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
    Relationship between1H and13C NMR chemical shifts and the secondary and tertiary structure of a zinc finger peptide (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 307-322 
    Details
    ISSN: 1573-5001
    Keywords: Zinc finger ; 2D NMR ; Secondary structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Essentially complete assignments have been obtained for the1H and protonated13C NMR spectra of the zinc finger peptide Xfin-31 in the presence and absence of zinc. The patterns observed for the1H and13C chemical shifts of the peptide in the presence of zinc, relative to the shifts in the absence of zinc, reflect the zinc-mediated folding of the unstructured peptide into a compact globular structure with distinct elements of secondary structure. Chemical shifts calculated from the 3D solution structure of the peptide in the presence of zinc and the observed shifts agree to within ca. 0.2 and 0.6 ppm for the backbone CaH and NH protons, respectively. In addition, homologous zinc finger proteins exhibit similar correlations between their1H chemical shifts and secondary structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01874810
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView (2000)
    Springer
    Journal of biomolecular NMR 18 (2000), S. 43-48 
    Details
    ISSN: 1573-5001
    Keywords: chemical shift ; CSI ; denaturant ; NMRView ; peptide ; random coil
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Studies of proteins unfolded in acid or chemical denaturant can help in unraveling events during the earliest phases of protein folding. In order for meaningful comparisons to be made of residual structure in unfolded states, it is necessary to use random coil chemical shifts that are valid for the experimental system under study. We present a set of random coil chemical shifts obtained for model peptides under experimental conditions used in studies of denatured proteins. This new set, together with previously published data sets, has been incorporated into a software interface for NMRView, allowing selection of the random coil data set that fits the experimental conditions best.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008386816521
    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...