
la música otra vez toca:
saquémoslas a bailar.
La Hermosa
La Vieja
Al de la Pata de Cabra
saludo y beso los pies:
Si queréis...
· · · · · · · · · · · · ·
· · · · · · · · · · · · ·
El Proktofantasmista
Fausto
El Proktofantasmista
Mefistófeles
Fausto
De la boca
le ha salido un ratón rojo.
Mefistófeles
Fausto
Y a más...
Mefistófeles
¿Qué más?
Fausto
¡Ay, Mefisto!
¿Una pálida doncella,
sola y triste, dulce y bella,
allá, a lo lejos, no has visto?
Entre la turba precita,
sin mover los pies, avanza:
¡tiene cierta semejanza
con la pobre Margarita!
Mefistófeles
Fausto
Mefistófeles
Mefistófeles
Servíbilis
Adelante.
Hoy siete piezas promete
el cartel; la que hace siete
va a comenzar al instante.
Cómicos son de afición;
el autor aficionado,
y a mí la afición me ha dado
de levantar el telón.
Permitidme, pues, marchar.
Mefistófeles
Un Heraldo
Puck[28]
Ariel[29]
Oberón
Titania
La Orquesta, tutti
Fortissimo
Solo
Una parejita[31]
Un Ortodoxo[33]
Un Purista[34]
Una Matrona
El Maestro de capilla
Los Xenios[35]
Hennings[36]
Musageta[37]
El Viajero curioso[38]
¿Quién es ese pedante que en su frente
soberbia y petulancia lleva escritas?
¿Qué busca, tan orondo y displicente?
Siguiendo la husma va de los Jesuitas.
[38] Otra alusión a Nicolai, que era apodado
Jesuitenrrècher (rastreador de los jesuitas) porque
tenía la preocupación de ver en todas partes la mano
de esta célebre Orden religiosa. (Véase la nota
segunda de la pág. 324.)
Una Grulla[39]
Un Hombre de mundo
Un Danzante
El Maestro de baile