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  • 1
    Electronic Resource
    Electronic Resource
    Determination of heteronuclear three-bond J-coupling constants in peptides by a simple heteronuclear relayed E.COSY experiment (1995)
    Springer
    Journal of biomolecular NMR 6 (1995), S. 95-105 
    Details
    ISSN: 1573-5001
    Keywords: 2D heteronuclear NMR ; Isotope labeling ; Coupling constants ; Antamanide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A simple heteronuclear relayed E.COSY pulse sequence with a minimum number of pulses is proposed for the quantitative determination of heteronuclear three-bond J-coupling constants in uniformly 13C-enriched polypeptide samples. Numerous heteronuclear three-bond coupling constants, including $${}^3{\text{J}}_{{\text{H}}^{\text{N}} {\text{C}}'} $$ , $${}^3{\text{J}}_{{\text{H}}^{\text{N}} {\text{C}}^\beta } $$ , $${}^3{\text{J}}_{{\text{H}}^\beta {\text{C}}'} $$ , and $${}^3{\text{J}}_{{\text{H}}^\alpha {\text{C}}^\gamma } $$ , can be determined for each residue from a single heteronuclear relayed E.COSY spectrum. Couplings relevant for stereospecific assignments as well as for the determination of dihedral angles in the amino acid backbone and in side chains are obtained. The method is demonstrated on the uniformly 13C-enriched decapeptide antamanide (-Val1-Pro2-Pro3-Ala4-Phe5-Phe6-Pro7-Pro8-Phe9-Phe10-).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417495
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  • 2
    Electronic Resource
    Electronic Resource
    Self-consistent 3J coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles (1999)
    Springer
    Journal of biomolecular NMR 14 (1999), S. 1-12 
    Details
    ISSN: 1573-5001
    Keywords: cross validation ; data redundance ; φ torsion angle ; vicinal coupling constants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The concept of self-consistent J coupling evaluation exploits redundant structure information inherent in large sets of 3J coupling constants. Application to the protein Desulfovibrio vulgaris flavodoxin demonstrates the simultaneous refinement of torsion-angle values and related Karplus coefficients. The experimental basis includes quantitative coupling constants related to the polypeptide backbone φ torsion originating from a variety of heteronuclear 2D and 3D NMR correlation experiments, totalling 124 3J(HN,Hα), 129 3J(HN,C′), 121 3J(HN,Cβ), 128 3J(C′i−1,Hαi), 121 3J(C′i−1,C′i), and 122 3J(C′i−1,Cβi). Without prior knowledge from either X-ray crystallography or NMR data, such as NOE distance constraints, accurate φ dihedral angles are specified for 122 non-glycine and non-proline residues out of a total of 147 amino acids. Different models of molecular internal mobility are considered. The Karplus coefficients obtained are applicable to the conformational analysis of φ torsions in other polypeptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008345303942
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  • 3
    Electronic Resource
    Electronic Resource
    Heteronuclear relayed E.COSY revisited: Determination of 3J(Hα,Cγ) couplings in Asx and aromatic residues in proteins (2000)
    Springer
    Journal of biomolecular NMR 18 (2000), S. 13-22 
    Details
    ISSN: 1573-5001
    Keywords: χ1-angle ; flavodoxin ; multiple-quantum line-narrowing ; multiplet simulation ; ribonuclease T1 ; vicinal coupling constants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Constant-time 3D heteronuclear relayed E.COSY [Schmidt et al. (1996) J. Biomol. NMR, 7, 142–152], as based on generic 2D small-flip-angle HMQC-COSY [Schmidt et al. (1995) J. Biomol. NMR, 6, 95–105], has been modified to allow for quantitative determination of heteronuclear three-bond 3 J(Hα,Cγ) couplings. The method is applicable to amino acid spin topologies with carbons in the γ position which lack attached protons, i.e. to asparagine, aspartate, and aromatic residues in uniformly 13C-enriched proteins. The pulse sequence critically exploits heteronuclear triple-quantum coherence (HTQC) of CH2 moieties involving geminal Hβ proton pairs, taking advantage of improved multiple-quantum relaxation properties, at the same time avoiding scalar couplings between those spins involved in multiple-quantum coherence, thus yielding E.COSY-type multiplets with a splitting structure that is simpler than with the original scheme. Numerical least-squares 2D line-shape simulation is used to extract 3 J(Hα,Cγ) coupling constants which are of relevance to side-chain χ1 dihedral-angle conformations in polypeptides. Methods are demonstrated with recombinant 15N,13C-enriched ribonuclease T1 and Desulfovibrio vulgaris flavodoxin with bound oxidized FMN.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008385202639
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