Binding of monovalent cations induces large changes in the secondary structure of Na super(+),K super(+)-ATPase as probed by Raman spectroscopy

Raman spectra of active Na super(+),K super(+)-ATPase from pig kidney in media containing Na super(+) (E sub(1)), K super(+) (E sub(2)) or without exogenous ions (E sub(1) conformation) were recorded in order to calculate the changes in the enzyme's secondary structure induced by binding of mon...

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Bibliographic Details
Published in:FEBS letters 1988-01, Vol.236 (1), p.235-239
Main Authors: Nabiev, IR, Dzhandzhugazyan, K N, Efremov, R G, Modyanov, N N
Format: Article
Language:English
Subjects:
adenosinetriphosphatase
kidney
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Summary:Raman spectra of active Na super(+),K super(+)-ATPase from pig kidney in media containing Na super(+) (E sub(1)), K super(+) (E sub(2)) or without exogenous ions (E sub(1) conformation) were recorded in order to calculate the changes in the enzyme's secondary structure induced by binding of monovalent cations. It is demonstrated that: K super(+) binding to the E sub(1) form of the enzyme leads to conversion of similar to 100 peptide groups from the beta -structure to alpha -helical conformation; the transition is reversible and fully reproducible in the E sub(1) arrow right E sub(2) arrow right E sub(1) and E sub(2) arrow right E sub(1) arrow right E sub(2) experimental schemes.
ISSN:0014-5793