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LBT - Lebensmittel und Biotechnologie • Thema anzeigen - prüfung
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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 23.06.2016, 13:50 
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Registriert: 04.10.2009, 17:30
Beiträge: 26
Prüfung vom 23.06.2016, keine Überraschungen

1) Basic amino acids / Peptide bond / Ramachandran plot
2) To obtain the overall amino acid composition of a protein / Three supersecondary structures / Definition of domain
3) Explain principle & applications of yeast display / phage display
4) CD spectroscopy & applications
5) Error-prone PCR / Saturation mutagenesis / Divergent evolution + example
6) Km, Kcat, kcat/Km / pre-steady & steady state

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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 04.10.2017, 09:37 

Registriert: 23.01.2012, 10:47
Beiträge: 8
Zur Prüfung am 28.09.2017 kamen nur bereits gepostete Fragen.
Danke für die Sammlung!

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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 24.06.2019, 16:20 

Registriert: 30.01.2014, 12:33
Beiträge: 1
Hier wäre eine Ausarbeitung der Altfragen, die sich hier im Forum herumtreiben. Viel Erfolg, Leute! :D

Exam questions.docx [1.91 MiB]
355-mal heruntergeladen
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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 11.07.2019, 14:28 

Registriert: 30.10.2015, 14:09
Beiträge: 3
First of all thanks to everyone who posted the questions. Those cover the exam pretty good.
Questions that were shared before are just mentioned. For details look at posts before.
Here are the questions from today:

Amino acid question:
1. Structure, 3-letter code and full name of K, F, E
2. Draw the Dipeptide Gln-Tyr
3. Which amino acids have two chiral centers? Name and structure and mark the chiral centers.

Peptide bond: relationship of the properties of a peptide bond to protein folding and what are cis- and trans-configurations in this relation.

Van der Waals
Hydrogen bonds

DSC, principle, scheme of apparatus, draw a typical diagram, explain Tm and how you get it.

How many mutant proteins do you get if you randomize 4 amino acid positions by saturation mutagenesis? Explain your calculation.
Describe the differences between rational protein design and directed evolution.

Michaelis Menten kinetic question was quite detailed. I can't recall everything but:
Describe the principle of a Michaelis Menten kinetic. Explain the parameters and how you get them. Explain the initial rate and product inhibition in a reversible Michaelis Menten reaction.

Each paragraph were 5 points resulting in 30 points total. Passed >15

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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 24.06.2022, 17:25 

Registriert: 22.09.2014, 13:38
Beiträge: 2

1. Write down the full name, three letter code and structure of the following amino acids: T, R, Q!

2. Draw the structure of the dipeptide Val-Trp!

3. Which 2 of the 20 proteinogenic amino acids have a second chiral centre? Draw rheir structure and mark the second chiral centre!

4. Describe the structure of an alpha helix! Which forces stabilize the structure?

5. Describe the beta-turn!

6. What are supersecondary structures? Name 2 examples!

7. Describe the following non-covalent interactions: Van der Waals and H-bonds

8. DSC:
- describe the principle of the measurement
- draw a scheme of such an apparatus
- draw a typical diagram
- What is Tm and how can it be determined from such an experiment?

9. How many mutants do you have to screen if you want to randomize 7 different amino acid positions in a protein? Explain your calculation!

10. Describe the differences between rational design and directed evolution!

11. Describe yeast display and its major applications!

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 Betreff des Beitrags: Re: prüfung
 Beitrag Verfasst: 07.07.2022, 16:59 

Registriert: 04.01.2021, 17:19
Beiträge: 1

1. Draw peptide: KSLP
2. Draw the structure, write the whole name, 3-letter and 1-letter code for the AA that are negatively charged in neutral pH.
3. Describe H-bond and salt bridge.
4. Describe beta-sheet structure. How is it stabilized? In which direction point the side chains?
5. Describe the principles, method and lab applications for directed evolution.
6. You perform saturation mutagenesis on 3 amino acid sites of a protein. How many unique protein variants will you obtain? Explain the calculation.
7. What is convergent evolution and what divergent evolution?
8. Describe cooperative binding, draw the alpha versus [ligand] plot and describe why is this a key regulatory mechanism in nature with the help of this plot. How can you detect binding of multiple ligands to identical binding sites on one molecule?
(this question was really random and unexpected)

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