English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.

MPS-Authors
/persons/resource/persons130763

Shi,  C.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons45954

Fasshuber,  H. K.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons82487

Chevelkov,  V.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons86706

Xiang,  S. Q.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons79129

Habenstein,  B.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons127393

Vasa,  S. K.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15414

Lange,  A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://link.springer.com/content/pdf/10.1007%2Fs10858-014-9820-8.pdf
(Publisher version)

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

2030413.pdf
(Publisher version), 967KB

Supplementary Material (public)

2030413_Suppl.docx
(Supplementary material), 56KB

Citation

Shi, C., Fasshuber, H. K., Chevelkov, V., Xiang, S. Q., Habenstein, B., Vasa, S. K., et al. (2014). BSH-CP based 3D solid-state NMR experiments for protein resonance assignment. Journal of Biomolecular NMR, 59(1), 15-22. doi:10.1007/s10858-014-9820-8.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-908B-8
Abstract
We have recently presented band-selective homonuclear cross-polarization (BSH-CP) as an efficient method for CO-CA transfer in deuterated as well as protonated solid proteins. Here we show how the BSH-CP CO-CA transfer block can be incorporated in a set of three-dimensional (3D) solid-state NMR (ssNMR) pulse schemes tailored for resonance assignment of proteins at high static magnetic fields and moderate magic-angle spinning rates. Due to the achieved excellent transfer efficiency of 33 % for BSH-CP, a complete set of 3D spectra needed for unambiguous resonance assignment could be rapidly recorded within 1 week for the model protein ubiquitin. Thus we expect that BSH-CP could replace the typically used CO-CA transfer schemes in well-established 3D ssNMR approaches for resonance assignment of solid biomolecules.