Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-12-01T01:02:32.477Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)