Folding of bovine growth hormone is consistent with the molten globule hypothesis
- 1 January 1989
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 5 (1) , 93-95
- https://doi.org/10.1002/prot.340050110
Abstract
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 largely a-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 106127 that readily leads association.Keywords
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