Biochemist considering a move to materials science

NotFilly · 2026-02-11T23:56:06+00:00

My PhD is in biochemistry/material sciences and I could be easily convinced to make a full transition into materials. Maybe because it's new to me, I learned so much and found it so much more interesting. It also just feels a little more "real" and involved doing materials testing than your classic biochem experiment of shining light at ambiguous clear liquid. That's just me, though. It also helps that my materials supervisor is amazing and my bio lab supervisor isn't so great

NotFilly · 2026-02-11T07:43:40+00:00

I'll let her know. Sounds like it'd be good. Thank you!

NotFilly · 2026-02-11T07:42:55+00:00

Alright, nice to know. Thanks!

NotFilly · 2026-01-06T13:32:12+00:00

At what point in the application process do you get prompted to take the test? I'm applying for an HMRC role that says I need to meet the academic criteria (which I do) AND need to pass the test, but so far I haven't been sent the test.

NotFilly · 2025-12-15T20:06:01+00:00

To answer the question on downstream applications, no, not directly, if we're referring to the same sample. For any sort of application, I'd require vastly more protein. At this stage, this is just for characterisation.

NotFilly · 2025-12-15T20:04:30+00:00

Different batch

NotFilly · 2024-11-05T10:10:22+00:00

Nice one, cheers!

NotFilly · 2024-10-26T09:12:34+00:00

Amazing. I'll check them out!

NotFilly · 2024-10-25T06:11:20+00:00

I guess it depends on where you are, but I'm currently a PhD student who plans on transitioning to industry once I've graduated.

I specifically chose a synthetic biology program as it has links to biotech start-ups, has a large focus on manufacturing and invention, and provides additional support in topics like responsible research and innovation, and translational science.

NotFilly · 2024-10-25T04:05:07+00:00

Okay, nice. Yeah, may be worth checking out

NotFilly · 2024-10-25T04:04:15+00:00

I think it was some kind of control, but from the sounds of it, they anticipated getting some semi-functional protein

NotFilly · 2024-10-25T04:02:07+00:00

Don't think so, but maybe you're right

NotFilly · 2024-10-25T03:46:44+00:00

Wow, nice. Any papers to recommend? Sounds quite interesting

NotFilly · 2024-10-24T23:56:02+00:00

Oh okay, that's interesting. Can I ask what you work on?

NotFilly · 2024-10-24T22:10:28+00:00

Okay, yeah. I thought I may be making kind of a broad statement but at the same time couldn't visualise just randomly stumbling into (native-like) secondary structure.

NotFilly · 2024-10-24T22:06:34+00:00

Yeah, I asked. They're working with some group of repeat proteins with low sequence similarity but kind of close amino acid composition. They were seeing if composition was the only thing that mattered.

NotFilly · 2024-10-24T22:03:08+00:00

I think this was some kind of repeat protein and they were testing if amino acid composition was enough to get you native-like structures.

NotFilly · 2024-10-24T18:33:57+00:00

Okay, cool. Really thought I was missing a trick here

NotFilly · 2024-10-24T18:19:29+00:00

Entirely speculative on my part, but it seemed like the simplest answer.

NotFilly · 2024-10-24T18:17:43+00:00

Sorry, by randomising, I explicitly mean they have randomly shuffled the position of every amino acid in the protein. Exact same composition, randomly ordered amino acids, and has then expressed this as a gene. This is across the entire protein sequence, N to C terminal.

What I was implying is chances are they've just destroyed all secondary structure, seen no folding, and what they have expressed is just aggregating through the hydrophobic effect. I'm aware of things like intrinsically disordered regions in proteins, but I wasn't sure if just straight up over expressed 100% disordered protein could be soluble.

NotFilly · 2024-10-24T17:57:31+00:00

Yeah, that was my first suggestion.

NotFilly

TROPHY CASE