Application of Heating and Cooling Strategy on Trp-cage Folding
Post date: Jan 31, 2020 6:42:37 PM
In our body, the proteins that are synthesized fold to their native structure at physiological temperature. Heating a protein breaks interaction between the amino acid residues and extreme temperature causes a protein to unfold and be denatured. What if during protein folding the system is heated? How will it affect the folding process? Will this strategy provide better conformational search during folding that will eventually lead to the native structure of the protein?
Figure 2. Line representation (top) and cartoon representation (bottom) extended structure of the peptide Trp-cage from the sequence of PDB ID 1RIJ.