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dc.contributor.authorTorres, J.
dc.contributor.authorKukol, A.
dc.contributor.authorArkin, I.T.
dc.date.accessioned2011-10-18T10:01:14Z
dc.date.available2011-10-18T10:01:14Z
dc.date.issued2000-12
dc.identifier.citationTorres , J , Kukol , A & Arkin , I T 2000 , ' Use of a single glycine residue to determine the tilt and orientation of a transmembrane helix : A new structural label for infrared spectroscopy ' , Biophysical Journal , vol. 79 , no. 6 , pp. 3139-3143 . https://doi.org/10.1016/S0006-3495(00)76547-7
dc.identifier.issn0006-3495
dc.identifier.otherPURE: 420825
dc.identifier.otherPURE UUID: a120aed4-571e-4c8f-b984-92cf815dc0ea
dc.identifier.otherWOS: 000165749000031
dc.identifier.otherScopus: 0033636640
dc.identifier.urihttp://hdl.handle.net/2299/6696
dc.description.abstractSite-directed dichroism is an emerging technique for the determination of membrane protein structure. However, due to a number of factors, among which is the high natural abundance of C-13, the use of this technique has been restricted to the study of small peptides. We have overcome these problems through the use of a double C-deuterated glycine as a label. The modification of a single residue (Gly) in the transmembrane segment of M2, a protein from the Influenza A virus that forms H+-selective ion channels, has allowed us to determine its helix tilt and rotational orientation. Double C-deuteration shifts the antisymmetric and symmetric stretching vibrations of the CD2 group in glycine to a transparent region of the infrared spectrum where the dichroic ratio of these bands can be measured. The two dichroisms, along with the helix amide I dichroic ratio, have been used to determine the helix tilt and rotational orientation of M2. The results are entirely consistent with previous site-directed dichroism and solid-state NMR experiments, validating C-deuterated glycine (GlyCD(2)) as a structural probe that can now be used in the study of polytopic membrane proteins.en
dc.format.extent5
dc.language.isoeng
dc.relation.ispartofBiophysical Journal
dc.subjectDICHROISM
dc.subjectPROTEINS
dc.subjectCHANNEL
dc.titleUse of a single glycine residue to determine the tilt and orientation of a transmembrane helix : A new structural label for infrared spectroscopyen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionAgriculture, Veterinary and Food Sciences
dc.contributor.institutionPharmacology and Clinical Science Research
dc.contributor.institutionCardiovascular Pathologies
dc.contributor.institutionBiochemistry and Bioinformatics
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted2000-12
rioxxterms.versionofrecordhttps://doi.org/10.1016/S0006-3495(00)76547-7
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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