ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
  • Evaluation of errors  (1)
  • FK506 binding proteins  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Evaluation of errors of interproton distances and correlation time determined from NMR cross-relaxation rates (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 573-582 
    Details
    ISSN: 1573-5001
    Keywords: Amaninamide ; Correlation time ; Evaluation of errors ; Interproton distances ; NOESY ; ROESY ; 2D NMR ; Peptides ; Cross-relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have analyzed a combined use of the two-dimensional nuclear Overhauser effect in the laboratory frame (NOESY) and in the rotating frame (ROESY) to determine interproton distances and correlation time in medium-sized rigid molecules (Davis, 1987). This method can be applied in the intermediate motional regime, 0.2 〈 ωoτc, 〈 5, (τc, correlation time, (ωo resonance frequency). Error limits depend on the motional regime and are smallest near ωoτc=1.14. The method was tested on six geminal proton pairs in the bicyclic octapeptide (S-deoxo-γ-[R]-OH-Ile3 amaninamide, Mw =870) for which at 297 K in DMSO, a correlation time of 1.0 ns, with a standard deviation of 0.12 ns, and an interproton distance of 1.87 Å, with standard deviation of 0.04 Å, are obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02192846
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Solution conformational preferences of a peptidic analogue of a natural macrolide (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 349-361 
    Details
    ISSN: 0006-3525
    Keywords: cyclic peptides ; molecular dynamics ; nmr ; conformation ; FK506 ; FK506 binding proteins ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational behavior in solution of a cyclic peptide with sequence cyclo-(Pro1-Pro2-Dab3 (cHexA)ψ[N7HCO]-Leu4ψ[NHCO]-Suc5-Gly6-) has been throughly investigated with the combined use of nmr and molecular dynamic techniques. The compound, which has been modeled to mimic the FK506 macrolide bound to the FK506 binding protein structure, can be considered as a peptidic analogue of the FK506 system.The synthesis was carried out on a phenylacetoamidomethyl resin using an appropriate protocol for the peptide chain elongation. The conformational properties of the cyclic hexapeptide were studied in DMSO and water. The nmr data in DMSO and restrained molecular dynamics simulations show the presence of two contiguous cis peptide bonds involving the -Gly-Pro-Pro- segment. This segment in water exhibits conformational heterogeneity presenting at least two distinct conformational families, characterized the first by cis-cis and the second by a trans-cis Gly-Pro-Pro configuration; the trans-cis isomer was fully characterized. © 1997 John Wiley & Sons, Inc. Biopoly 42: 349-361, 1997
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...