So they both denature protein – but are the result or procedure any different? If so, how exactly?
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The reason they denature protein isn’t quite the same, but the results are the same. Protein is a long series of amino acids, but it folds into a structure held together by hydrogen bonds, which are weak bonds between relatively positively charged hydrogens and relatively negatively charged other atoms. Those bonds hold the protein into a 3D shape instead of just a ribbon.
When the bonds are broken by heat or alcohol, the protein becomes a floppy ribbon. Proteins work entirely by their shape, so losing the shape means they lose their specific nature as a specific protein: they’re denatured.
Yes, different environments will change how the protein changes as it denatures. The other answer is sort of right, in that the protein doesn’t work anymore in any case, but it’s sorta wrong in saying that it always becomes a floppy ribbon.
A floppy ribbon is a relatively “high energy” state compared to a protein that is folded “somehow”. Totally unfolding the entire structure of the protein is a very unlikely state. It’s more likely to be a small(er) change that “breaks” the protein.
Different environments will change what is favorable for the protein to do. Some will make it likely for the protein’s peptide chain to break at a certain point. Some will make the [chiral](https://en.wikipedia.org/wiki/Chirality) amino acids turn into their “other-handed” versions. Some will make it fold itself into useless-form-#-1, some will make it turn into useless-form-#-23109XYZ.
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