1 Comment

Recently Isis wrote:

’For me, the joy in science comes from realizing that you are looking at data that no one else has seen. I remember standing at the bench with a new student several months ago looking at a piece of data. I leaned over and whispered to him, “I want you to remember this instance, looking at these data. Right now, you and I are the only people in the world who know this thing.” The smile on his face while he pondered that little secret that we shared was amazing. Absolutely, truly one of the reasons I do science.’

(Source: Wikimedia Commons.)

(Source: Wikimedia Commons.)

I think all research scientists would say they experienced a moment something like that.

When you start as an undergraduate, you have a textbook understanding of science. Over time you start learning the cutting edge. Somewhere along the way you realise that you are not learning about knowledge, but creating that knowledge.

You cross the line at some point.

It’s curious, addictive buzz. That for a little while some idea or ‘discovery’ is your own.

Until you publish it you are the only person who knows that little thing and you can – briefly –bask in your own glory.

Or, as often happens, you later realise that it had already been found by someone else, perhaps using another means. On a personal level that’s OK, you still came up with it for yourself.

One moment I had like this as a Ph.D. student was Jade Li dragging me off to excitedly look at her newly calculated x-ray density map of the Bacillus thuringiensis insect toxin.

We sat there in the dark, rotating the image on the screen trying to guess what the structure of the protein might look like from the density map.

(Source: Biochemistry, University of Washington)

(Source: Biochemistry, University of Washington)

Imagine the image above without the protein chain, the stick model of the molecule. The blue ’cages’ represent the electron density in three dimensions. We were trying to guess what would fit within it.( You can view an animated version of the image showed at the University of Washington website.)

Zif268-DNA complex (Source: Wikimedia Commons.)

Zif268-DNA complex (Source: Wikimedia Commons.)

These moments are not always instant.

Over several months of so of my Ph.D. studies I came to recognise that the sequence variation between equivalent zinc fingers C2H2 zinc finger proteins I was studying were indicating the residues of these proteins that bound DNA, and this type of variation could be used to identify the functional residues of other types of proteins.

One of the things that keep research scientists going are those little moments when you know that you, and only you, have this little gem of knowledge. (Well, to you it’s a gem; you’ve worked hard for it.)

Other articles at Code for life:

Loops to tie a knot in proteins?

Rex and The Wrong Trousers – uncanny resemblance?

Mid-week links and a milestone

Consumer brain-computer interface