PubMed · 5619087
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P Chapuy, G Vignon, D Pansu. [Osteomalacia].. https://pubmed.ncbi.nlm.nih.gov/5619087/
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Melittin is a naturally occurring hexacosa peptide which forms an amphiphilic helix in methanol, a random coil in water, and a tetramer of helices at basic pH or in the presence of a high salt concentration. The monomeric structure in methanol has been well characterized by proton NMR (Pastore et al. (1989) Eur. Biophys. J., 16, 363-367). In the present paper, chemical shifts of the backbone alpha-carbons of melittin in methanol were determined by mapping previously published alpha-proton shifts (Bazzo et al. (1988) Eur. J. Biochem., 173, 139-146), to natural abundance (1H)13C cross peaks appearing in the 2D heteronuclear multiple-quantum NMR spectrum. Changes in chemical shifts consequent to stepwise increases in the percentage of water in a mixed methanol/water solvent system were observed in similar spectra. The alpha-carbon shifts varied more smoothly than the corresponding alpha-proton shifts and were found to correlate with the transition from the helix to the random coil conformer in parallel with changes in the circular dichroism spectrum. Chemical shifts of this peptide are interpreted with regard to the current database of assignments in proteins of known 3D structure (Wishart et al. (1991) J. Mol. Biol., 222, 311-333). The N-terminal region of the peptide shows increased flexibility at lower methanol concentrations, as evidenced by the merger of the alpha-proton resonances of G1 (at 40% and 15% methanol) and G3 (at 15% methanol). Conformational exchange rates for G1 and G3 were estimated by comparison of the experimental spectra with simulated spectra and found to be as large as 4000 s-1 for G1 in 40% and 15% methanol and 600 s-1 for G3 in 15% methanol. Overall, these 1H and 13C chemical shift data support the description of monomeric melittin in methanol currently evolving in the literature and suggest a structure composed of a linked pair of helices with different structural stabilities, each of which experiences dynamical fraying at its free terminus.
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Using a dual tracer (44Ca orally and 46Ca i.v.) stable isotope technique, true dietary Ca absorption, endogenous fecal Ca excretion, and net Ca retention were measured in 12 low birth weight (1426 +/- 260 g) infants fed a high Ca-containing formula. Endogenous fecal Ca excretion averaged 7.2 +/- 4.1% of intake, and exceeded 10% of intake in three infants. Net Ca retention, 103 +/- 38 mg/kg/d, was consistent with previous studies of Ca retention obtained using mass balance techniques and correlated closely (r = 0.98, p less than 0.001) with true Ca absorption but not with endogenous fecal excretion (r = -0.40, p = 0.19). Although endogenous fecal excretion may represent a significant source of Ca loss for some low birth weight infants, these data suggest that net Ca retention in low birth weight infants fed a high Ca-containing formula is primarily determined by the total dietary Ca absorbed.