Biochem Review

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Amino Acid
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Non-polar Amino Acids
Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, and Proline
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Glycine
Gly, G
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Alanine
Ala, A
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Valine
Val, V
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Leucine
Leu, L
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Isoleucine
LIe, I
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Methionine
Met, M
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Proline
Pro, P
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Aromatic Hydrophobic
Tryptophan, Tyrosine, and PhenylAlanine
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Tryptophan
Trp, W
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Tyrosine
Tyr, Y
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Phenylalanine
Phe, F
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Polar
Serine, Threonine, Asparagine, Glutamine, and Cysteine
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Serine
Ser,S
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Threonine
Thr, T
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Asparagine*
Asn, N
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Glutamine
Gln, Q
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Cysteine
Cys, C
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Acidic
Aspartic Acid and Glutamic Acid
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Aspartic Acid (at a neutral pH, it would be a basic COO-)
Asp, D
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Glutamic Acid
Glu, E
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Basic
Arginine, Lysine, and Histidine
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Arginine
Arg, R
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Lysine *
Lys, K
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Histidine (at a neutral pH, one amino group is protonated)
His, H
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Amphoteric
accept or donate protons
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-Under acidic conditions, gain protons
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-Under basic conditions, lose protons
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NH3 would be protonated to NH4+.
At a pH= 1, what would happen to an AA?
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Amino would be protonated and carboxyl would be deprotonated.
At a pH=7, what would happen to an AA?
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The carbonyl group would be deprotonated.
At a pH=10, what would happen to AA?
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Condensation or dehydration (removal of water)
How to peptide bonds form? (Two processes)
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N-terminus
What end does translation start at?
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Primary
Linear arrangement to encode for higher levels
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-Sequencing can be done here
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Secondary
Hydrogen bonding between alpha (Keratin) and beta (fibroin) kinky :)
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Tertiary
3D structure of hydrophobic areas facing inward and hydrophilic facing outward (disulfide bond)
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Quart-nary
More than one polypeptide with subunits involved
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For example, hemoglobin and immunoglobin
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More stable by lower surface area, lower amount of DNA needed, Bring catalytic sites closer
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Cooperatively or allosteric effects
Several Roles in 4th structure
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Prosthetics
organic (vitamins) or metal (Fe)
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For example, lipoproteins, glycoproteins, and nucleoproteins along with heme
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Denaturation
Interactions between the hydrophobic interactions (higher temperature) or bonds broken between disulfide bridges and HB (urea) lessens a proteins ability to function
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SDS
Detergents that solubilize proteins, disrupting covalent bonds, and promoting denaturation
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What do enzymes do?
Does not change H, G, or Keq
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Lower activation energy
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Increases rate of reaction
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Appears in reactants and products
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pH and temperature
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Specific
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LIL' HOT
Acronym for type of enzymes
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Ligases
addition or synthesis that requires ATP
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For example, synthase
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Isomerases
rearrangement of bonds
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For example, oxireductase, transferase, or ligases
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Lyases
cleavage of a single molecule without water
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For example, sythnases
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Hydrolyases
cleavages of a single molecule with water
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For example, phosphates, peptidase, lipase, and nucleases
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Oxireductase
NAD+, dehydrogenase, or reductase
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Transferase
movement of functional group from one molecule to another
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For example, aminotransferase for the TCA or Kinases with pi
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Michaelis Menton
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Endergonic
Delta G is positive (non-spontaneous)
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Exergonic
Delta G is negative (spontaneous) which can reduce energy when released
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Yes mam! :)
Can enzymes provide a favorable microenvironment in terms of charge and pH
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Hydrogen Bonding, Ionic Interactions, and transient covalent bonds
What interactions lie within an active site?
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Lock n' Key
Already in an appropriate conformation for the substrate to bind
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-No alternation of tertiary or quartnery structure
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Induced Fit Model
The substrate induces a change in the shape of the enzyme (requires energy: endergonic)
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Alters between relaxed and tight phase
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Apoenzyme
inactive form of enzyme without cofactor
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Holoenzyme
active form of enzyme with cofactor
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Cofactor
Inorganic, such as metals and dietary minerals
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Coenzymes
Small and organic, such as NAD+, Coenzyme A, and vitamins
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Water Based Vitamins
B and C
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Fat Based Vitamins
A D E K
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Km
the lower the Km then the higher affinity for substrate (adding more substrate or enzyme will not affect Km because it strictly deals with ES complex)
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K2+K3/K1
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V0
(Vmax x [S]) / (Km +[S])
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Reaction Mechanism
E+S--> ES--> EP (K1 and K2) ... (K3)
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Lineweaver Plot
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Cooperatively
Allosteric Sites with a sigmoidal shaped curve
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For example, heme or PFK1 in glycolysis
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R State
Higher affinity for substrate
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T State
Lower affinity for substrate
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Temperature ( Higher-> denature)
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pH (pH= 7.4)
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Salinity ( Interrupts ionic and hydrogen bonding, slight change in conformation, which may lead to denaturing)
What are some local conditions that affect enzyme activity? (Name 3)
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Competitive
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Noncompetitive
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Uncompetitive
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Mixed
What are the four reversible inhibitors?
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Competitive
Binds directly to active site
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Increases the Km
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No change in Vmax
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Noncompetitive
Binds "equally" to either enzyme or ES complex
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Lowers Vmax