English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy

Luca, S., & Baldus, M. (2002). Enhanced spectral resolution in immobilized peptides and proteins by combining chemical shift sum and difference spectroscopy. Journal of Magnetic Resonance, 159(2), 243-249. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WJX-479TFSJ-4-2B&_cdi=6890&_user=38661&_pii=S1090780702000198&_orig=search&_coverDate=12%2F31%2F2002&_sk=998409997&view=c&wchp=dGLbVlb-zSkzk&md5=0fb80dd870cbe7d0d84d3db72ed09452&ie=/sdarticle.pdf.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F273-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-EEDF-6
Genre: Journal Article

Files

show Files
hide Files
:
17180.pdf (Publisher version), 0B
Name:
17180.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Luca, S.1, Author              
Baldus, M.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Solid State NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society, ou_persistent22              

Content

show
hide
Free keywords: chemical shifts; correlation spectroscope; magic angle spinning; protein backbone structure; spectral resolution
 Abstract: A two-dimensional correlation experiment is introduced that records the sum and difference chemical shift of two scalar or dipolar coupled nuclei. Statistical results indicate that the suggested pulse scheme can significantly increase the possibility of separating chemical shift contributions due to residue type and backbone conformation in immobilized peptides and proteins. Experimental applications demonstrate the theoretical concept and lead to the predicted resolution enhancement between different amino acid types and among protein residues of different secondary structure. (C) 2002 Elsevier Science (USA). All rights reserved.

Details

show
hide
Language(s): eng - English
 Dates: 2002-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Magnetic Resonance
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 159 (2) Sequence Number: - Start / End Page: 243 - 249 Identifier: -