Principles of Biochemistry Test 1
3-D structure of a protein is determined by its - ANS-number one structure
a buffer machine has its greatest impact when the pH of the solution is around the - ANS-pKa of
the susceptible acid
a buffer generally consists of a - ANS-susceptible acid and its salt
Acids are proton donors or proton acceptors - ANS-proton donors
activation energy - ANS-the energy distinction among substrates and the transition nation
allosteric activators - ANS-provoke or boom the activity of an enzyme
allosteric effectors bind to allosteric web sites and modify enzymes by way of -
ANS-conformational adjustments
allosteric enzyme - ANS-an enzyme whose pastime is tormented by the binding of effector
molecule
allosteric has subunits - ANS-catalytic and regulatory subunits
allosteric inhibitors - ANS-make an enzyme less lively
allosteric web site - ANS-2nd regulatory website online distinct from the active website
alpha helix - ANS-proper passed coiled structure around a protracted primary axis, stabilized by
interchain hydrogen bonds
three.6 amino acid in line with flip
all facet chains project outward from the helix axis
amino terminal end - ANS-the cease of a peptide with a free alpha amino organization
amphiphilic (or amphipathic) molecules contain what organizations - ANS-polar and nonpolar
organizations
amyloids - ANS-series of improperly folded protein aggregates which are discovered in the
human frame
, an allosteric enzyme plot with reaction pace v substrate awareness is what shape -
ANS-sigmoidal (s fashioned)
an enzyme that contains its cofactors is - ANS-a holoenzyme
an enzyme that lacks its cofactors or prosthetic organization is an - ANS-apoenzyme
antiparallel beta sheets - ANS-polypeptide chain that folds to and fro with every section jogging
inside the contrary of that of its acquaintances
strands run in contrary N to C instructions
are amino acids soluble in water? - ANS-yes, very soluble
Are water insoluble molecules non-polar? - ANS-yes
arginine amino acid - ANS-high-quality facet chain
asparatic acid amino acid - ANS-terrible aspect chain
at very excessive temperatures, an enzyme - ANS-becomes greater volatile and denaturation
happens
beta-pleated sheets - ANS-form whilst distinct sections of the polypeptide chain run alongside
each different, every phase is a beta strand
stabilized by hydrogen bonds between C --O and -NH on adjacent strands
biological function of a protein depends on its - ANS-native conformation
Can a substrate bind whilst a aggressive inhibitor is also bound? - ANS-no
Can uncompetitive inhibition be triumph over by means of elevating the substrate awareness? -
ANS-no
carboxyl terminal quit - ANS-the stop of a peptide with a loose alpha carboxyl organization
catalytic allosteric subunit - ANS-in which substrate binds
catalytic constant (turnover number) - ANS-how speedy a given enzyme can catalyze a specific
reaction
catalytic constant equation - ANS-Vmax/[E]overall
3-D structure of a protein is determined by its - ANS-number one structure
a buffer machine has its greatest impact when the pH of the solution is around the - ANS-pKa of
the susceptible acid
a buffer generally consists of a - ANS-susceptible acid and its salt
Acids are proton donors or proton acceptors - ANS-proton donors
activation energy - ANS-the energy distinction among substrates and the transition nation
allosteric activators - ANS-provoke or boom the activity of an enzyme
allosteric effectors bind to allosteric web sites and modify enzymes by way of -
ANS-conformational adjustments
allosteric enzyme - ANS-an enzyme whose pastime is tormented by the binding of effector
molecule
allosteric has subunits - ANS-catalytic and regulatory subunits
allosteric inhibitors - ANS-make an enzyme less lively
allosteric web site - ANS-2nd regulatory website online distinct from the active website
alpha helix - ANS-proper passed coiled structure around a protracted primary axis, stabilized by
interchain hydrogen bonds
three.6 amino acid in line with flip
all facet chains project outward from the helix axis
amino terminal end - ANS-the cease of a peptide with a free alpha amino organization
amphiphilic (or amphipathic) molecules contain what organizations - ANS-polar and nonpolar
organizations
amyloids - ANS-series of improperly folded protein aggregates which are discovered in the
human frame
, an allosteric enzyme plot with reaction pace v substrate awareness is what shape -
ANS-sigmoidal (s fashioned)
an enzyme that contains its cofactors is - ANS-a holoenzyme
an enzyme that lacks its cofactors or prosthetic organization is an - ANS-apoenzyme
antiparallel beta sheets - ANS-polypeptide chain that folds to and fro with every section jogging
inside the contrary of that of its acquaintances
strands run in contrary N to C instructions
are amino acids soluble in water? - ANS-yes, very soluble
Are water insoluble molecules non-polar? - ANS-yes
arginine amino acid - ANS-high-quality facet chain
asparatic acid amino acid - ANS-terrible aspect chain
at very excessive temperatures, an enzyme - ANS-becomes greater volatile and denaturation
happens
beta-pleated sheets - ANS-form whilst distinct sections of the polypeptide chain run alongside
each different, every phase is a beta strand
stabilized by hydrogen bonds between C --O and -NH on adjacent strands
biological function of a protein depends on its - ANS-native conformation
Can a substrate bind whilst a aggressive inhibitor is also bound? - ANS-no
Can uncompetitive inhibition be triumph over by means of elevating the substrate awareness? -
ANS-no
carboxyl terminal quit - ANS-the stop of a peptide with a loose alpha carboxyl organization
catalytic allosteric subunit - ANS-in which substrate binds
catalytic constant (turnover number) - ANS-how speedy a given enzyme can catalyze a specific
reaction
catalytic constant equation - ANS-Vmax/[E]overall
