Solution structure and dynamics of bovine beta-lactoglobulin A |
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| Authors: | Kuwata K Hoshino M Forge V Era S Batt C A Goto Y |
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| Affiliation: | Department of Physiology, School of Medicine, Gifu University, Tsukasamachi, Japan. |
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| 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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| Keywords: | α-helix to β-sheet transition β-lactoglobulin dynamics heteronuclear NMR protein folding |
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