Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments (1999)
    Springer
    Journal of biomolecular NMR 15 (1999), S. 181-184 
    Details
    ISSN: 1573-5001
    Keywords: concatenation ; protein NMR ; resonance assignments ; sensitivity enhancement ; TROSY in triple resonance experiments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In experiments with proteins of molecular weights around 100 kDa the implementation of [15N,1H]-TROSY-elements in [15N]-constant-time triple resonance experiments yields sensitivity enhancements of one to two orders of magnitude. An additional gain of 10 to 20% may be obtained with the use of ‘sensitivity enhancement elements’. This paper describes a novel sensitivity enhancement scheme which is based on concatenation of the 13 Cα → 15N magnetization transfer with the ST2-PT element, and which enables proper TROSY selection of the 15N multiplet components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008358030477
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    [13c]-Constant-Time [15n,1h]-Trosy-Hnca for Sequential Assignments of Large Proteins (1999)
    Springer
    Journal of biomolecular NMR 14 (1999), S. 85-88 
    Details
    ISSN: 1573-5001
    Keywords: HNCA with 13C constant-time evolution ; protein NMR ; resonance assignments ; spectral resolution ; triple resonance experiments ; TROSY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The greatly improved sensitivity resulting from the use of TROSY during 15N evolution and amide proton acquisition enables the recording of HNCA spectra of large proteins with constant-time 13Cα evolution. In [13C]-ct-[15N,1H]-TROSY-HNCA experiments with a 2H/13C/15N-labeled 110 kDa protein, 7,8-dihydroneopterin aldolase from Staphylococcus aureus, nearly all correlation peaks seen in the [15N,1H]-TROSY-HNCA spectrum were also detected. The improved resolution in the 13C dimension then enabled a significant number of sequential assignments that could not be obtained with [15N,1H]-TROSY-HNCA without [13C]-constant-time period.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008346931993
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...