Anfinsen won me 1973 Chemistry Nobel prize for proposing that the correctly fold
ID: 15198 • Letter: A
Question
Anfinsen won me 1973 Chemistry Nobel prize for proposing that the correctly folded state of proteins is thermodynamically favored. This means that under physiological conditions the correctly folded state of a protein is the preferred conformation of the protein and this is in turn dictated sole by the amino acid sequence. However, it is also well known that under a variety of conditions proteins fail to fold properly, forming aggregates instead. Why does this happen? When protein aggregates form in bacteria what can be done to obtain the correctly folded (and functional) form of the protein? [8 points total]Explanation / Answer
Protein folding is highly specific and depends entirely on the physiological conditions because the folding (which happens with forming of H-bonds over different amino acid units) depends on the pI of the amino acid units.If appropriate conditions are not available, the bonding will be haphazard and we get protein aggregates. To obtain correctly folded form of the aggragates, we have to first denature it and then provide appropriate conditions required for the folding. NOTE: Please mark my answer Lifesaver