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
  • 1
    Electronic Resource
    Electronic Resource
    A three-dimensional NMR experiment with improved sensitivity for carbonyl–carbonyl J correlation in proteins (1997)
    Springer
    Journal of biomolecular NMR 9 (1997), S. 207-211 
    Details
    ISSN: 1573-5001
    Keywords: Carbon–carbon J coupling ; HOHAHA ; TOCSY ; Relaxation ; φ Angle ; HIV-1 Nef ; Ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Recently, a quantitative J correlation technique has been presented that permits measurementof 3JC′C′ in proteins isotopically enriched with 13C [Hu, J.-S. and Bax, A.(1996) J. Am. Chem. Soc., 118, 8170–8171]. Here, we describe an analogousexperiment that is less sensitive to transverse 13C′ relaxation, which is the principallimiting factor in all 13C-13C long-range correlation experiments on macromolecules. Thenew scheme utilizes homonuclear Hartmann–Hahn cross polarization (TOCSY) insteadof a COSY-type transfer to accomplish magnetization transfer; a description of the relevantrelaxation terms is presented. The experiment is demonstrated for ubiquitin and HIV-1 Nef.The results show excellent agreement between 3JC′C′ values measured forubiquitin with the new scheme and those reported previously. The experiment is particularlyuseful for distinguishing backbone φ angles that are smaller than -120° from thoselarger than -120°.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018614505948
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N (1995)
    Springer
    Journal of biomolecular NMR 5 (1995), S. 376-382 
    Details
    ISSN: 1573-5001
    Keywords: Deuterium ; Triple resonance ; Isotope labeling ; Sequential assignment ; Ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary It is demonstrated that sequential resonance assignment of the backbone 1Hα and 15N resonances of proteins can be obtained without recourse to the backbone amide protons, an approach which should be useful for assignment of regions with rapidly exchanging backbone amide protons and for proteins rich in proline residues. The method relies on the combined use of two 2D experiments, HA(CA)N and HA(CACO)N or their 3D analogs, which correlate 1Hα with the intraresidue 15N and with the 15N resonance of the next residue. The experiments are preferably conducted in D2O, where very high resolution in the 15N dimension can be achieved by using 2H decoupling. The approach is demonstrated for a sample of human ubiquitin, uniformly enriched in 13C and 15N. Complete backbone and 13Cβ/1Hβ resonance assignments are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00182281
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    χ1 angle information from a simple two-dimensional NMR experiment that identifies trans 3JNCγ couplings in isotopically enriched proteins (1997)
    Springer
    Journal of biomolecular NMR 9 (1997), S. 323-328 
    Details
    ISSN: 1573-5001
    Keywords: χ1 angle ; Calmodulin ; Carbon-nitrogen J coupling ; Quantitative J correlation ; Stereospecific assignment ; Ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract New quantitative J correlation experiments are used for measuring all two- and three-bondcouplings between 15N and aliphatic side-chain carbons in proteins uniformly enriched in 13Cand 15N. Results show that 3JNCβ and 2JNCβ invariably are very small.Therefore, a simple and relatively sensitive two-dimensional spin-echo difference experimentcan be used to identify residues with a 3JNCγ coupling substantially larger than 1Hz, indicative of a trans arrangement between N and Cγ. This measurement thereforeprovides χ1 angle information for residues with an aliphatic Cγ carbon, andthereby also aids in making stereospecific assignments of Hβ resonances. Experimentsare demonstrated for ubiquitin and for a complex between calmodulin and a 26-residuepeptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018691228238
    Location Call Number Expected 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...