English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Direct observation of millisecond to second motions in proteins by dipolar CODEX NMR spectroscopy.

Krushelnitsky, A., deAzevedo, E., Linser, R., Reif, B., Saalwächter, K., & Reichert, D. (2009). Direct observation of millisecond to second motions in proteins by dipolar CODEX NMR spectroscopy. Journal of the American Chemical Society, 131(34), 12097-12099. doi:10.1021/ja9038888.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-EE2C-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C5C5-6
Genre: Journal Article

Files

show Files
hide Files
:
2007689.pdf (Publisher version), 616KB
 
File Permalink:
-
Name:
2007689.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), MBPC; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2007689_Suppl.pdf (Supplementary material), 552KB
Name:
2007689_Suppl.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://pubs.acs.org/doi/pdf/10.1021/ja9038888 (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Krushelnitsky, A., Author
deAzevedo, E., Author
Linser, R.1, Author              
Reif, B., Author
Saalwächter, K., Author
Reichert, D., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

Content

show
hide
Free keywords: -
 Abstract: We present a site-resolved study of slow (ms to s) motions in a protein in the solid (microcrystalline) state performed with the use of a modified version of the centerband-only detection of exchange (CODEX) NMR experiment. CODEX was originally based on measuring changes in molecular orientation by means of the chemical shift anisotropy (CSA) tensor, and in our modification, angular reorientations of internuclear vectors are observed. The experiment was applied to the study of slow 15N−1H motions of the SH3 domain of chicken α-spectrin. The protein was perdeuterated with partial back-exchange of protons at labile sites. This allowed indirect (proton) detection of 15N nuclei and thus a significant enhancement of sensitivity. The diluted proton system also made negligible proton-driven spin diffusion between 15N nuclei, which interferes with the molecular exchange (motion) and hampers the acquisition of dynamic parameters. The experiment has shown that approximately half of the peaks in the 2D 15N−1H correlation spectrum exhibit exchange in a different extent. The correlation time of the slow motion for most peaks is 1 to 3 s. This is the first NMR study of the internal dynamics of proteins in the solid state on the millisecond to second time scale with site-specific spectral resolution that provides both time-scale and geometry information about molecular motions.

Details

show
hide
Language(s): eng - English
 Dates: 2009-08-122009-09-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/ja9038888
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of the American Chemical Society
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 131 (34) Sequence Number: - Start / End Page: 12097 - 12099 Identifier: -