Determination of the Complete Structure of a Uniformly Labeled Molecule by Rotational Resonance Solid-State NMR in the Tilted Rotating Frame

Nomura, Kaoru; Takegoshi, K.; Terao, Takehiko; Uchida, Kenichi; Kainosho, Masatsune

doi:10.1021/ja984330j

Cited by 84 publications

(77 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Such efforts have given rise to a handful of 3D structures ranging from two-and three-residue peptides to small proteins. [3,[11][12][13] In particular, we have shown [13][14][15] that 3D molecular structures can be constructed through the use of a single, uniformly labeled sample.…”

Section: Introductionmentioning

confidence: 98%

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin

et al. 2005

View full text Add to dashboard Cite

Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly [13C,15N]-labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the construction of 3D molecular structure and study the influence of solid-phase protein preparation on solid-state NMR spectra. A comparative analysis of 13C', 13Calpha, and 13Cbeta resonance frequencies suggests that 13C chemical-shift variations are most likely to occur in protein regions that exhibit an enhanced degree of molecular mobility. Our results can be refined by additional solid-state NMR techniques and serve as a reference for ongoing efforts to characterize the structure and dynamics of (membrane) proteins, protein complexes, and other biomolecules by high-resolution solid-state NMR.

show abstract

Section: Introductionmentioning

confidence: 98%

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Solid-state Nuclear Magnetic Resonance (ssNMR) has recently made significant progress in probing molecular structures in applications ranging from solid-phase peptides and small proteins [1][2][3][4][5][6][7][8] to protein fibrils [5,[9][10][11][12][13] and membrane protein complexes [14][15][16] . In addition, the structural characterization of nonpeptidic molecules and the conformational changes associated with their coordination in a (bio)chemical matrix or within the bulk of larger structures is of high technological and pharmacological interest.…”

Section: Introductionmentioning

confidence: 99%

High‐Resolution Solid‐State NMR Structure of an Anticancer Agent

et al. 2007

View full text Add to dashboard Cite

We demonstrate that solid-state NMR methods can be used to rapidly determine the high-resolution 3D structure of Epothilone B in the polycrystalline state. The solid-state NMR structures exhibit an average heavy atom RMSD to the mean structure of 0.14 A. The 3D-structural analysis leads to stereospecific assignments and provides insight into the influence of intermolecular interactions upon ssNMR chemical-shift parameters. Our results pave the way to the study of ligand-microtubule interactions in a noncrystalline and insoluble environment at atomic level.

show abstract

“…3D molecular structures of small peptides have been probed by using solid-state NMR spectroscopic methods based on the determination of specific 13 C- 13 C or 13 C-15 N distances. [3,4] These techniques can require a high degree of spectral dispersion and the recording of a large number of NMR spectra. The extension of such methods to larger polypeptides may therefore be difficult.…”

mentioning

confidence: 99%

A Concept for Rapid Protein‐Structure Determination by Solid‐State NMR Spectroscopy

et al. 2005

View full text Add to dashboard Cite

The three‐dimensional fold of an immobilized polypeptide is predicted at atomic resolution from solid‐state NMR spectroscopic data (see picture) obtained for a single uniformly [13C,15N] isotope labeled sample. The method involves the combined analysis of conformation‐dependent NMR frequencies and short 1H–1H distances and may lead to the rapid characterization of three‐dimensional protein structures.

show abstract

Determination of the Complete Structure of a Uniformly Labeled Molecule by Rotational Resonance Solid-State NMR in the Tilted Rotating Frame

Cited by 84 publications

References 26 publications

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin

High‐Resolution Solid‐State NMR Structure of an Anticancer Agent

A Concept for Rapid Protein‐Structure Determination by Solid‐State NMR Spectroscopy

Contact Info

Product

Resources

About

Determination of the Complete Structure of a Uniformly Labeled Molecule by Rotational Resonance Solid-State NMR in the Tilted Rotating Frame

Cited by 84 publications

References 26 publications

High‐Resolution Solid‐State NMR Studies on Uniformly [13C,15N]‐Labeled Ubiquitin

High‐Resolution Solid‐State NMR Studies on Uniformly [13C,15N]‐Labeled Ubiquitin

High‐Resolution Solid‐State NMR Structure of an Anticancer Agent

A Concept for Rapid Protein‐Structure Determination by Solid‐State NMR Spectroscopy

Contact Info

Product

Resources

About

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin

High‐Resolution Solid‐State NMR Studies on Uniformly [¹³C,¹⁵N]‐Labeled Ubiquitin