English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins.

Yao, X., Becker, S., & Zweckstetter, M. (2014). A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins. Journal of Biomolecular NMR, 60(4), 231-240. doi:10.1007/s10858-014-9872-9.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-4B01-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-80C1-1
Genre: Journal Article

Files

show Files
hide Files
:
2077098.pdf (Publisher version), 956KB
 
File Permalink:
-
Name:
2077098.pdf
Description:
-
OA-Status:
Visibility:
Restricted (UNKNOWN id 303; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2077098_Suppl.pdf (Supplementary material), 84KB
View   Save
File Permalink:
https://hdl.handle.net/11858/00-001M-0000-0024-4B04-1
Name:
2077098_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
View
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://link.springer.com/content/pdf/10.1007%2Fs10858-014-9872-9.pdf (Publisher version)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Yao, X.1, Author           
Becker, S.2, Author           
Zweckstetter, M.1, Author           
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: NMR; Intrinsically disordered protein; Assignment;Alpha-synuclein; APSY; Solvent exchange
 Abstract: Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY) experiment for backbone assignment of intrinsically disordered proteins. The 6D HCACONCAH APSY correlates the six different chemical shifts, Halpha(i-1), Calpha(i-1), C'(i-1), N(i), Calpha(i) and Halpha(i). Application to two intrinsically disordered proteins, 140-residue alpha-synuclein and a 352-residue isoform of Tau, demonstrates that the chemical shift information provided by the 6D HCACONCAH APSY allows efficient backbone resonance assignment of intrinsically disordered proteins.

Details

show
hide
Language(s): eng - English
 Dates: 2014-11-042014-12
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s10858-014-9872-9
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biomolecular NMR
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 60 (4) Sequence Number: - Start / End Page: 231 - 240 Identifier: -