E-resources
Peer reviewed
-
O’Hare, Bernie; Benesi, Alan J.; Showalter, Scott A.
Journal of magnetic resonance (1997), 10/2009, Volume: 200, Issue: 2Journal Article
Exclusively heteronuclear 13C-detected NMR spectroscopy of proteins in solution has seen resurgence in the past several years. For disordered or unfolded proteins, which tend to have poor 1H-amide chemical shift dispersion, these experiments offer enhanced resolution and the possibility of complete heteronuclear resonance assignment at the cost of leaving the 1H resonances unassigned. Here we report two novel 13C-detected NMR experiments which incorporate a 1H chemical shift evolution period followed by 13C-TOCSY mixing for aliphatic 1H resonance assignment without reliance on 1H detection.
![loading ... loading ...](themes/default/img/ajax-loading.gif)
Shelf entry
Permalink
- URL:
Impact factor
Access to the JCR database is permitted only to users from Slovenia. Your current IP address is not on the list of IP addresses with access permission, and authentication with the relevant AAI accout is required.
Year | Impact factor | Edition | Category | Classification | ||||
---|---|---|---|---|---|---|---|---|
JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
Select the library membership card:
If the library membership card is not in the list,
add a new one.
DRS, in which the journal is indexed
Database name | Field | Year |
---|
Links to authors' personal bibliographies | Links to information on researchers in the SICRIS system |
---|
Source: Personal bibliographies
and: SICRIS
The material is available in full text. If you wish to order the material anyway, click the Continue button.