Biological And Biochemical Foundations Of Living S
Biological and Biochemical Foundations of Living S
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Biological and Biochemical Foundations of Living Systems || with Complete Solutions.
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Biological and Biochemical Foundations of Living S
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Biological And Biochemical Foundations Of Living S
Amino Acid and Side Groups correct answers - Negative Side Groups = Acidic
- Positive Side Groups = Basic
Absolute Configuration correct answers refers the R/S naming convention. Some amino acids are R, and some are S.
Relative Configuration correct answers - D/L naming convention.
- All b...
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Biological and Biochemical Foundations of Living Systems ||
with Complete Solutions.
Amino Acid and Side Groups correct answers - Negative Side Groups = Acidic
- Positive Side Groups = Basic
Absolute Configuration correct answers refers the R/S naming convention. Some amino acids are
R, and some are S.
Relative Configuration correct answers - D/L naming convention.
- All biologically produced amino acids are in the L configuration.
Conformational stability correct answers - Temperature: Denatures second, third, and fourth
tertiary
- pH: Third and fourth; Destroys ionic bonds:+ & - interactions
- Chemicals: Denatures Hydrogen bonds1-4
- Enzyme: Also denatures them except primary
Electrophoresis Separation correct answers - used to separate complex mixtures of proteins
- depends on the existence of a negative net charge.
Isoelectric Point; Zwitterion Point correct answers pH at which the molecule does not have a net
charge.
- Amino acids that carry two Nitrogen bases ( Asparagine (N), Glutamine (Q), Tryptophan (W))
Enzymatic cofactor and coenzyme correct answers - Coenzyme
* Tend to be small organic molecules (vitamins), NAD+, FAD, and coenzyme A
* Water soluble vitamin: B & C
* Fat soluble vitamins: ADEK
- Cofactors
* Nonorganic molecule (minerals) whose presence is necessary for the proper function of an
enzyme.
* Ex) Mg2+, FAD, Heme
- In both cases, these regulators induce a conformational change in the enzyme that promote its
activity. Tightly bound cofactors and coenzymes that are necessary for enzyme function are
termed prosthetic groups.
B Vitamins correct answers - Coenzymes
- familiarity with this table will make biochemistry passages easier
Induced fit model VS. Lock and Key correct answers - Lock and Key model
* Active site of enzyme fits exactly around substrate
* No alteration to tertiary or quaternary structure of enzyme
* Less accurate model
,- The induced fit model holds that the shape of the active site is altered during the course of
substrate binding
* Requires energy; endergonic reaction
* Tertiary and quaternary structure is modified for enzyme to function.
Ligase correct answers - catalyzes the formation of a single bond between two substrates through
the elimination of water.
- In DNA, it joins two separate nucleic acid strands by the formation of a phosphodiester bond.
Hydrolase correct answers catalyzes a reaction opposite to the sort catalyzed by a ligase: the
hydrolysis of a covalent bond.
Enzyme Active Site correct answers - is stabilized by non-covalent intramolecular interactions.
- Non-covalent intramolecular interactions are affected by heat and pH, amongst other things.
Michaelis-Menten Constant correct answers - shows the concentration of the substrate when the
reaction velocity is equal to one half of the maximal velocity for the reaction. It can also be
thought of as a measure of how well a substrate complexes with a given enzyme
- Inverse Equation: Y = mx+b
- x = 1/[S]
- km = (slope)*(1/y-intercept)
- Catalytic Efficiency= Kcat/ Km;
Catalytic Efficiency correct answers - Higher Kcat; lower Km = Higher catalytic efficiency
- function by lowering the activation energy of a reaction.
- Do NOT affect the position or the direction of equilibrium
Ex) The reaction S⇋P would proceed at an increased rate with the addition of an enzyme
catalyst.
Allosteric Enzymes correct answers - Bind modulators in a non-covalent; reversible at specific
sites, and are characterized by conformational changes upon binding.
- Covalent bonds are not readily reversible
Classes of Reversible Inhibition correct answers - Reversible = non-covalent binding
- Competitive: compete for the active site; preventing substrates from binding
- Non-competitive: Bind to a site distinct from the active site; Either the E or the ES
- Uncompetitive: Bind to a site distinct from the active site; only to the ES complex
Competitive Inhibitor correct answers - Compete for the active site; preventing substrates from
binding
- Inhibitor competes with substrate for space on the enzyme
- Inc Km but no difference in Vmax
- Enzyme may not be effective in low substrate concentration
Non-Competitive Inhibitor correct answers - Bind to a site distinct from the active site; Either the
E or the ES
, - Acts as both competitive and uncompetitive inhibitor
- Inc Km & dec. Vmax
- Inc Km, enzyme will also be inhibited at low concentrations
Uncompetitive Inhibitor correct answers - Bind to a site distinct from the active site; only to the
ES complex
- Inhibits the enzyme to turn the substrate into a product
- As you increase the concentration of inhibitors, you see a decrease in Vmax
- Even if you add more substrates, you will not be able to overcome the inhibition
- The enzyme will be effective at low substrate concentration
Histidine correct answers - Pka ≈6.5≈ close to Physiological pH 7.4
- Ph<PKA: protonated
- Ph>PKA: deprotonated
- It can stabilize and destabilize a substrate
- Found in seconday protein structure known as alpha helix § Coiled up polypeptide chain
§ Proline introduces kinks into this
- Known as alpha helix breakers
Cysteine & or Cystine correct answers - "e" stands for electrons when you are in the reduced
form
- If cystein's side chain are in close proximity then they can form disulfide bridge
- Intracellular = Reduced form = Antioxidants
Chirality correct answers - when light hit that protein,
the chiral carbon will rotate to that light.
- All 20 amino acids have it EXCEPT Glycine
Covalent Modification correct answers
"Small" Protein Modification correct answers - it can make certain proteins acidic, polar, non
polar
Zymogens correct answers
Suicide Inhibitors correct answers
Autosomal Inheritance correct answers - Each offspring receives one allele from the father and
one from the mother.
X-Linked Inheritance correct answers - Males receive one allele from the mother (on the X
chromosome) and none from the father (since the father provides the Y chromosome and no X
chromosomes). In contrast females receive one allele from the father and one allele from the
mother.
Chief Cells in the stomach correct answers Produce pepsinogen and Gastric Lipase
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