Biochemistry Study Questions and Answers
Verifies 100% Correct
Amphoteric
accept or donate protons
-Under acidic conditions, gain protons
-Under basic conditions, lose protons
NH3 would be protonated to NH4+.
At a pH= 1, what would happen to an AA?
Amino would be protonated and carboxyl would be deprotonated.
At a pH=7, what would happen to an AA?
The carbonyl group would be deprotonated.
At a pH=10, what would happen to AA?
Condensation or dehydration (removal of water)
How to peptide bonds form? (Two processes)
N-terminus
What end does translation start at?
Primary
Linear arrangement to encode for higher levels
-Sequencing can be done here
Secondary
Hydrogen bonding between alpha (Keratin) and beta (fibroin) kinky :)
,Tertiary
3D structure of hydrophobic areas facing inward and hydrophilic facing outward
(disulfide bond)
Quart-nary
More than one polypeptide with subunits involved
For example, hemoglobin and immunoglobin
More stable by lower surface area, lower amount of DNA needed, Bring catalytic sites
closer
Cooperatively or allosteric effects
Several Roles in 4th structure
Prosthetics
organic (vitamins) or metal (Fe)
For example, lipoproteins, glycoproteins, and nucleoproteins along with heme
Denaturation
Interactions between the hydrophobic interactions (higher temperature) or bonds
broken between disulfide bridges and HB (urea) lessens a proteins ability to function
SDS
Detergents that solubilize proteins, disrupting covalent bonds, and promoting
denaturation
What do enzymes do?
Does not change H, G, or Keq
Lower activation energy
Increases rate of reaction
,Appears in reactants and products
pH and temperature
Specific
LIL' HOT
Acronym for type of enzymes
Ligases
addition or synthesis that requires ATP
For example, synthase
Isomerases
rearrangement of bonds
For example, oxireductase, transferase, or ligases
Lyases
cleavage of a single molecule without water
For example, sythnases
Hydrolyases
cleavages of a single molecule with water
For example, phosphates, peptidase, lipase, and nucleases
Oxireductase
NAD+, dehydrogenase, or reductase
Transferase
movement of functional group from one molecule to another
For example, aminotransferase for the TCA or Kinases with pi
, Michaelis Menton
Endergonic
Delta G is positive (non-spontaneous)
Exergonic
Delta G is negative (spontaneous) which can reduce energy when released
Yes mam! :)
Can enzymes provide a favorable microenvironment in terms of charge and pH
Hydrogen Bonding, Ionic Interactions, and transient covalent bonds
What interactions lie within an active site?
Lock n' Key
Already in an appropriate conformation for the substrate to bind
-No alternation of tertiary or quartnery structure
Induced Fit Model
The substrate induces a change in the shape of the enzyme (requires energy:
endergonic)
Alters between relaxed and tight phase
Apoenzyme
inactive form of enzyme without cofactor
Holoenzyme
active form of enzyme with cofactor
Cofactor
Verifies 100% Correct
Amphoteric
accept or donate protons
-Under acidic conditions, gain protons
-Under basic conditions, lose protons
NH3 would be protonated to NH4+.
At a pH= 1, what would happen to an AA?
Amino would be protonated and carboxyl would be deprotonated.
At a pH=7, what would happen to an AA?
The carbonyl group would be deprotonated.
At a pH=10, what would happen to AA?
Condensation or dehydration (removal of water)
How to peptide bonds form? (Two processes)
N-terminus
What end does translation start at?
Primary
Linear arrangement to encode for higher levels
-Sequencing can be done here
Secondary
Hydrogen bonding between alpha (Keratin) and beta (fibroin) kinky :)
,Tertiary
3D structure of hydrophobic areas facing inward and hydrophilic facing outward
(disulfide bond)
Quart-nary
More than one polypeptide with subunits involved
For example, hemoglobin and immunoglobin
More stable by lower surface area, lower amount of DNA needed, Bring catalytic sites
closer
Cooperatively or allosteric effects
Several Roles in 4th structure
Prosthetics
organic (vitamins) or metal (Fe)
For example, lipoproteins, glycoproteins, and nucleoproteins along with heme
Denaturation
Interactions between the hydrophobic interactions (higher temperature) or bonds
broken between disulfide bridges and HB (urea) lessens a proteins ability to function
SDS
Detergents that solubilize proteins, disrupting covalent bonds, and promoting
denaturation
What do enzymes do?
Does not change H, G, or Keq
Lower activation energy
Increases rate of reaction
,Appears in reactants and products
pH and temperature
Specific
LIL' HOT
Acronym for type of enzymes
Ligases
addition or synthesis that requires ATP
For example, synthase
Isomerases
rearrangement of bonds
For example, oxireductase, transferase, or ligases
Lyases
cleavage of a single molecule without water
For example, sythnases
Hydrolyases
cleavages of a single molecule with water
For example, phosphates, peptidase, lipase, and nucleases
Oxireductase
NAD+, dehydrogenase, or reductase
Transferase
movement of functional group from one molecule to another
For example, aminotransferase for the TCA or Kinases with pi
, Michaelis Menton
Endergonic
Delta G is positive (non-spontaneous)
Exergonic
Delta G is negative (spontaneous) which can reduce energy when released
Yes mam! :)
Can enzymes provide a favorable microenvironment in terms of charge and pH
Hydrogen Bonding, Ionic Interactions, and transient covalent bonds
What interactions lie within an active site?
Lock n' Key
Already in an appropriate conformation for the substrate to bind
-No alternation of tertiary or quartnery structure
Induced Fit Model
The substrate induces a change in the shape of the enzyme (requires energy:
endergonic)
Alters between relaxed and tight phase
Apoenzyme
inactive form of enzyme without cofactor
Holoenzyme
active form of enzyme with cofactor
Cofactor
