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

Brems David N. | Zendy; Havel Henry A. | Zendy

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

Author(s) -

Brems David N.,

Havel Henry A.

Publication year - 1989

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.340050110

Subject(s) - molten globule , chemistry , protein folding , folding (dsp implementation) , crystallography , solvent , biophysics , chemical physics , thermodynamics , biochemistry , biology , electrical engineering , engineering , physics

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.

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