High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine

Title:
High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine
Authors:
Barnes, Alexander B.; Andreas, Loren B.; Huber, Matthias; Ramachandran, Ramesh; van der Wel, Patrick C. A.; Veshtort, Mikhail; Griffin, Robert G.; Mehta, Manish A.
Abstract:
We present a de novo high-resolution structure of the peptide Alanyl-Prolyl-Glycine using a combination of sensitive solid-state NMR techniques that each yield precise structural constraints. High-quality 13C–13C distance constraints are extracted by fitting rotational resonance width (R2W) experiments using Multimode Multipole Floquet Theory and experimental chemical shift anisotropy (CSA) orientations. In this strategy, a structure is first calculated using DANTE-REDOR and torsion angle measurements and the resulting relative CSA orientations are used as an input parameter in the 13C–13C distance calculations. Finally, a refined structure is calculated using all the constraints. We investigate the effect of different structural constraints on structure quality, as determined by comparison to the crystal structure and also self-consistency of the calculated structures. Inclusion of all or subsets of these constraints into CNS calculations resulted in high-quality structures (0.02 Å backbone RMSD using all 11 constraints).
Citation:
Barnes, Alexander B., Loren B. Andreas, Matthias Huber, Ramesh Ramachandran, et al. 2009. "High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine." Journal Of Magnetic Resonance 200(1): 95-100.
Publisher:
Elsevier
DATE ISSUED:
2009
Department:
Chemistry
Type:
article
PUBLISHED VERSION:
10.1016/j.jmr.2009.06.009
PERMANENT LINK:
http://hdl.handle.net/11282/309409

Full metadata record

DC FieldValue Language
dc.contributor.authorBarnes, Alexander B.en_US
dc.contributor.authorAndreas, Loren B.en_US
dc.contributor.authorHuber, Matthiasen_US
dc.contributor.authorRamachandran, Rameshen_US
dc.contributor.authorvan der Wel, Patrick C. A.en_US
dc.contributor.authorVeshtort, Mikhailen_US
dc.contributor.authorGriffin, Robert G.en_US
dc.contributor.authorMehta, Manish A.en_US
dc.date.accessioned2013-12-23T16:09:02Z-
dc.date.available2013-12-23T16:09:02Z-
dc.date.issued2009en
dc.identifier.citationBarnes, Alexander B., Loren B. Andreas, Matthias Huber, Ramesh Ramachandran, et al. 2009. "High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine." Journal Of Magnetic Resonance 200(1): 95-100.en_US
dc.identifier.issn1090-7807en_US
dc.identifier.urihttp://hdl.handle.net/11282/309409-
dc.description.abstractWe present a de novo high-resolution structure of the peptide Alanyl-Prolyl-Glycine using a combination of sensitive solid-state NMR techniques that each yield precise structural constraints. High-quality 13C–13C distance constraints are extracted by fitting rotational resonance width (R2W) experiments using Multimode Multipole Floquet Theory and experimental chemical shift anisotropy (CSA) orientations. In this strategy, a structure is first calculated using DANTE-REDOR and torsion angle measurements and the resulting relative CSA orientations are used as an input parameter in the 13C–13C distance calculations. Finally, a refined structure is calculated using all the constraints. We investigate the effect of different structural constraints on structure quality, as determined by comparison to the crystal structure and also self-consistency of the calculated structures. Inclusion of all or subsets of these constraints into CNS calculations resulted in high-quality structures (0.02 Å backbone RMSD using all 11 constraints).en_US
dc.publisherElsevieren_US
dc.identifier.doi10.1016/j.jmr.2009.06.009-
dc.subject.departmentChemistryen_US
dc.titleHigh-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycineen_US
dc.typearticleen_US
dc.identifier.journalJournal Of Magnetic Resonanceen_US
dc.identifier.volume200en_US
dc.identifier.issue1en_US
dc.identifier.startpage95en_US
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