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Solution structure and dynamics of bovine beta-lactoglobulin A.


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.

SUBMITTER: Kuwata K 

PROVIDER: S-EPMC2144202 | biostudies-other | 1999 Nov

REPOSITORIES: biostudies-other

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Solution structure and dynamics of bovine beta-lactoglobulin A.

Kuwata K K   Hoshino M M   Forge V V   Era S S   Batt C A CA   Goto Y Y  

Protein science : a publication of the Protein Society 19991101 11


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  ...[more]

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