Preparations derived from willow have been a regular feature of the human medicine cabinet for centuries: Ancient Egyptians drank willow ‘tea’ to relieve pain, and the Classic Greek physician Hippocrates wrote about the remedy in 400 BC. But it took a team of German chemists in 1897, working for Bayer, to synthesise a pure compound related to the active substances in willow, acetylsalicylic acid. They packaged it up neatly in pill form, and sold it under its trademarked name, Aspirin, which quickly became a household word.
Small molecules can be great for sending biochemical signals between cells, or between different parts of a cell, because they can diffuse rapidly in water – notably, the water in your body. Big, multicellular organisms rely on hundreds of such molecules to get on with the business of living.
If there is one molecule that could be called the ‘currency’ of life, it is ATP: adenosine triphosphate. It belongs to a large class of molecules of life, which are all high in energy and have constituent parts that would – given enough time – much prefer to separate.
Water is such an everyday substance – you use water to wash, drink, make food; it is commonplace in our weather and rivers, and surrounds us in oceans. Its ubiquity is not only important for our environment: it is absolutely critical for life.
This is an idle muse on information and biology as I wait for my SFO to Burbank plane (also an experiment in “fast blogging”).
Biology is truly an information science – what are biological systems? They are way more than the atoms that make them up; they are far more than just the molecules that make them up; ultimately they are remarkable systems which can harness the inevitable flow of energy towards heat to their own persistence and, in many animal’s case, information capture and decision making.
Reflections on reproducibility, digital communication and open science
Is science sound? There has been a sustained discussion about this over the past five years – ever-present in the background, and punctuated by intense public debates, both in the scientific press and more broadly. There is a host of concerns – from reproducibility of science to incentive structures – all focused ultimately on how we know what is true and what is not. The answer is not always straightforward.
My final Structure of Christmas may look like an unremarkable enzyme, but it heralded the arrival of a game-changing method in structural biology.
My ninth (and final) Structure of Christmas is beta-galactosidase: a pretty run-of-the-mill enzyme that turns compound sugars into monosaccharides. When you put a special dye on it, it turns the dye blue (whee!). It’s a mainstay of molecular biology and millions of students have used it in countless experiments, both fascinating and mundane. It doesn’t have much of a ‘wow’ factor – it’s a solid member of a respectable family of sugar-cleaving enzymes.
What is so special about it is the way its structure was determined.
My penultimate structure of Christmas is actually two molecular partners, which work together to make muscle move.
Most of my Christmas structures have been separable units – some large, some small – that float around in cells or cell membranes. But to move physically, organisms need to have more at their disposal than some things floating in solution. For most life forms, movement is managed by proteins working together. A perfect example of this is the beautiful partnership between actin and tropomyosin.
Once a parasite makes it past our outer defences, it encounters some seriously sophisticated weaponry. One of these is the ever-shifting antibody, my seventh structure of Christmas.
Every large organism – you included – is just a feast laid out for any parasite (bacteria, virus or beastie) clever enough to break in and access its carefully amassed energy. Throughout the Billion-Years’ Evolutionary War between hosts and parasites, the host has always been on the defensive, endlessly innovating to fend off invaders.
My sixth structure of Christmas is out to kill human gut cells, with help from a human protein. But has it simply shown up (drunk) at the wrong party?
Interactions between two living organisms nearly always involve proteins. All proteins fold into precise, beautiful shapes, tweaked and perfected by evolution over millions of years to perform very specific tasks. In a successful interaction, two of these shapes will fit together perfectly – like a plug and socket – to make things happen.