1992 Fiscal Year Final Research Report Summary
Molten-Globule of Proteins and Its Physiological Role
| Project/Area Number |
02454536
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Osaka University |
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Principal Investigator |
GOTO Yuji Osaka Univ., Fac. of Sci., Associate Prof., 理学部, 助教授 (40153770)
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| Co-Investigator(Kenkyū-buntansha) |
TESHIMA Keizo Hiroshima Univ., Fac. of Integrated Arts and Science, Associate Prof., 総合科学部, 助教授 (30155452)
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| Project Period (FY) |
1990 – 1992
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| Keywords | molten globule / structure of proteins / protein denaturation / protein folding / cytochrome c / melittin / protein chemistry / small angle X-ray scattering |
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| Research Abstract |
The molten globule is a compact denatured state with a significant amount of secondary structure, but largely disordered tertiary structure. To understand the role of the molten globule in protein folding and its physiological role, we studied the conformation and stability of the molten globule of various proteins and the corresponding state of peptides. We obtained following major results.
1. The stability of the molten globule is determined by a balance of various forces. We showed that electrostatic repulsion is a critical factor destabilizing the molten globule state.
2. The molten globule of cytochrome c was studied by small angle X-ray scattering and its conformational properties were clarified.
3. We indicated that the reversibly denatured conformation of cytochrome c under physiological conditions (i.e. neutral ph, physiological temperature and no denaturant) is the molten globule.
4. We showed the mechanism of the anion and ph-dependent conformational transition of melittin and an amphiphilic polypeptide.
5. We showed that Guanidine-Hydrochloride induces the refolding of acid-unfolded proteins, stabilizing the molten globule state.
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