SIAM, a Novel NMR Experiment for the Determination of Homonuclear Coupling Constants

Prasch, Thomas; Gröschke, Peter; Glaser, Steffen J.

doi:10.1002/(sici)1521-3773(19980403)37:6<802::aid-anie802>3.3.co;2-d

Cited by 5 publications

(5 citation statements)

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“…Before Fourier transformation, the time domain data were multiplied with shifted squared sinebell window functions. The vicinal scalar coupling constants 3 J NHa were determined using the SIAM-TACSY and Keeler-Titman approaches [11,12] using macros written by T. Prasch for the program FELIX (Felix 95; MSI, San Diego, CA, USA). Signal overlap in the 800-MHz NOESY made peak integration unreliable.…”

Section: Nmr Measurementsmentioning

confidence: 99%

Structure and potential C‐terminal dimerization of a recombinant mutant of surfactant‐associated protein C in chloroform/methanol

Luy

Diener

Hummel³

et al. 2004

European Journal of Biochemistry

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The solution structure of a recombinant mutant [rSP‐C (FFI)] of the human surfactant‐associated protein C (hSP‐C) in a mixture of chloroform and methanol was determined by high‐resolution NMR spectroscopy. rSP‐C (FFI) contains a helix from Phe5 to the C‐terminal Leu34 and is thus longer by two residues than the helix of porcine SP‐C (pSP‐C), which is reported to start at Val7 in the same solvent. Two sets of resonances at the C‐terminus of the peptide were observed, which are explained by low‐order oligomerization, probably dimerization of rSP‐C (FFI) in its α‐helical form. The dimerization may be induced by hydrogen bonding of the C‐terminal carboxylic groups or by the strictly conserved C‐terminal heptapeptide segment with a motif similar to the GxxxG dimerization motif of glycophorin A. Dimerization at the heptapeptide segment would be consistent with findings based on electrospray ionization MS data, chemical cross‐linking studies, and CNBr cleavage data.

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Section: Nmr Measurementsmentioning

confidence: 99%

Structure and potential C‐terminal dimerization of a recombinant mutant of surfactant‐associated protein C in chloroform/methanol

Luy

Diener

Hummel³

et al. 2004

European Journal of Biochemistry

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“…Three-bond coupling constants between H N and H d atoms, 3 J HN-Ha , were measured by MOCCA-SIAM experiments [23,24]. The values of the coupling constants were determined using the procedure described by Titman and Keeler [25].…”

Section: Determination Of Dihedral Angles and Hydrogen Bondsmentioning

confidence: 99%

“…Note that the z-axis denoting the direction of largest partial alignment is oriented nearly parallel to the b-sheet and the a-helices. The eigenvalues of the tensor are S zz ¼ 0.000491, S yy ¼ )0.000313, S xx ¼ )0.000178.program PROCHECK-NMR[46] recognizes a central antiparallel b-sheet consisting of strands A (residues 2-7), B (31-37), C (40-43) and D (60-67), two relatively long a-helices a(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27) and c (70-83), as well as the short a-helix b(47)(48)(49)(50). The analysis of chemical shifts[44] predicts essentially the same secondary structure elements at slightly different positions (b-strands: strand A, 1-9; strand B, 32-36; strand C, 39-42; strand D, 59-66; a-helices: helix a, 12-26; helix b, 47-51; helix c, 69-82).…”

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confidence: 99%

Solution structure of the active‐centre mutant I14A of the histidine‐containing phosphocarrier protein from Staphylococcus carnosus

Möglich

Koch

Gronwald

et al. 2004

European Journal of Biochemistry

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High‐pressure NMR experiments performed on the histidine‐containing phosphocarrier protein (HPr) from Staphylococcus carnosus have shown that residue Ile14, which is located in the active‐centre loop, exhibits a peculiarly small pressure response. In contrast, the rest of the loop shows strong pressure effects as is expected for typical protein interaction sites. To elucidate the structural role of this residue, the mutant protein HPr(I14A), in which Ile14 is replaced by Ala, was produced and studied by solution NMR spectroscopy. On the basis of 1406 structural restraints including 20 directly detected hydrogen bonds, 49 1HN‐15N, and 25 1HN‐1Hα residual dipolar couplings, a well resolved three‐dimensional structure could be determined. The overall fold of the protein is not influenced by the mutation but characteristic conformational changes are introduced into the active‐centre loop. They lead to a displacement of the ring system of His15 and a distortion of the N‐terminus of the first helix, which supports the histidine ring. In addition, the C‐terminal helix is bent because the side chain of Leu86 located at the end of this helix partly fills the hydrophobic cavity created by the mutation. Xenon, which is known to occupy hydrophobic cavities, causes a partial reversal of the mutation‐induced structural effects. The observed structural changes explain the reduced phosphocarrier activity of the mutant and agree well with the earlier suggestion that Ile14 represents an anchoring point stabilizing the active‐centre loop in its correct conformation.

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“…The approach is also applicable to isotropic mixing conditions as produced by heteronuclear isotropic Hartmann-Hahn (HIHAHA) sequences and homonuclear Hartmann-Hahn (HOHAHA/TOCSY) experiments, for which the transfer into inphase and antiphase magnetization was already used in the SIAM-TACSY approach [38,39]. HOHAHA experiments applied to dipolar coupled spins, however, do not produce isotropic mixing conditions [40][41][42] and the spin state selective approach can only be applied along the principle axis of the transfer element [43,33].…”

Section: Discussionmentioning

confidence: 99%

Spin state selectivity and heteronuclear Hartmann–Hahn transfer

Luy¹

2004

Journal of Magnetic Resonance

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SIAM, a Novel NMR Experiment for the Determination of Homonuclear Coupling Constants

Cited by 5 publications

References 0 publications

Structure and potential C‐terminal dimerization of a recombinant mutant of surfactant‐associated protein C in chloroform/methanol

Structure and potential C‐terminal dimerization of a recombinant mutant of surfactant‐associated protein C in chloroform/methanol

Solution structure of the active‐centre mutant I14A of the histidine‐containing phosphocarrier protein from Staphylococcus carnosus

Spin state selectivity and heteronuclear Hartmann–Hahn transfer

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