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
Filter
  • Heme protein  (2)
  • 2D NMR  (1)
  • CSI  (1)
  • 1
    Electronic Resource
    Electronic Resource
    1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin (1994)
    Springer
    Journal of biomolecular NMR 4 (1994), S. 491-504 
    Details
    ISSN: 1573-5001
    Keywords: Heme protein ; Multidimensional NMR ; Sequential assignment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Sequence-specific backbone 1H and 15N resonance assignments have been made for 95% of the amino acids in sperm whale myoglobin, complexed with carbon monoxide (MbCO). Many assignments for side-chain resonances have also been obtained. Assignments were made by analysis of an extensive series of homonuclear 2D spectra, measured with unlabeled protein, and both 2D and 3D 1H-15N-correlated spectra obtained from uniformly 15N-labeled myoglobin. Patterns of medium-range NOE connectivities indicate the presence of eight helices in positions that are very similar to those found in the crystal structures of sperm whale myoglobin. The resonance assignments of MbCO form the basis for determination of the solution structure and for hydrogen-exchange measurements to probe the stability and folding pathways of myoglobin. They will also form a basis for assignment of the spectra of single-site mutants with altered ligand-binding properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00156616
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Overexpression of myoglobin and assignment of its amide, Cα and Cβ resonances (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 271-276 
    Details
    ISSN: 1573-5001
    Keywords: Inclusion bodies ; Heme protein ; Heteronuclear NMR ; Myoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Sperm whale apomyoglobin was expressed to high levels on minimal media and isotopically labeled with 13C and 15N nuclei. The isotopically labeled apoprotein was purified to homogeneity in a single step by reversed-phase chromatography and reconstituted with hemin and carbon monoxide gas for NMR analysis. Sequence-specific backbone 1HN, 15N and 13Cα as well as side-chain 13Cβ resonance assignments have been made for over 90% of the amino acids in the carbon monoxide complex of the protein. Resonance assignments were made by analysis of a series of 3D triple resonance spectra measured on the uniformly labeled sample. These assignments will provide the basis for analyzing the effects of point site mutations on the structure, stability and dynamics of the protein in solution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197808
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
  • 4
    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...