Direct visualization of disulfide bonds through diselenide proxies using<sup>77</sup>Se NMR spectroscopy

Mobli, M; De Araújo, AD; Lambert, LK; Pierens, GK; Windley, MJ; Nicholson, GM; Alewood, PF; King, GF

Direct visualization of disulfide bonds through diselenide proxies using<sup>77</sup>Se NMR spectroscopy

Mobli, M De Araújo, AD Lambert, LK Pierens, GK Windley, MJ Nicholson, GM

Alewood, PF King, GF

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Publication Type:: Journal Article
Citation:: Angewandte Chemie - International Edition, 2009, 48 (49), pp. 9312 - 9314
Issue Date:: 2009-11-23

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Field	Value	Language
dc.contributor.author	Mobli, M	en_US
dc.contributor.author	De Araújo, AD	en_US
dc.contributor.author	Lambert, LK	en_US
dc.contributor.author	Pierens, GK	en_US
dc.contributor.author	Windley, MJ	en_US
dc.contributor.author	Nicholson, GM https://orcid.org/0000-0002-4277-4296	en_US
dc.contributor.author	Alewood, PF	en_US
dc.contributor.author	King, GF	en_US
dc.date.issued	2009-11-23	en_US
dc.identifier.citation	Angewandte Chemie - International Edition, 2009, 48 (49), pp. 9312 - 9314	en_US
dc.identifier.issn	1433-7851	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8428
dc.description.abstract	Chemical Equation Presentation Se-ing is believing: Many proteins are cross-braced by disulfide bonds that frequently play key roles in protein structure, folding, and function. Unfortunately, the methods available for assignment of disulfide-bond connectivities in proteins are technically difficult and prone to misinterpretation. Now disulfide bond connectivities in native proteins can be visualized directly using 77Se NMR spectroscopy. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.	en_US
dc.relation.ispartof	Angewandte Chemie - International Edition	en_US
dc.relation.isbasedon	10.1002/anie.200905206	en_US
dc.subject.classification	Organic Chemistry	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Disulfides	en_US
dc.subject.mesh	Selenium	en_US
dc.subject.mesh	Isotopes	en_US
dc.subject.mesh	Cysteine	en_US
dc.subject.mesh	Peptides	en_US
dc.subject.mesh	Spider Venoms	en_US
dc.subject.mesh	Nuclear Magnetic Resonance, Biomolecular	en_US
dc.subject.mesh	Molecular Structure	en_US
dc.subject.mesh	Protein Structure, Tertiary	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.title	Direct visualization of disulfide bonds through diselenide proxies using<sup>77</sup>Se NMR spectroscopy	en_US
dc.type	Journal Article
utslib.citation.volume	49	en_US
utslib.citation.volume	48	en_US
utslib.for	030406 Proteins and Peptides	en_US
utslib.for	03 Chemical Sciences	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/Strength - CHT - Health Technologies
utslib.copyright.status	closed_access
pubs.issue	49	en_US
pubs.publication-status	Published	en_US
pubs.volume	48	en_US

Abstract:

Chemical Equation Presentation Se-ing is believing: Many proteins are cross-braced by disulfide bonds that frequently play key roles in protein structure, folding, and function. Unfortunately, the methods available for assignment of disulfide-bond connectivities in proteins are technically difficult and prone to misinterpretation. Now disulfide bond connectivities in native proteins can be visualized directly using 77Se NMR spectroscopy. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/8428