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how could it be that the form that the protein is folded to, does not have anything to do with the amino-acid sequence that constitute this protein? The quote by the researcher says that the form is unrelated to the direction of synthesis (N->C rather than C->N). It implies that all that matters is the amino-acid sequence that constitutes the protein, and ...


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The quote is getting at protein structure is generally thermodynamically driven and not kinetically driven. The structures would be different if you took a mirror image of the sequence that you showed as the amino acid at the n and c terminus are different as is the orientation of all the other amino acids. However, if the ribosome were to be able to ...


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In addition to what is already said, I want to mention something more subtle. What other people have commented here is about an old 'dogma' due to Christian Anfinsen, which postulates that all that matters is the sequence of aminoacids + the microenvironment (pH, temperature, etc). However, I think you might be confounding two other layers of biochemical ...


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I suspect the author meant something a little different. It's not just that it doesn't matter if a protein is synthesized from N- or C-terminus it's also not important for the end result of folding that the synthesis is gradual at all. When designing proteins de novo they model the folding on a computer. The gradual addition of amino acid residues to the ...


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There are three broad questions here, together covering much of the field of structural bioinformatics. I will answer each briefly but point you to a textbook for more. Why is predicting protein structure useful? This is actually a very good question. The standard answer here is "drug discovery", but as things stand anything other than a high quality ...


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