1995 Fiscal Year Final Research Report Summary
STUDIES ON NON-NATIVE STRUCTURES OF PROTEINS
| Project/Area Number |
05404082
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | DEPARTMENT OF CHEMISTRY,FACULTY OF SCIENCE,KOBE UNIVERSITY |
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Principal Investigator |
AKASAKA Kazuyuki DEPARTMENT OF CHEMISTRY,FACULTY OF SCIENCE,PROFESSOR, 理学部, 教授 (50025368)
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| Co-Investigator(Kenkyū-buntansha) |
TAMURA Atuo THE GRADUATE SCHOOL OF SCIENCE AND TECHNOLOGY, 自然科学研究科, 講師 (90273797)
KONNO Takashi THE GRADUATE SCHOOL OF SCIENCE AND TECHNOLOGY,ASSISTANT, 自然科学研究科, 助手 (50225637)
TACHIBANA Hideki DEPARTMENT OF CHEMISTRY,FACULTY OF SCIENCE,ASSISTANT PROFESSOR, 理学部, 助教授 (70126118)
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| Project Period (FY) |
1993 – 1995
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| Keywords | x ray scattering / circular dichroism / NMR / cold denaturation / pressure denaturation / temperature jump / high pressure NMR / denaturation by methanol |
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| Research Abstract |
1.Structure of denatured proteins using small angle x ray scattering, circular dichroism, and NMR spectroscopy.
The combination of the three techniques revealed the characteristic structure of the cold denatured state of Streptomyces subtilisin inhibitor (SSI), methanol-induced denatured states of cytochrome c, myoglobin, and lysozyme. In the latter, the compact denatured states (molten globule) and the expanded helical states were both observed, depending on the methanol concentration and pH.
2.Structure and thermodynamic stability of proteins at high pressure.
A versatile high pressure NMR technique was developed for use with a high field NMR spectrometer. This allowed measurement of "deformation" of the native structure and denaturation by pressure.
3.Protein unfolding by temperature-jump NMR.
The process of unfolding of ribonuclease A was studied with the microwave-pulsed temperature-jump NMR spectroscopy developed in our laboratory. The method allowed us to detect an intermediate species within a few hundred milliseconds upon unfolding of the protein.
4.The role of disulfide bridges on the folding process.
An genetically engineered lysozymes in which one, two, three or all of the four disulfide bridges were removed were investigated for their folding. The results clarified the roles of different disulfide bridges in the folding process.
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Research Products
(13 results)
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[Publications] Kamatari, Y., Konno, T., Kataoka, M., and Akasaka, K: "The Methanol-Induced Globular and Expanded Denatured States of Cytochrome c : A study by CD,Fluorescence, NMR,and Small Angle X-ray Scattering." J.Mol.Biol.259 (3). (1996)
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「研究成果報告書概要(欧文)」より
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[Publications] Tamura, A., Matsushita, M., Naito, A., Kojima, S., Miura, K-I., and Akasaka, K: "Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in solid." Protein Science. 5 (1). 127-139 (1996)
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[Publications] Konno, T., Kataoka, M., Kamatari, Y., Kanaori, K., Nosaka, A., and Akasaka, K.: "Solution X-ray Scattering of Cold-, Heat-, and Urea-Denatured States in a Protein, Streptomyces Subtilisin Inhibitor." J.Mol.Biol.250 (1). 95-103 (1995)
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「研究成果報告書概要(欧文)」より
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