Solution structure and dynamics of bovine β-lactoglobulin A

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...

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Bibliographic Details
Published in:Protein science 1999-11, Vol.8 (11), p.2541-2545
Main Authors: KUWATA, KAZUO, HOSHINO, MASARU, FORGE, VINCENT, ERA, SEIICHI, BATT, CARL A., GOTO, YUJI
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cattle
dynamics
FOR THE RECORD
Genetic Variation
heteronuclear NMR
Hydrogen-Ion Concentration
Lactoglobulins - chemistry
Lactoglobulins - metabolism
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
protein folding
Protein Structure, Secondary
Solutions
α‐helix to β‐sheet transition
β‐lactoglobulin
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Summary: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 βI-strand 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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.8.11.2541