| Literature DB >> 22966895 |
Andy Zhou1, Shadi Abu-Baker, Indra D Sahu, Lishan Liu, Robert M McCarrick, Carole Dabney-Smith, Gary A Lorigan.
Abstract
A new method has been developed to determine α-helical and β-sheet secondary structural components of aqueous and membrane-bound proteins using pulsed electron paramagnetic resonance (EPR) spectroscopy. The three-pulse electron spin echo envelope modulation (ESEEM) technique was used to detect weakly coupled (2)H-labeled nuclei on side chains in the proximity of a strategically placed nitroxide spin-label up to 8 Å away. Changes in the ESEEM spectra for different samples correlate directly to periodic structural differences between α-helical and β-sheet motifs. These distinct trends were demonstrated with α-helical (M2δ subunit of the acetylcholine receptor) and β-sheet (ubiquitin) peptides in biologically relevant sample environments.Entities:
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Year: 2012 PMID: 22966895 PMCID: PMC3535504 DOI: 10.1021/bi3010736
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162