Folding of bovine growth hormone is consistent with the molten globule hypothesis.

作者: David N. Brems , Henry A. Havel

DOI: 10.1002/PROT.340050110

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摘要: Previous results from equilibrium and kinetic studies of the folding bovine growth hormone (bGH) have demonstrated that bGH does not follow a simple two-step mechanism. These are summarized interpreted according to "molten globule" model. The molten globule state is characterized as intermediate which largely alpha-helical, retains compact hydrodynamic radius, has packing aromatic side chains similar unfolded state, possesses solvent-exposed hydrophobic surface along helix 106-127 readily leads association.

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