Solution structure and dynamics of bovine β‐lactoglobulin A

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Abstract
Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine β‐lactoglobulin A at pH 2.0 and 45 °C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight‐stranded continuous antiparallel β‐barrel and one major α‐helix, is similar to the X‐ray dimeric structure obtained at pH 6.2, including βIstrand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. {1H}‐15N NOE revealed that βf, βg, and βH strands buried under the major α‐helix are rigid on a pico‐ to nanosecond time scale and also emphasized rapid fluctuations of loops and the N‐ and C‐terminal regions.