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. 1999 Nov;8(11):2541–2545. doi: 10.1110/ps.8.11.2541

Solution structure and dynamics of bovine beta-lactoglobulin A.

K Kuwata 1, M Hoshino 1, V Forge 1, S Era 1, C A Batt 1, Y Goto 1
PMCID: PMC2144202  PMID: 10595563

Abstract

Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.

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Selected References

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