Note that because of processes such as the post-translational modifications to proteins we still need protein sequencing and I believe that we currently rely too heavily on DNA sequencing. This is because it is now much easier to sequence DNA. Instead, since it has been worked out (mostly) how DNA codes for protein, we usually infer the protein sequence from the DNA sequence.
Several chaperones also function to reactivate aggregated proteins. However, it is now relatively rare to directly determine protein sequence! In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. Molecular chaperones, including Hsp60s, Hsp70s, Hsp90s and sHsps, assist in the folding of unfolded and misfolded polypeptides by stabilization of folding intermediates and prevention of protein misfolding and aggregation. The very first protein sequence (bovine insulin) was determined by Fredrick Sanger in 1951-2 (note that this was more than a decade before the first nucleotide sequence). Most proteins require molecular chaperones to achieve a biologically functional conformation. There are many different techniques for directly determining protein sequences - this wikipedia article is a decent introduction:
There are also methods that have been developed to remove amino acids one at a time.īy combining theses techniques it is possible to directly determine protein sequences. This is a great question, but actually quite complicated so I'm not going to try to give a complete answer - I have given some useful links below if you wish to learn more.Įach amino acid has unique chemical properties that can be used to tell them apart.
0 kommentar(er)
