We have a lot of type 1 diabetes and genetic propensity for coronary artery disease plus some unique inheritable diseases. The small gene pool combined with easily traceable diseases and really extensive church records of births going back many centuries means Finland is a gold mine for people who research human genetics.

I seem to have fortunately dodged both of the diabetes and CAD bullets.

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It's kind of like "entropy is always trying to destroy structures, these are just the ones that continue to work" or whatever? Like, "nature is in fact constantly trying other ways of continuing these structures--they just get destroyed faster than they can be built" or whatever?

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Does this account for the sponge absorbing the water?

There are two reasons. The soft tap. Loosening particles (sugar, salt etc) that form a rough surface.

Second one is the slap. Inertia makes the contents move the lid relative to the jar breaking the seal. No more vacuum, less friction, easy access.

How has that affected the normal day to day of life, if at all?

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there needs to be a lot more context to give you a good answer.

how much material do your have? do you mind if we destroy it as part of the measurement? how accurate (significant figures) do you want the result to be? what is the material made out of? how much money do you have to spend on this?

cheap simple solutions will work for some levels, but eg crushing may be to be done under vacuum to avoid trapped gas during the crush. you may even need to heat the sample to outgas it better before crushing. assuming that it can survive heating and vacuum conditions.

you could use a sectioning method with image analysis like microtomy to get a good answer, if your sample is soft enough, and you know the density of the two phases (sponge/pore). or you can go high tech, and use ct scanning to get the same answer, provided that your sample is xray transparent enough, and fits in the scanner.

i doubt you would want to try a crush method if the sample is a pu based foam!

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The amino acids interact with each other. The individual interactions are often very simple and involve such things as hydrogen bonding, acid/base salt bridges, hydrophobic exclusion, Van der Waals, sometimes covalent bonds such as disulfides.

While the interactions are simple, the sum of these interactions is very complex and significant. By changing the order that the amino acids are connected (and some other factors that are a bit more complex), the shape of the protein can be controlled.

The end result is a very large and bulky molecule with a very specific shape and that can interact with other molecules in very specific ways.

It's kinda like Legos. The individual bricks connect to each other in very simple ways, but a skilled builder with a plan can build a large creation with a very specific shape and function.

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Your question's very weird honestly. It's completely unfocused and therefore really hard to answer satisfactory.

First, There are very many different proteins with different functions. They look nothing alike. So yes, some are stretchy or bendable, some are easy to manufacture. Others, not so much.

You learned DNA/RNA, those are like a prescription/recipe on how to form a protein. They're "just a strain of repeated units than can be read by ribosomes" (for simplicity's sake we stick to the highschool explanation here).

The ribosomes "read" the recipe and built the protein strand, which starts out as a long chain of amino acids. Each amino acid has its own unique characteristics like pH or sulpher atoms. When connected into a strand, those characteristics influence nearby amino acids to bend away or towards them. Polarity and Hydrogen and sulpher bridges shape the strand into a 3D structure. This is the "why": interactions make it that way. That kinda answers your question as well.

The last answer is "because it works". Proteins which are useless and cost energy to make or have a cool function but cannot be broken down afterwards affect the cell negatively. Efficient cells on average do better than inefficient ones, so good traits survive in the long run (yes, again, I simplify). Structures that work well are conserved throughout evolution, hence why we can make whole trees based on similarity. Which is also a reason why they're structural (and even more so than based on sequence similarity alone)

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Been trying phrase an answer to this for a few minutes and keep coming up with something that sounds like it's been written while half dunk on Christmas Day. which it has so with that disclaimer. structural proteins are ones where their function is related to 'structural roles'. things like actin or tubulin which form parts of the cells cytoskeleton, or collagen or fibronectin in the extra cellular matrix. the shapes off these monomers madness them suitable for building complex 3d structures. this is different from things like enzymes where their shape is critical too their ability to catalyse reactions. there are other biochemicals that can have structural roles such as large sugars things like hyaluronic acid but most structural elements are proteins, probably because of the diversity of different possible structures and the fact that cells already have systems for making, processing and transporting them.

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Effects you describe are not used for propulsion because they are short-range and you can't really for example push away from Earth using magnets. The only practical space-application are https://en.wikipedia.org/wiki/Magnetorquer - electromagnets which can be used to stabilize the spacecraft along magnetic lines.

You can use magnetic forces for some plasma propulsion engines like https://en.wikipedia.org/wiki/Magnetoplasmadynamic_thruster

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