Pressure-induced changes in the secondary structure of the Escherichia coli methionine repressor protein

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DOIResolve DOI: http://doi.org/10.1016/0167-4838(89)90257-4
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TypeArticle
Journal titleBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
ISSN0167-4838
Volume996
Issue3
Pages260262
SubjectHigh pressure; Methionine repressor; (E. coli)
AbstractThe 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.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001186
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Record identifier8fe3e45c-bd2e-478f-948a-ce703458c1d5
Record created2017-01-03
Record modified2017-01-03
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