73 research outputs found
Tautomerism provides a molecular explanation for the mutagenic properties of the anti-HIV nucleoside 5-aza-5,6-dihydro-2'-deoxycytidine
Nuclear magnetic resonance studies on old yellow enzyme I. 15N NMR spectra of the enzyme recombined with 15N labeled flavin mononucleotides
Nuclear magnetic resonane investigation of 15 N-labeled flavins, free and bound to Megasphaera elsdenii apoflavodoxin
NMR stud. O.Y.E. II.13C NMR spect. enzyme recomb. with 13C labeled flavin mononucl.,31P NMR spect. interact. O.Y.E. with phenols reveal. 13C & 15N NMR spectra
PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION INVESTIGATION OF COMPLEX-FORMATION OF THE NH2-TERMINAL DNA-BINDING DOMAIN OF LAC REPRESSOR WITH POLY[D(AT)]
Semi-automatic Stereospecific Resonance and NOESY Assignment of Proteins Based on the Tertiary Structure – the Program nmr2st
PHOTOCHEMICALLY INDUCED DYNAMIC NUCLEAR-POLARIZATION INVESTIGATION OF COMPLEX-FORMATION OF THE NH2-TERMINAL DNA-BINDING DOMAIN OF LAC REPRESSOR WITH POLY[D(AT)]
Solution structure of fatty acid-binding protein from human brain.
Item does not contain fulltextHuman brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity
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