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A circular dichrois...
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Persson, Bengt L.Department of Biochemistry and Biotechnology, Royal Institute of Technology
(author)
A circular dichroism study of mitochondrial transhydrogenase from beef heart
- Article/chapterEnglish1991
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LIBRIS-ID:oai:DiVA.org:lnu-1174
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https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-1174URI
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https://doi.org/10.1016/0301-4622(91)80004-BDOI
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Language:English
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Summary in:English
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Subject category:art swepub-publicationtype
Notes
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This paper describes a circular dichroism (CD) spectroscopy study of purified proton-pumping nicotinamide nucleotide transhydrogenase from beef heart. The CD spectrum obtained was used to estimate the content of secondary structures of the purified enzyme and suggests the presence of 40–45% α-helical structure and long, possibly membrane-spanning α-helices. The spectrum was essentially unaffected by the absence or presence of transhydrogenase substrates, suggesting that the catalytic and proton-translocating activities of the enzyme occur without major rearrangements at the level of secondary structures.
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Rydström, J
(author)
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Kubista, M
(author)
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Department of Biochemistry and Biotechnology, Royal Institute of Technology
(creator_code:org_t)
Related titles
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In:Biophysical Chemistry39:3, s. 267-2720301-46221873-4200
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