Solution structure and dynamics of bovine beta-lactoglobulin A.
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.
Kuwata
K
K
Department of Physiology, School of Medicine, Gifu University, Tsukasamachi, Japan.
Hoshino
M
M
Forge
V
V
Era
S
S
Batt
C A
CA
Goto
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D014644:Genetic Variation; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012996:Solutions
D007782:Lactoglobulins; D012996:Solutions