Since I cannot find a section for the new Biotech specialization here are the questions of todays exam to see how possible questions look like. Afterwards, I don't think that learning all of the examples in the slides makes sense and they are only there to aid the understanding.

Describe how to design a linker between two protein domains. Using an scFv as example, how can the necessary length of the linker be determined? What happens if the linker is very short? Which types of amino acids are well suited in such linkers, and which are less well suited?

Which molecular strategies can be applied to fight allergy and which kinds of proteins are used for this purpose? Name a few of them. Describe the mechanism of action of one of the antibodies that are relevant in the field.

Describe the main fields of applications of fusion proteins in research and therapy including 2 examples from each field. Which parameters are important for the design of a fusion protein?

Describe the molecular properties of alternative antigen-recognition scaffolds (other than antibodies). Which methods can be applied in engineering a protein into an antigen recognition scaffold?

The accumulation of mutations causes destabilization of a protein and/or compromised solubility and foldability. What strategies do we have to counter that?

Describe the major characteristics and prerequisites of “screening by selection”!

NAME: Matriculation number: _________________
6 Questions, 5 points each
27-30 points: sehr gut (1)
22-26 points: gut (2)
18-21 points: befriedigend (3)
15-17 points: genügend (4)
14 or less points: nicht genügend (please send us an email or talk to us (also in case you want to improve
your mark))
• Questions 1 and 2 will be marked by Florian Rüker
• Questions 3 and 4 will be marked by Gordana Wozniak-Knopp
• Questions 5 and 6 will be marked by Clemens Peterbauer
Don’t forget to write your name and matriculation number on every page
1. In the treatment of some diseases, the therapeutic strategy is to prevent the binding
between ligands and their receptors. How can this be achieved by engineered
proteins?
2. Describe two methods that can be used to generate fully human monoclonal
antibodies
3. Fusion proteins are commonly used for many different purposes. Briefly describe
fusion proteins designed for (1) therapeutic purposes, (2) facilitation of protein
purification and/or detection. Please refer to two examples in each category.
4. Describe the molecular properties of alternative antigen-recognition scaffolds (other
than antibodies). Which methods can be applied in engineering a protein into an
antigen recognition scaffold?
5. The accumulation of mutations causes destabilization of a protein and/or
compromised solubility and foldability. What strategies do we have to counter that?
6. Diversifying a sequence via error-prone PCR introduces point mutations randomly.
The diversity that can be achieved is, however, somewhat limited. Why?


The new questions are not in the summary. No guarantee that everything is right, and some answers kind of confusing but I hope it will still help some of you

EXAM 20.04.2021

1. Single-chain Fv fragments:
a. Describe which types of amino acids a preferentially used for the linker, and which
types should be avoided
b. What is the typical length of such a linker?
c. What happens when the linker is too short?

2.
a. List at least 4 of the most common types of vaccines that are currently used or
developed against SARS-CoV-2.
b. Describe how an mRNA vaccine is produced and how it is acting in vivo


3. Difficult-to-express proteins:
a. Why are difficult-to-express proteins of interest?
b. Which methods are used for engineering of difficult-to-express proteins? Which novel
analysis techniques have been developed to determine their structure?

4. Alternative binding scaffolds:
a. Which are their common properties?
b. In what aspects are they similar and how do they differ from antibodies?
c. Briefly describe 2 examples of alternative binding scaffolds.

5. What are the prerequisites for the high-throughput screening of “cells as bioreactors”?

6. Describe – in short words – two methods for laboratory recombination of genes!

Go Boku Beez Football!

Three questions were old, three were new or at the least two, by the exam today. We were 6 participants but about 20 in total, the others did the "Einführung in die Immunologie" exam I think.

Just from memory, the ~two new questions were something like this:

25.04.2023:

- What are obligate bispecific antibodies?
- How to perform recombination in the lab?

There was a bit more e. g. the real questions were longer but I forgot the specifies. Also the therapy question was in regards to designing Anti-VEGF, e. g. how would we go about this if we want to block the ligand-receptor binding aka engineer something there.