| DOI | Resolve DOI: https://doi.org/10.1016/0167-4838(89)90257-4 |
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| Author | Search for: Wong, P. T. T.1; Search for: Girons, I. Saint; Search for: Guillou, Y.; Search for: Cohen, G. N.; Search for: Bârzu, O.; Search for: Mantsch, H. H.1 |
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| Affiliation | - National Research Council of Canada
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| Format | Text, Article |
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| Subject | High pressure; Methionine repressor; (E. coli) |
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| Abstract | The effect of hydrostatic pressure on the conformational properties of the E. coli methionine repressor protein in aqueous solution was investigated by infrared spectroscopy. Changes in hydrostatic pressure produce dramatic changes in the spectral region of the conformation-sensitive amide I band. As the pressure is raised up to 18 kbar, the protein undergoes a rearrangement of α-helical segments into β-type structures; after the pressure is released the β-strands reconvert into less ordered α-helical or random segments. |
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| Publication date | 1989-07-06 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 23001186 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 8fe3e45c-bd2e-478f-948a-ce703458c1d5 |
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| Record created | 2017-01-03 |
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| Record modified | 2020-03-17 |
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