Fourier-Transform infrared spectroscopic investigation of the secondary structure of P <inf>2</inf> protein in deuterium oxide solution

Stuart, BH; McFarlane, EF

Fourier-Transform infrared spectroscopic investigation of the secondary structure of P <inf>2</inf> protein in deuterium oxide solution

Stuart, BH

McFarlane, EF

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Publication Type:: Journal Article
Citation:: Australian Journal of Chemistry, 1991, 44 (11), pp. 1523 - 1531
Issue Date:: 1991-01-01

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Field	Value	Language
dc.contributor.author	Stuart, BH https://orcid.org/0000-0001-9540-4435	en_US
dc.contributor.author	McFarlane, EF	en_US
dc.date.issued	1991-01-01	en_US
dc.identifier.citation	Australian Journal of Chemistry, 1991, 44 (11), pp. 1523 - 1531	en_US
dc.identifier.issn	0004-9425	en_US
dc.identifier.uri	http://hdl.handle.net/10453/26071
dc.description.abstract	Fourier transform infrared (F.t.i.r.) spectroscopy has been used to investigate the secondary structure of bovine P2 protein in deuterium oxide (D2O) solution. The amide 1 region of the spectrum was analysed quantitatively by means of resolution enhancement and band-fitting procedures. The protein was found to consist mainly of β-structure (61%), with a small amount of α-helix (11%). A reason for the existence of an unusually intense low-frequency band assigned to β-structure is discussed. The F.t.i.r. results are compared with those from an X-ray crystallographic study and from circular dichroism and explanations are offered for discrepancies between the results from the different methods. © 1991 ASEG.	en_US
dc.relation.ispartof	Australian Journal of Chemistry	en_US
dc.relation.isbasedon	10.1071/CH9911523	en_US
dc.subject.classification	General Chemistry	en_US
dc.title	Fourier-Transform infrared spectroscopic investigation of the secondary structure of P <inf>2</inf> protein in deuterium oxide solution	en_US
dc.type	Journal Article
utslib.citation.volume	11	en_US
utslib.citation.volume	44	en_US
utslib.for	0399 Other Chemical Sciences	en_US
utslib.for	0303 Macromolecular and Materials Chemistry	en_US
utslib.for	0301 Analytical Chemistry	en_US
utslib.for	03 Chemical Sciences	en_US
dc.location.activity	ISI:A1991GP57500002	en_US
dc.location.activity	WOS:000184376400021
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	11	en_US
pubs.publication-status	Published	en_US
pubs.volume	44	en_US

Abstract:

Fourier transform infrared (F.t.i.r.) spectroscopy has been used to investigate the secondary structure of bovine P2 protein in deuterium oxide (D2O) solution. The amide 1 region of the spectrum was analysed quantitatively by means of resolution enhancement and band-fitting procedures. The protein was found to consist mainly of β-structure (61%), with a small amount of α-helix (11%). A reason for the existence of an unusually intense low-frequency band assigned to β-structure is discussed. The F.t.i.r. results are compared with those from an X-ray crystallographic study and from circular dichroism and explanations are offered for discrepancies between the results from the different methods. © 1991 ASEG.

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