✦ LIBER ✦
Folding of bovine growth hormone is consistent with the molten globule hypothesis
✍ Scribed by Dr. David N. Brems; Dr. Henry A. Havel
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 250 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
✦ Synopsis
Previous results from equilibrium and kinetic studies of the folding of bovine growth hormone (bGH) have demonstrated that bGH does not follow a simple two-step folding mechanism. These results are summarized and interpreted according to the "molten globule" model. The molten globule state of bGH is characterized as a folding intermediate which is largely alpha-helical, retains a compact hydrodynamic radius, has packing of the aromatic side chains that is similar to the unfolded state, and possesses a solvent-exposed hydrophobic surface along helix 106-127 that readily leads to association.