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dc.contributor.authorTorres, J.
dc.contributor.authorKukol, A.
dc.contributor.authorGoodman, J. M.
dc.contributor.authorArkin, I.T.
dc.date.accessioned2011-10-18T09:01:07Z
dc.date.available2011-10-18T09:01:07Z
dc.date.issued2001-11
dc.identifier.citationTorres , J , Kukol , A , Goodman , J M & Arkin , I T 2001 , ' Site-specific examination of secondary structure and orientation determination in membrane proteins: The peptidic C-13=O-18 group as a novel infrared probe ' , Biopolymers , vol. 59 , no. 6 , pp. 396-401 . https://doi.org/10.1002/1097-0282(200111)59:6<396::AID-BIP1044>3.0.CO;2-Y
dc.identifier.issn0006-3525
dc.identifier.otherPURE: 420941
dc.identifier.otherPURE UUID: c44f8c40-34ef-4ac3-adf1-57ced5a1c6bd
dc.identifier.otherWOS: 000171916600002
dc.identifier.otherScopus: 0034752541
dc.identifier.urihttp://hdl.handle.net/2299/6687
dc.descriptionFull text of this article is not available in the UHRA
dc.description.abstractDetailed site-specific information can be exceptionally useful in structural studies of macromolecules in general and proteins in particular. Stich information is usually obtained from spectroscopic studies using a label/probe that can reflect on particular properties of the protein. A suitable probe must not modify the native properties of the protein, and should yield interpretable structural information, as is the case with isotopic labels used by Fourier transform infrared (FTIR) spectroscopy. In particular, 1-C-13=O labels have been shown to relay site-specific secondary structure and orientational information, although limited to small peptides. The reason for this limitation is the high natural abundance of C-13 and the lack of baseline resolution between the main amide I band and the isotope-edited peak Herein; we dramatically extend the utility of isotope edited FTIR spectroscopy to proteins of virtually any size through the use of a new 1-C-13=O-18 label. ne double-isotope label virtually eliminates any contribution from natural abundance C-13. More importantly, the isotope-edited peak is further red-shifted (in accordance with ab lnitio Hartree-Fock calculations) and is now completely baseline resolved fi-om the main amide I band Taken together this new label enables determination of site specific secondary structure and orientation in proteins of virtually any size. Even in small peptides 1-C-13=O-18 is far preferable as a label in comparison to 1-O-13=O-16 since it enables analysis without the need for any deconvolution or peak fitting procedures. Finally, the results obtained herein represent the first stage in the application of site-directed dichroism to the structural elucidation of polytopic membrane proteins. (C) 2001 John Wiley & Sons, Inc.en
dc.format.extent6
dc.language.isoeng
dc.relation.ispartofBiopolymers
dc.subjectFourier transform infrared
dc.subjectmembrane protein
dc.subjectprotein structure
dc.subjectTRANSMEMBRANE PEPTIDE
dc.subjectHELIX TILT
dc.subjectDICHROISM
dc.subjectPHOSPHOLAMBAN
dc.subjectSPECTROSCOPY
dc.subjectCHANNEL
dc.subjectDOMAIN
dc.titleSite-specific examination of secondary structure and orientation determination in membrane proteins: The peptidic C-13=O-18 group as a novel infrared probeen
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
rioxxterms.versionofrecordhttps://doi.org/10.1002/1097-0282(200111)59:6<396::AID-BIP1044>3.0.CO;2-Y
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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