biology

Protein–protein interaction screening

Protein–protein interaction screening is a biology topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Protein–protein interaction screening rather than just read about it. In short: Protein–protein interaction screening refers to the identification of Protein–protein interaction with high-throughput screening methods such as computer- and/or robot-assisted plate reading, flow cytometry analyzing. The interactions between proteins are central to virtually every process in a living cell.

Key takeaways

Protein–protein interaction screening belongs to biology; place it in that map before memorising details.
Learn the definition first, then one example that makes the definition concrete.
Connect Protein–protein interaction screening to a quantity you can measure, compute or draw — that is where exam questions come from.
Reproduce the core statement of Protein–protein interaction screening from memory before moving on to harder problems.

Reference excerpt

Protein–protein interaction screening refers to the identification of Protein–protein interaction with high-throughput screening methods such as computer- and/or robot-assisted plate reading, flow cytometry analyzing. The interactions between proteins are central to virtually every process in a living cell. Information about these interactions improves understanding of diseases and can provide the basis for new therapeutic approaches.

Methods to screen protein–protein interactions Though there are many methods to detect protein–protein interactions, the majority of these methods—such as co-immunoprecipitation, fluorescence resonance energy transfer (FRET) and dual polarisation interferometry—are not screening approaches.

Ex vivo or in vivo methods Methods that screen protein–protein interactions in the living cells. Bimolecular fluorescence complementation (BiFC) is a technique for observing the interactions of proteins. Combining it with other new techniques, dual expression recombinase based (DERB) methods can enable the screening of protein–protein interactions and their modulators. The yeast two-hybrid screen investigates the interaction between artificial fusion proteins inside the nucleus of yeast. This approach can identify the binding partners of a protein without bias. However, the method has a notoriously high false-positive rate, which makes it necessary to verify the identified interactions by co-immunoprecipitation.

In-vitro methods The tandem affinity purification (TAP) method allows the high-throughput identification of proteins interactions. In contrast with the Y2H approach, the accuracy of the method can be compared to those of small-scale experiments (Collins et al., 2007) and the interactions are detected within the correct cellular environment as by co-immunoprecipitation. However, the TAP tag method requires two successive steps of protein purification, and thus can not readily detect transient protein–protein interactions. Recent genome-wide TAP experiments were performed by Krogan et al., 2006, and Gavin et al., 2006, providing updated protein interaction data for yeast organisms. Chemical crosslinking is often used to "fix" protein interactions in place before trying to isolate/identify interacting proteins. Common crosslinkers for this application include the non-cleavable [NHS-ester] crosslinker, [bis-sulfosuccinimidyl suberate] (BS3); a cleavable version of BS3, [dithiobis(sulfosuccinimidyl propionate)](DTSSP); and the [imidoester] crosslinker [dimethyl dithiobispropionimidate] (DTBP) that is popular for fixing interactions in ChIP assays.

References

External links HPRD Human Protein Reference Database, a (manually) curated database of human protein information with visualization tools IntAct Interaction Database, a public repository for manually curated molecular interaction data from the literature DIP Database of Interacting Proteins, a manual and automatic catalog of experimentally determined interactions between proteins MIPS Mammalian Protein–Protein Interaction Database, the MIPS mammalian protein–protein interaction database

Worked examples

Example 1 — a first encounter with Protein–protein interaction screening

Start with the simplest possible case. Write down what Protein–protein interaction screening claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In biology, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Protein–protein interaction screening before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Protein–protein interaction screening ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Protein–protein interaction screening

In research: Protein–protein interaction screening appears in biology research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Protein–protein interaction screening in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Protein–protein interaction screening is common in secondary-school and first-year university syllabi. It links to neighbouring topics Biochemistry methods, Proteomics, Signal transduction, so understanding it makes those chapters shorter.
In everyday life: Look for Protein–protein interaction screening outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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How to study Protein–protein interaction screening in 20 minutes

Read the reference excerpt below once, without taking notes.
Close the page and write down what Protein–protein interaction screening means in your own words.
Compare your version with the excerpt and mark what you missed.
Work through the three examples above with pen and paper.
Explain Protein–protein interaction screening out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Protein–protein interaction screening in simple terms?

Why does Protein–protein interaction screening matter?

Because it connects several biology ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Protein–protein interaction screening?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Protein–protein interaction screening.