WGU C785 BIOCHEMISTRY OA
QUESTIONS AND ANSWERS
Which\level\of\protein\structure\is\disrupted\through\the\hydrolysis\of\peptide\bonds?
Quaternary
Tertiary
Primary
Secondary\-\ans✔Primary
The\primary\structure\of\a\protein\is\the\sequence\of\amino\acids\held\together\by\peptide\
bonds.\Peptide\bonds\are\formed\by\dehydration\reactions\and\disrupted\by\hydrolysis.
A\mutation\in\the\beta-hemoglobin\gene,\which\results\in\the\replacement\of\the\amino\
acid\glutamate\in\position\6\with\the\amino\acid\valine,\leads\to\the\development\of\sickle\
cell\anemia.\The\structures\of\glutamate\and\valine\are\shown\below.
If\the\beta\hemoglobin\gene\in\a\patient\with\sickle-cell\anemia\were\to\be\edited\so\that\
the\valine\in\position\6\was\replaced\with\a\different\amino\acid,\which\replacement\for\
valine\would\be\expected\to\have\the\best\clinical\outcome,\in\theory,\for\the\patient?\
(Assume\the\valine\can\potentially\be\replaced\with\any\amino\acid\other\than\
glutamate.)\-\ans✔The\original\amino\acid\in\a\healthy\patient\is\glutamate,\which\is\
negatively\charged.\The\mutated\amino\acid\is\valine,\which\is\non-polar.\Valine\is\
causing\sickle\cell\anemia.\The\best\amino\acid\to\replace\valine\so\that\the\patient\is\
healthy\again\would\be\the\one\most\like\glutamate,\so\any\negatively\charged\amino\
acid.
Secondary,\tertiary,\and\quaternary\levels\of\protein\structure\can\all\be\impacted\by\
exposing\a\protein\to\which\treatment?
Change\of\a\hydrophobic\amino\acid\to\a\different\hydrophobic\amino\acid
Addition\of\a\reducing\agent
Placement\of\the\protein\in\a\solution\with\a\low\pH
,Increase\in\the\concentration\of\the\protein\in\solution\-\ans✔Placement\of\the\protein\in\a\
solution\with\a\low\pH
Changes\in\pH\affect\hydrogen\bonds\and\ionic\bonds.\Hydrogen\bonds\in\the\backbone\
of\amino\acids\occur\in\secondary\structure,\and\both\hydrogen\bonds\and\ionic\bonds\
occur\in\the\side\chains\of\amino\acids\in\tertiary\structure.
An\increase\in\beta-pleated\sheet\structure\in\some\brain\proteins\can\lead\to\an\increase\
in\amyloid\deposit\formation,\characteristic\of\some\neurodegenerative\diseases.\What\is\
the\primary\biochemical\process\that\follows\the\increase\in\beta-pleated\sheet\structure\
that\leads\to\the\development\of\the\amyloid\deposits?
An\increase\in\glycogen\formation\in\the\brain\cells
Aggregation\of\the\proteins\in\the\brain
Secretion\of\glucagon,\leading\to\excessive\ketogenesis
An\increase\in\anaerobic\metabolism\of\glucose\in\the\brain\-\ans✔Aggregation\of\the\
proteins\in\the\brain
This\question\is\describing\changes\in\protein\structure.\Aggregation\occurs\when\
proteins\clump\together\inappropriately,\causing\plaques\like\amyloid\deposits\to\
accumulate.
Which\level\of\protein\structure\is\determined\by\the\sequence\of\amino\acids?
Secondary\structure
Quaternary\structure
Tertiary\structure
Primary\structure\-\ans✔Primary\structure
The\primary\structure\of\a\protein\is\simply\the\sequence\of\amino\acids\held\together\by\
peptide\bonds.
Which\force\is\most\influential\in\determining\the\secondary\structure\of\a\protein?
Hydrophobic\effect
Disulfide\bonding
Hydrogen\bonding
, Electrostatic\interactions\-\ans✔Hydrogen\bonding
The\secondary\structure\of\a\protein\is\built\by\hydrogen\bonds\between\the\carboxyl\
groups\and\amino\groups\on\the\backbones\of\the\amino\acids.
Which\amino\acid\would\most\likely\participate\in\hydrogen\bonds?\-\ans✔Amino\Acid\
structure\4
This\is\a\polar,\uncharged\amino\acid\due\to\the\OH\group\on\the\side\chain.\Polar,\
uncharged\amino\acids\containing\oxygen\or\NH\groups\make\hydrogen\bonds.
Which\portion\of\the\amino\acid\is\inside\the\box?
\
The\box\is\surrounding\the\section\below\the\Alpha\Carbon\-\ans✔Side\Chain
The\side\chain\is\the\variable\group\of\the\amino\acid,\also\called\the\R\group.\Every\
amino\acid\has\the\same\amino\group,\carboxylic\acid\group,\and\an\alpha\carbon,\but\
the\side\chain\is\different.
Which\pair\of\amino\acids\will\most\likely\interact\through\hydrophobic\forces\between\
their\side\chains?\-\ans✔Both\of\these\amino\acids\are\non-polar\and\therefore\can\
interact\together\with\a\hydrophobic\interaction.\Please\note\that\the\"S"\in\the\amino\acid\
on\the\right\is\non-polar,\while\the\"SH"\group\in\answer\choice\D\is\polar.\The\S\must\
have\an\H\to\be\polar\and\is\otherwise\non-polar.
Which\portion\of\the\amino\acid\is\inside\the\box?
The\box\is\over\the\Carbon\at\the\Center\of\the\chain\-\ans✔Alpha\Carbon
The\alpha\carbon\is\the\central\carbon\on\an\amino\acid\that\holds\together\the\other\
groups\of\the\amino\acid.\It\is\always\attached\to\the\amino\group,\the\carboxyl\group,\the\
side\chain,\and\a\single\hydrogen.\It\is\part\of\the\backbone\of\the\amino\acid\and\is\found\
in\every\amino\acid.
Given\the\following\amino\acid\structure,\what\is\the\strongest\intermolecular\force\it\
would\participate\in\to\stabilize\a\protein\structure?
Ionic\bond
Disulfide\bond
Hydrogen\bond
Hydrophobic\interaction\-\ans✔Hydrophobic\interaction
QUESTIONS AND ANSWERS
Which\level\of\protein\structure\is\disrupted\through\the\hydrolysis\of\peptide\bonds?
Quaternary
Tertiary
Primary
Secondary\-\ans✔Primary
The\primary\structure\of\a\protein\is\the\sequence\of\amino\acids\held\together\by\peptide\
bonds.\Peptide\bonds\are\formed\by\dehydration\reactions\and\disrupted\by\hydrolysis.
A\mutation\in\the\beta-hemoglobin\gene,\which\results\in\the\replacement\of\the\amino\
acid\glutamate\in\position\6\with\the\amino\acid\valine,\leads\to\the\development\of\sickle\
cell\anemia.\The\structures\of\glutamate\and\valine\are\shown\below.
If\the\beta\hemoglobin\gene\in\a\patient\with\sickle-cell\anemia\were\to\be\edited\so\that\
the\valine\in\position\6\was\replaced\with\a\different\amino\acid,\which\replacement\for\
valine\would\be\expected\to\have\the\best\clinical\outcome,\in\theory,\for\the\patient?\
(Assume\the\valine\can\potentially\be\replaced\with\any\amino\acid\other\than\
glutamate.)\-\ans✔The\original\amino\acid\in\a\healthy\patient\is\glutamate,\which\is\
negatively\charged.\The\mutated\amino\acid\is\valine,\which\is\non-polar.\Valine\is\
causing\sickle\cell\anemia.\The\best\amino\acid\to\replace\valine\so\that\the\patient\is\
healthy\again\would\be\the\one\most\like\glutamate,\so\any\negatively\charged\amino\
acid.
Secondary,\tertiary,\and\quaternary\levels\of\protein\structure\can\all\be\impacted\by\
exposing\a\protein\to\which\treatment?
Change\of\a\hydrophobic\amino\acid\to\a\different\hydrophobic\amino\acid
Addition\of\a\reducing\agent
Placement\of\the\protein\in\a\solution\with\a\low\pH
,Increase\in\the\concentration\of\the\protein\in\solution\-\ans✔Placement\of\the\protein\in\a\
solution\with\a\low\pH
Changes\in\pH\affect\hydrogen\bonds\and\ionic\bonds.\Hydrogen\bonds\in\the\backbone\
of\amino\acids\occur\in\secondary\structure,\and\both\hydrogen\bonds\and\ionic\bonds\
occur\in\the\side\chains\of\amino\acids\in\tertiary\structure.
An\increase\in\beta-pleated\sheet\structure\in\some\brain\proteins\can\lead\to\an\increase\
in\amyloid\deposit\formation,\characteristic\of\some\neurodegenerative\diseases.\What\is\
the\primary\biochemical\process\that\follows\the\increase\in\beta-pleated\sheet\structure\
that\leads\to\the\development\of\the\amyloid\deposits?
An\increase\in\glycogen\formation\in\the\brain\cells
Aggregation\of\the\proteins\in\the\brain
Secretion\of\glucagon,\leading\to\excessive\ketogenesis
An\increase\in\anaerobic\metabolism\of\glucose\in\the\brain\-\ans✔Aggregation\of\the\
proteins\in\the\brain
This\question\is\describing\changes\in\protein\structure.\Aggregation\occurs\when\
proteins\clump\together\inappropriately,\causing\plaques\like\amyloid\deposits\to\
accumulate.
Which\level\of\protein\structure\is\determined\by\the\sequence\of\amino\acids?
Secondary\structure
Quaternary\structure
Tertiary\structure
Primary\structure\-\ans✔Primary\structure
The\primary\structure\of\a\protein\is\simply\the\sequence\of\amino\acids\held\together\by\
peptide\bonds.
Which\force\is\most\influential\in\determining\the\secondary\structure\of\a\protein?
Hydrophobic\effect
Disulfide\bonding
Hydrogen\bonding
, Electrostatic\interactions\-\ans✔Hydrogen\bonding
The\secondary\structure\of\a\protein\is\built\by\hydrogen\bonds\between\the\carboxyl\
groups\and\amino\groups\on\the\backbones\of\the\amino\acids.
Which\amino\acid\would\most\likely\participate\in\hydrogen\bonds?\-\ans✔Amino\Acid\
structure\4
This\is\a\polar,\uncharged\amino\acid\due\to\the\OH\group\on\the\side\chain.\Polar,\
uncharged\amino\acids\containing\oxygen\or\NH\groups\make\hydrogen\bonds.
Which\portion\of\the\amino\acid\is\inside\the\box?
\
The\box\is\surrounding\the\section\below\the\Alpha\Carbon\-\ans✔Side\Chain
The\side\chain\is\the\variable\group\of\the\amino\acid,\also\called\the\R\group.\Every\
amino\acid\has\the\same\amino\group,\carboxylic\acid\group,\and\an\alpha\carbon,\but\
the\side\chain\is\different.
Which\pair\of\amino\acids\will\most\likely\interact\through\hydrophobic\forces\between\
their\side\chains?\-\ans✔Both\of\these\amino\acids\are\non-polar\and\therefore\can\
interact\together\with\a\hydrophobic\interaction.\Please\note\that\the\"S"\in\the\amino\acid\
on\the\right\is\non-polar,\while\the\"SH"\group\in\answer\choice\D\is\polar.\The\S\must\
have\an\H\to\be\polar\and\is\otherwise\non-polar.
Which\portion\of\the\amino\acid\is\inside\the\box?
The\box\is\over\the\Carbon\at\the\Center\of\the\chain\-\ans✔Alpha\Carbon
The\alpha\carbon\is\the\central\carbon\on\an\amino\acid\that\holds\together\the\other\
groups\of\the\amino\acid.\It\is\always\attached\to\the\amino\group,\the\carboxyl\group,\the\
side\chain,\and\a\single\hydrogen.\It\is\part\of\the\backbone\of\the\amino\acid\and\is\found\
in\every\amino\acid.
Given\the\following\amino\acid\structure,\what\is\the\strongest\intermolecular\force\it\
would\participate\in\to\stabilize\a\protein\structure?
Ionic\bond
Disulfide\bond
Hydrogen\bond
Hydrophobic\interaction\-\ans✔Hydrophobic\interaction
