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SciCom – Limit Yourself to Once Message!
Published 5 days ago • 3 min read
A Central Concept in SciCom
Hi Reader, how do you find the core?
Okay, I threw you in at the deep end here.
“Finding the core” is, to my mind, one of the most essential aspects of any communication.
So, let me share a section of the guide I’m putting together.
The Main Lesson (from the Guide)
The core is the main message you want to communicate. It is the through-line, the essence of all the thoughts you want to express.
The perspective of the piece, your tone, and the facts or examples you include must revolve around the core. Otherwise, your content becomes overwhelming and confusing.
Finding the core message is often difficult because, once you have read a paper, review, or article, you have so much information floating around in your mind. However, for concise communication, you must identify the central message because that is what will evoke awe, inspiration, or surprise in your reader – complexity kills that effect. This post is a good example because after reading the paper you must ask what’s the core? That there is a new immune cell, how it differs from others, how exactly it works, why it is important, its evolution, etc.? Once you have identified your core message, you can mention the other aspects, but they must all contribute to that central message. We decided to go for the fascination of a weirdly new immune mechanism.
The core applies to the entire piece, but you can also apply the same principle to each paragraph, or even each sentence. Each of these smaller elements should build towards the core message of your piece.
All in all, before you sart writing, ask yourself: What is the point you want to get across?
How to Apply it
Let's go through a concrete example together. Imagine someone wrote the following lines:
Recombinant protein expression, for example in E. coli, is important in a large number of laboratories today.
However, proteins produced in E. coli do not typically contain disulfide bonds. This is a major limitation of the system. Therefore, a number of alternatives, such as insect cells, are used.
One famous example is insulin. E. coli was the first bacterium used to produce insulin in large quantities. Previously, it took 23,000 animals to produce enough insulin for just 750 people.
Because production was limited and prices were unstable, ensuring a reliable supply for patients was challenging.
E. coli helped solve that problem, despite not being able to produce insulin in exactly the same way as it is found in humans.
Our Verdict
That text is informative, but it's not really exciting to read. People will wonder: What are you trying to tell them?
It's not a comprehensive overview of protein expression, yet the informal story isn't particularly exciting either …
Just so you know, the first protein to be expressed recombinantly was somatostatin. This is how the plasmid was constructed. You can read more about it right here.
Either you're writing about protein expression, e.g., for a textbook or a test, or you're doing science communication and want to tell a compelling story.
So what could the core be? I would argue: Fascination - E. coli solved a problem that seems obvious to us today but was causing major headaches just a few decades ago.
Knowing About the Core
Here's how I would write it:
In 1981, it took over 23,000 animals to produce enough insulin for just 750 people.
Indeed, from the 1920s until the early 1980s, insulin came from the pancreases of pigs and cows.
But then scientists found a way to use bacteria to produce it, and everything changed.
In 1978, a collaboration between several scientists led to a paper describing how to produce insulin using recombinant DNA technology.
The host: E. coli. It grows fast, thrives on inexpensive growth media, and is easy to scale up, allowing insulin production for millions of patients worldwide.
Four years later, the FDA approved Eli Lilly's Humulin to treat patients with diabetes. It was the first mass-produced therapeutic protein made using recombinant DNA technology.
The odd part? Insulin needs disulfide bonds, and E. coli isn't exactly known for forming those.
Luckily, scientists found a way to make it work anyway!
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