ABSTRACT
The folding-unfolding of a 16 residue polypeptide, a ß-hairpin in B1 domain of protein G is investigated here to account for the factors assisting the extra stability of the polypeptide in the presence of an explicit solvent and even when a denaturant like urea is present in the medium. It is observed here that the backbone H-bond network well defines the folded state and is even capable of forming the folded state, but it is not the only criteria for making a stable ß-hairpin fold. Factors such as the side chain H-bonds and the alignment of the certain hydrophobic group side chains play a prominent role in preserving the ß-hairpin structure and thus providing an extra stability to the hairpin architecture. It is also affirmed that the mentioned hydrophobic groups side chain interactions are very crucial in holding the ß-hairpin together and without which the hairpin collapses completely. We also confirm that the denaturant urea acts on the GB1-hairpin backbone H-bonds and in the presence of strong hydrophobic interactions with a consistent side chain H-bonding network, the denaturation being comparatively a slower process with respect to the protein devoid of the side chain interactions.Communicated by Ramaswamy H. Sarma.
