This depends a bit on what you mean with “held-together” the covalent bonds are what holds the string together but the 3D structure needs the hydrogen bonds. If you exert force on the protein the hydrogen bonds will break first and the 3D structure breaks.
The magic of protein folding is that you have a machine that can create a 2D string of amino acids gives you a 3D protein with a stable shape and reliably the same shape. For that to happen you likely inherently require that the 2D string is hold together is a way that’s strong while it wiggles around and finds the desired 3D shape. If there would be a lot of ways to create stronger bonds it would likely misfold a lot easier. And when biology does need stronger bonds Cysteine with it’s sulfide bond is available. If
Proteins are a good solution given the design constraints under which they operate, so putting them in the same category of the human retina is wrong, but I don’t think your post does a good explanation as to why.
* I studied bioinformatics but it has been a while since I have been in my molecular biology lectures.
The magic of protein folding is that you have a machine that can create a 2D string of amino acids gives you a 3D protein with a stable shape and reliably the same shape. For that to happen you likely inherently require that the 2D string
No, strings are 1D, not 2D. Sheets are 2D.
And, of course, we can see that the ammino acid molecules that the “strings” are made of were 3D to begin with (not 2D), meaning that the strings are 3D too if you look closely enough. We can only call strings (nearly) 1D because the other two dimensions are small enough to be negligible for some purposes.
This depends a bit on what you mean with “held-together” the covalent bonds are what holds the string together but the 3D structure needs the hydrogen bonds. If you exert force on the protein the hydrogen bonds will break first and the 3D structure breaks.
The magic of protein folding is that you have a machine that can create a 2D string of amino acids gives you a 3D protein with a stable shape and reliably the same shape. For that to happen you likely inherently require that the 2D string is hold together is a way that’s strong while it wiggles around and finds the desired 3D shape. If there would be a lot of ways to create stronger bonds it would likely misfold a lot easier. And when biology does need stronger bonds Cysteine with it’s sulfide bond is available. If
Proteins are a good solution given the design constraints under which they operate, so putting them in the same category of the human retina is wrong, but I don’t think your post does a good explanation as to why.
* I studied bioinformatics but it has been a while since I have been in my molecular biology lectures.
No, strings are 1D, not 2D. Sheets are 2D.
And, of course, we can see that the ammino acid molecules that the “strings” are made of were 3D to begin with (not 2D), meaning that the strings are 3D too if you look closely enough. We can only call strings (nearly) 1D because the other two dimensions are small enough to be negligible for some purposes.
Yes, you are right.
The important aspect is that the ribosome can add one amino acid at a time to the string and once it’s finished the string can fold into the 3D shape.