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Default 1H and 15N NMR resonance assignments and solution secondary structure of oxidized Des

1H and 15N NMR resonance assignments and solution secondary structure of oxidized Desulfovibrio desulfuricans flavodoxin.

Related Articles 1H and 15N NMR resonance assignments and solution secondary structure of oxidized Desulfovibrio desulfuricans flavodoxin.

J Biomol NMR. 1996 May;7(3):225-35

Authors: Pollock JR, Swenson RP, Stockman BJ

Sequence-specific 1H and 15N resonance assignments have been made for 137 of the 146 nonprolyl residues in oxidized Desulfovibrio desulfuricans [Essex 6] flavodoxin. Assignments were obtained by a concerted analysis of the heteronuclear three-dimensional 1H-15N NOESY-HMQC and TOCSY-HMQC data sets, recorded on uniformly 15N-enriched protein at 300 K. Numerous side-chain resonances have been partially or fully assigned. Residues with overlapping 1HN chemical shifts were resolved by a three-dimensional 1H-15N HMQC-NOESY-HMQC spectrum. Medium- and long-range NOEs, 3JNH alpha coupling constants, and 1HN exchange data indicate a secondary structure consisting of five parallel beta-strands and four alpha-helices with a topology similar to that of Desulfovibrio vulgaris [Hildenborough] flavodoxin. Prolines at positions 106 and 134, which are not conserved in D. vulgaris flavodoxin, contort the two C-terminal alpha-helices.

PMID: 8785498 [PubMed - indexed for MEDLINE]



Source: PubMed
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