2D SOLID STATE NMR SPECTRAL SIMULATION OF 3(10), ALPHA, AND PI-HELICES
SCIE
SCOPUS
- Title
- 2D SOLID STATE NMR SPECTRAL SIMULATION OF 3(10), ALPHA, AND PI-HELICES
- Authors
- Kim, S; Cross, TA
- Date Issued
- 2004-06
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Abstract
- Transmembrane helices are more uniform in structure than similar helices in water soluble proteins. Solid state NMR of aligned bilayer samples is being increasingly used to characterize helical membrane protein structures. Traditional spectroscopic methods have difficulty distinguishing between helices with i to i + 3 (3(10)), i to i + 4 (alpha), and i to i + 5 (pi) hydrogen bonding topology. Here, we show that resonance patterns in PISEMA spectra simulated for these different helices show unique and striking features. The size and shape of these Polar Index Slant Angle (PISA) wheels, its well as the resonances per turn and clockwise versus counter-clockwise sequential connectivity of the resonances demonstrate how these different helical structures, if present as a uniform structure, will be readily distinguished, and characterized. (C) 2004 Elsevier Inc. All rights reserved.
- Keywords
- PISEMA; PISA wheels; 3(10) helices; alpha-helices pi-helices; C-13 CHEMICAL-SHIFT; PEPTIDE 3(10)-HELIX; H+ CHANNEL; PROTEINS; RESOLUTION; CONFORMATION; SPECTROSCOPY; MEMBRANE; POLYPEPTIDE; TOPOLOGY
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/28842
- DOI
- 10.1016/J.JMR.2004.0
- ISSN
- 1090-7807
- Article Type
- Article
- Citation
- JOURNAL OF MAGNETIC RESONANCE, vol. 168, no. 2, page. 187 - 193, 2004-06
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