A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin

Stuart, BH

A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin

Stuart, BH

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Publication Type:: Journal Article
Citation:: Biochemistry and Molecular Biology International, 1996, 38 (4), pp. 839 - 845
Issue Date:: 1996-08-20

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Field	Value	Language
dc.contributor.author	Stuart, BH https://orcid.org/0000-0001-9540-4435	en_US
dc.date.issued	1996-08-20	en_US
dc.identifier.citation	Biochemistry and Molecular Biology International, 1996, 38 (4), pp. 839 - 845	en_US
dc.identifier.issn	1039-9712	en_US
dc.identifier.uri	http://hdl.handle.net/10453/18160
dc.description.abstract	The secondary structure of myelin basic protein (MBP) in reconstituted central nervous system myelin was studied using Fourier transform infrared (FTIR) spectroscopy. The spectra of the protein in aqueous solution and in the lipid environment were compared and notable differences were observed. It is proposed that there are significant differences in the conformation of the protein in the contrasting environments. Significant increases in both α-helical structure and β-structure were observed on reconstitution in myelin. The findings of this study also support the view that the presence of both α-helices and β-structure plays a important role in membrane proteins.	en_US
dc.relation.ispartof	Biochemistry and Molecular Biology International	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Central Nervous System	en_US
dc.subject.mesh	Myelin Sheath	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Cattle	en_US
dc.subject.mesh	Myelin Basic Proteins	en_US
dc.subject.mesh	Spectroscopy, Fourier Transform Infrared	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Protein Structure, Secondary	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Myelin Basic Protein	en_US
dc.title	A Fourier transform infrared spectroscopic study of the secondary structure of myelin basic protein in reconstituted myelin	en_US
dc.type	Journal Article
utslib.citation.volume	4	en_US
utslib.citation.volume	38	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0604 Genetics	en_US
utslib.for	1101 Medical Biochemistry and Metabolomics	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CFS - Centre for Forensic Science
utslib.copyright.status	closed_access
pubs.issue	4	en_US
pubs.publication-status	Published	en_US
pubs.volume	38	en_US

Abstract:

The secondary structure of myelin basic protein (MBP) in reconstituted central nervous system myelin was studied using Fourier transform infrared (FTIR) spectroscopy. The spectra of the protein in aqueous solution and in the lipid environment were compared and notable differences were observed. It is proposed that there are significant differences in the conformation of the protein in the contrasting environments. Significant increases in both α-helical structure and β-structure were observed on reconstitution in myelin. The findings of this study also support the view that the presence of both α-helices and β-structure plays a important role in membrane proteins.

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http://hdl.handle.net/10453/18160