T. Handel, Scott A. Williams, D. Menyhárd
Jun 1, 1993
Citations
0
Influential Citations
18
Citations
Journal
Journal of the American Chemical Society
Abstract
To investigate the dynamic properties of α 4 , a designed four-helix bundle protein, a Leu residue sequestered in the hydrophobic core of the bundle was changed to Trp. If the interior of the protein was very loosely packed, this replacement should be accommodated quite readily. On the other hand, if the protein was reasonably well-packed (as in the native state or an intermediate late on the folding pathway), the substitution should perturb the packing and destabilize the protein. In fact, the mutation of Leu to Trp was strongly destabilizing, decreasing the free energy of folding by approximately 3-4 kcal/mol