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Solution structure and dynamics of bovine β-lactoglobulin A

Published online by Cambridge University Press:  01 November 1999

KAZUO KUWATA ,
MASARU HOSHINO ,
VINCENT FORGE ,
SEIICHI ERA ,
CARL A. BATT  and
YUJI GOTO
KAZUO KUWATA
Affiliation:
Department of Physiology, School of Medicine, Gifu University, Tsukasamachi, Gifu 500-8705, Japan
MASARU HOSHINO
Affiliation:
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
VINCENT FORGE
Affiliation:
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan Present address: Departement de Biophysique Moleculaire et Structurale, CEA-Grenoble 17, av. des Martyrs, 38054 Grenoble Cedex 09, France.
SEIICHI ERA
Affiliation:
Department of Physiology, School of Medicine, Gifu University, Tsukasamachi, Gifu 500-8705, Japan
CARL A. BATT
Affiliation:
Department of Food Science, Cornell University, Ithaca, New York 14853
YUJI GOTO
Affiliation:
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
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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 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.

Keywords

α-helix to β-sheet transitionβ-lactoglobulindynamicsheteronuclear NMRprotein folding
Type
FOR THE RECORD
Information
Protein Science , Volume 8 , Issue 11 , November 1999 , pp. 2541 - 2545
Copyright
© 1999 The Protein Society

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