Denaturation of protein is easy, but can we restore the functional structure of protein again?
Yes you can refold some proteins under special conditions but it’s too hard to unscramble a cooked egg. The reasons for these two conflicting results are that intermolecular aggregation interactions compete with intra-molecular folding interactions. The heat denatured scrambled egg is a tangle of intermolecular aggregation interactions that is too hard to undo. Good conditions noted by Paul Lesbats might for example mean a purified protein kept from aggregation by binding to beads upon a column. For such systems that avoid non-native aggregation, proteins can often be refolded with different levels of success depending upon co-factors, disulfide bonds, the need for partners or heteromeric assembly, and oxidized or deaminated amino acid residues. In general ligands that selectively bind the folded state can help with folding and stability whereas things that favor the denatured state fight the folding process. So we can sometimes bias the interactions for the folded or unfolded state by design.
Yes you can refold some proteins under special conditions but it’s too hard to unscramble a cooked egg. The reasons for these two conflicting results are that intermolecular aggregation interactions compete with intra-molecular folding interactions. The heat denatured scrambled egg is a tangle of intermolecular aggregation interactions that is too hard to undo. Good conditions noted by Paul Lesbats might for example mean a purified protein kept from aggregation by binding to beads upon a column. For such systems that avoid non-native aggregation, proteins can often be refolded with different levels of success depending upon co-factors, disulfide bonds, the need for partners or heteromeric assembly, and oxidized or deaminated amino acid residues. In general ligands that selectively bind the folded state can help with folding and stability whereas things that favor the denatured state fight the folding process. So we can sometimes bias the interactions for the folded or unfolded state by design.
- Badges
- Science topic
- Similar topics
- Chemistry
- General Biochemistry
- Proteomics