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Translation, Enzyme kinetics/catalysis exam 2025 LATEST QUESTIONS AND DETAILS ANSWERS GR, Exams of Nursing

Chamberlain College of NursingNursing

Translation, Enzyme kinetics/catalysis exam 2025 LATEST QUESTIONS AND DETAILS ANSWERS GRADED A+

Typology: Exams

2024/2025

Available from 05/03/2025

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Translation, Enzyme kinetics/catalysis exam 2025
LATEST QUESTIONS AND DETAILS ANSWERS
GRADED A+
Central dogma - {ASNWER}-Dna replicates and transcribes into RNA which is translated into proteins. The
central dogma of molecular biology describes the flow of genetic information within a biological system.
It involves three main processes:
DNA Replication: The process where DNA is copied to produce identical DNA molecules. This is essential
for cell division and inheritance.
Transcription: The process where a segment of DNA is copied into RNA (specifically messenger RNA or
mRNA). This occurs in the nucleus (in eukaryotes).
Translation: The process where mRNA is used as a template to synthesize proteins. This occurs in the
cytoplasm, where ribosomes translate the mRNA sequence into a corresponding amino acid sequence to
form proteins.
The central dogma can be summarized as: DNA โ†’ RNA โ†’ Protein.
True or false: the central dogma all occurs within the nucleus - {ASNWER}-FALSE: translation occurs in
the cytoplasm. False: The central dogma does not all occur within the nucleus. While DNA replication
and transcription (the process of making mRNA from DNA) occur in the nucleus, translation (the process
of synthesizing proteins from mRNA) occurs in the cytoplasm, specifically at the ribosomes
Translation - {ASNWER}-Ribosome-mediated production of polypeptide whose amino acid sequence is
specified by the nucleotide sequence in an mRNA
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Download Translation, Enzyme kinetics/catalysis exam 2025 LATEST QUESTIONS AND DETAILS ANSWERS GR and more Exams Nursing in PDF only on Docsity!

Translation, Enzyme kinetics/catalysis exam 2025

LATEST QUESTIONS AND DETAILS ANSWERS

GRADED A+

Central dogma - {ASNWER}-Dna replicates and transcribes into RNA which is translated into proteins. The central dogma of molecular biology describes the flow of genetic information within a biological system. It involves three main processes: DNA Replication: The process where DNA is copied to produce identical DNA molecules. This is essential for cell division and inheritance. Transcription: The process where a segment of DNA is copied into RNA (specifically messenger RNA or mRNA). This occurs in the nucleus (in eukaryotes). Translation: The process where mRNA is used as a template to synthesize proteins. This occurs in the cytoplasm, where ribosomes translate the mRNA sequence into a corresponding amino acid sequence to form proteins. The central dogma can be summarized as: DNA โ†’ RNA โ†’ Protein. True or false: the central dogma all occurs within the nucleus - {ASNWER}-FALSE: translation occurs in the cytoplasm. False: The central dogma does not all occur within the nucleus. While DNA replication and transcription (the process of making mRNA from DNA) occur in the nucleus, translation (the process of synthesizing proteins from mRNA) occurs in the cytoplasm, specifically at the ribosomes Translation - {ASNWER}-Ribosome-mediated production of polypeptide whose amino acid sequence is specified by the nucleotide sequence in an mRNA

The 5 components required for translation - {ASNWER}-1. mRNA

  1. Amino Acids
  2. tRNAs
  3. ribosomes
  4. auxiliary factors The five components required for translation are:
    1. mRNA (messenger RNA) โ€“ carries the genetic information from DNA and serves as the template for protein synthesis.
    2. Amino acids โ€“ the building blocks of proteins, specified by the mRNA codons.
    3. tRNAs (transfer RNAs) โ€“ adaptors that bring the correct amino acids to the ribosome according to the mRNA codon sequence.
    4. Ribosomes โ€“ the molecular machines that facilitate protein synthesis by reading the mRNA and catalyzing the formation of peptide bonds between amino acids.
    5. Auxiliary factors โ€“ additional proteins and molecules, such as initiation, elongation, and release factors, that assist with the translation process. These components work together to ensure accurate and efficient translation of the genetic code into functional proteins. features of mRNA - {ASNWER}-1. capped at 5' end, polyadenylated at 3' end
  5. translated in 5' to 3' direction
  6. eukaryotic mRNAS are monocistronic (one mrna = one specific protein) where prokaryotics are polycistronic (one mrna = lots of protein types) Three stop codons - {ASNWER}-UAA, UAG, UGA (U Go Away, U Are Gone, U Are Away) Start codon - {ASNWER}-AUG (met) what does it mean for genetic code to be degenerate - {ASNWER}-amino acids are specificed by multiple codons not just one Which two amino acids are specified by a single codon only - {ASNWER}-Met (AUG) and Trp

idiefies the initiation codon and functions in codon anticodon interaction large subunit of Eukaryotic ribosome - {ASNWER}-60s catalyzes peptide bond formation between adjacent amino acids S total of small subunit and large subunit ribosomes put together - {ASNWER}-80s in prokaryotes 70s What do antibiotics interfere with - {ASNWER}-prokaryotic translation Primary structure - {ASNWER}-amino acid sequence of protein Secondary structure - {ASNWER}-Stable spatial arrangements held by HYDROGEN BONDS between backbone amide and carbonyl groups can be alpha helix, beta sheet or beta turn tertiary structure - {ASNWER}-overall conformation of polypeptie chain determined by hydrophobic interactions and hydrogen bonds the four common kinds of tertiary structure proteins - {ASNWER}-1. globular proteins

  1. fibrous proteins
  2. integral membrane proteins
  3. intrinsically disorder proteins Quaternary structure - {ASNWER}-WHen proteins have multiple subunits. Internal ribosome entry site (IRES) - {ASNWER}-an alternative mechanism to initiate translation and is commonly used by viruses that infect cells global regulation - {ASNWER}-affects regulations of ALL cellular mRNAS
  • occurs through eIF4E (increase global)
  • also by phosphorylation of eIF2 (decrease global) Specific regulation - {ASNWER}-positive or negative translation regulation of specific mRNAS
  • regulation through the 5'UTR or 3'UTR Steps of translation - {ASNWER}-initiation, elongation, termination what are the 4 components needed for translation initiation - {ASNWER}-1. mRNA (with a 5' cap and poly a tail)
  1. eIF4-cap binding complex
  2. 43S preinitiation complex
  3. Large ribosomal subunit What is apart of the 43S preinitation complex - {ASNWER}-1. the small ribosomal subunit
  4. Met-tRNA
  5. EIF2-GTP
  6. eIF2b-nucleotide exchange factor that exchanges GDP for GTP on eiF Steps of translation initiation - {ASNWER}-1. Binding of 43S preinitation complex to cap structure
  7. Scanning of 43 preinitiation complex to initiation AUG codon
  8. Recognition of AUG codon by Met-tRNA then hydrolysis of GTP to GDP
  9. Release of many initiation factors
  10. Joining of large ribosomal subunit containing eIF5B-GTP to small subunit initiation complex Kozak sequence - {ASNWER}-ACCAUGG that helps ribosomes find initiation sequence At the end of initiation what is the status of the E P and A site? - {ASNWER}-E and A remain empty and Met-tRNA Is position in P site

Release factors (eRF) - {ASNWER}-Recognize stop codons in the A site and are proteins not tRNA Steps of translation termination - {ASNWER}-1. eRF bound to GTP recognizes stop codons and the hydrolysis of GTP releases protein and tRNA from ribosome

  1. accessory factors assist with disassembly of ribosome into small and large (requires atp) Catalysts accelerate reactions by - {ASNWER}-Lowering activation energy to reach transition state What three things do catalysts NOT do - {ASNWER}-1. do not change free energy of substrates/products
  2. do not shift keq (equilibrum)
  3. do not get consumed What do enzymes bind to? - {ASNWER}-the TRANSITION STATE 5 ways enzymes accelerate the rate of reaction - {ASNWER}-1. proximity effects
  4. stabilization of transition state
  5. acid-base catalysis (Donating H+ and deprotonating)
  6. covalent catalysis
  7. prosthetic groups (metals drawing electrons to increase electronegativity and make it more reactive) What do catalysts reduce in the reaction - {ASNWER}-the free energy of activation Why? because it reduces the Free Energy of Activation which increases rate K= - {ASNWER}-[products]/[substrate] If Keq is positive - {ASNWER}-Delta g is negative and the reaction proceeds forward if its 0 its at equilibrum

if keq is negative - {ASNWER}-delta g is positive and the reaction proceeds in reverse True of false: in the thermodynamically favorable reaction the substrates must be less stable than the products - {ASNWER}-TRUE What reactions does entropy favor - {ASNWER}-reactions where one reactant is converted into multiple products *remember entropy is need to spread) Active site - {ASNWER}-where the substrate binds to the enzyme Catalysis by proximity and orientation - {ASNWER}-increases intramolecular reactions between groups when put closer together and puts in proper conformation to bond General acid base catalysis - {ASNWER}-speeds up reaction by donating or abstraction proteins. Charge development is unfavorable so they neutralize to help product formation Covalent catalysis - {ASNWER}-When a covalent enzyme-substrate intermediate is formed during the reaction. The intermediate reduce thea ctivation energy of later transition states Prosthetic group catalysis - {ASNWER}-uses a cofactor in the enzyme active site. a cation will increase electronegative character drawing electrons towards them which speeds up reaction Oxidoreductases - {ASNWER}-catalyzes transfer of electrons (hydride ions or H atoms) examples: NAD+ and dehydrogenases transferases - {ASNWER}-catalyzes Group transfer reactions kinase (transfers phosphate groups) hydrolases - {ASNWER}-catalyzes hydrolysis reactions (transfer of functional groups to water)

Substrates with a high Km have: - {ASNWER}-a weaker affinity of the enzyme and a greater ability to be convereted into products once bound. Faster K-1 and K2 and slower K substrates with a low Km have: - {ASNWER}-a strong affinity of the enzyme and a weak ability to be convereted into products once bound Faster K1 and slower K-1 and K When do we see zero order reactions - {ASNWER}-If [S] is equal to Km True of false Km will always be higher than Kd - {ASNWER}-TRUE If [S]= Km - {ASNWER}-equation is v0=1/2vMax if [S] is greater than Km - {ASNWER}-vo=vmax if [S] is less than Km - {ASNWER}-v0= vmax[s]/Km What does the Y/X intercept mean on a double-reciprocal plot (linear line) - {ASNWER}-Y= 1/Vmax x= - 1/Km what is the slope on a double reciropcial plot - {ASNWER}-Km/Vmax True of false: for the greatest regulation of a given enzyme catalyzed reaction Km should be less than the substrate - {ASNWER}-FALSE Km should be near or greater than substrance concentration for greatest regulation How do you find out the Km of enzymes with multiple substrates - {ASNWER}-Saturate the solution with one so it becomes first order and doesnt depend on that step

Allosteric enzymes - {ASNWER}-have both an active site for substrate binding and an allosteric site for binding of an allosteric effector (activator, inhibitor) cooperativity - {ASNWER}-A kind of allosteric regulation whereby a shape change in one subunit of a protein caused by substrate binding is transmitted to all the other subunits, facilitating binding of additional substrate molecules to those subunits.

  • Mutiple interacting subunits Concerted model (cooperativity) - {ASNWER}-enzyme subunits in two states R or T The greater the cooperativity the more likely its concerted model Sequential model (cooperativity) - {ASNWER}-enzyme subunits in three states R intermediate or T. Usually for enzymes with more than 2 subunits an allosteric effector negatively regulates enzymes by binding to the - {ASNWER}-T state an allosteric effector positively regulates enzymes by binding to the - {ASNWER}-R state Do cooperative enzymes follow michaelis-menten kinetics - {ASNWER}-NO. in cooperative enzymes the Km is decreased or vmax increases competitive inhibition - {ASNWER}-substance that resembles the normal substrate competes with the substrate for the active site Reversible inhibitors - {ASNWER}-are a type of competitive inhibition THey are similar to substrate and bind to enzyme to form EI that doesnt result in catalysis. As the substrate becomes large I becomes less effective. I and S COMPETE. True of false: vmax is unaffected by a competitive inhibitor - {ASNWER}-TRUE

First order - {ASNWER}-When the substrate is in EXCESS second order - {ASNWER}-When both reactants are LIMITING