In the cell, the environment is crowded and chaotic. Proteins—long chains of amino acids that need to fold into precise 3D shapes to function—are constantly at risk of tangling up, misfolding, or denaturing when the temperature rises.

Enter the Heat Shock Proteins (specifically the Hsp70 family). These are molecular chaperones. Their job is to bind to unfolded proteins, shield them from the chaos, and give them a chance to fold correctly. They prevent aggregation. They maintain function under stress.

The Metaphor

I chose the name Heat Shock Pineapple because my professional interests—wet lab biochemistry, computational pipelines, and photography—tend to drift toward entropy if they aren’t carefully managed.

  • Experiments generate messy data that needs cleaning.
  • Code rots if it isn’t documented and maintained.
  • Photography captures fleeting light that disappears if you aren’t ready.

This website is the chaperone. It is the structure that prevents these distinct disciplines from aggregating into a mess. It creates a space where the logic of an assay, the syntax of a script, and the composition of a photograph can sit side-by-side without interference.

The Pineapple?

That part is just for flavor. Science takes itself seriously enough; the portfolio doesn’t have to be sterile.

What to Expect

I am using this space to document the edge cases of my work:

  1. Assay Development: How to build robust tests for noisy biology.
  2. Data Hygiene: Python and R workflows that survive the test of time.
  3. Visuals: Frames from my Canon M system, treated with the same attention to detail as my data.

Welcome to the fold.