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Evaluation of errors of interproton distances and correlation time determined from NMR cross-relaxation rates (1992)

Isernia, Carla ; Paolillo, Livio ; Russo, Ernesto ; [et al.]

Springer

Journal of biomolecular NMR 2 (1992), S. 573-582

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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

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Elucidation of the structure of constrained bicyclopeptides in solution by two-dimensional cross-relaxation spectroscopy: Amatoxin analogues (1996)

Isernia, Carla ; Falcigno, Lucia ; Macura, Slobodan ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Peptide Science 2 (1996), S. 3-13

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ISSN: 1075-2617

Keywords: Structure of amatoxin analogues ; constrained bicyclopeptides ; NMR ; molecular dynamics ; Chemistry ; Biochemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The evaluation of peptide structures in solution is made feasible by the combined use of two-dimensional NMR in the laboratory (NOESY) and rotating frames (ROESY), and by the use of molecular dynamics calculations. The present paper describes how both the NMR method and molecular dynamics calculations were applied to very rigid synthetic bicyclic peptides that are analogues of natural amatoxins. The NMR theory, which allows the estimate of interatomic distances between interacting nuclei, is briefly discussed. The experimental data were compared with those of known solid-state structures. Three amatoxin analogues have been examined. Of these, one is biologically active (S-deoxo γ[R] OH-Ile3-amaninamide) and its structure in the solid state has recently been worked out. The second and third analogues (S-deoxo-Ile3 -Ala5-amaninamide and S-deoxo-D-Ile3 -amaninamide, respectively) are inactive and their solid-state structures are unknown. The data presented confirm the authors' previous hypothesis that lack of biological activity of S-deoxo-Ile3-Ala5- amaninamide is due to the masking of the tryptophan ring by the methyl group of L-Ala and not to massive conformational changes of the analogue.

Additional Material: 6 Ill.