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Comparative Study
. 1999 Nov;8(11):2541-5.
doi: 10.1110/ps.8.11.2541.

Solution structure and dynamics of bovine beta-lactoglobulin A

K Kuwata  1 , M Hoshino, V Forge, S Era, C A Batt, Y Goto
Affiliations
Comparative Study

Solution structure and dynamics of bovine beta-lactoglobulin A

K Kuwata et al. Protein Sci. 1999 Nov.

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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