Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy

DOI	Resolve DOI: https://doi.org/10.1021/bi00429a002
Author	Search for: Holloway, Peter W.¹; Search for: Mantsch, Henry H.¹
Name affiliation	National Research Council of Canada
Format	Text, Article
Journal title	Biochemistry
ISSN	0006-2960 1520-4995
Volume	28
Issue	3
Pages	931–935
Abstract	Fourier-transform infrared spectroscopy was used to examine the secondary structure of rabbit liver cytochrome b₅ and the polar and nonpolar domains of the protein. The data for both the ploar and nonpolar domains agree well with those previously obtained by other physical techniques. In particular it was found that the nonpolar membrane-binding domain was predominantly α helix and the polar domain was also highly helical, but not all α helix. The independence of the two domains in the whole molecule was, in general, confirmed by the additivity of the spectra of the two domains. The small differences that were seen inidicate the there is a loss of α helix when the protein is cut it into the two domains. In addition, there appears to be slight difference in the exposure to solvent of the amide NH groups in the α-helical portion of the nonpolar domain when it was examined in isolation.
Publication date	1989-02
Language	English
Peer reviewed	Yes
NRC number	NRCC 29208
NPARC number	23001645
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Record identifier	9ead928e-75f9-4df1-88bd-57c6ba512336
Record created	2017-03-14
Record modified	2020-03-17