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Solution structure and dynamics of bovine β‐lactoglobulin A
Author(s) -
Kuwata Kazuo,
Era Seiichi,
Hoshino Masaru,
Forge Vincent,
Goto Yuji,
Batt Carl A.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.11.2541
Subject(s) - antiparallel (mathematics) , heteronuclear molecule , chemistry , crystallography , dimer , monomer , nanosecond , helix (gastropod) , nuclear magnetic resonance spectroscopy , protein structure , molecular dynamics , circular dichroism , protein secondary structure , stereochemistry , physics , computational chemistry , biochemistry , biology , ecology , laser , organic chemistry , quantum mechanics , magnetic field , snail , optics , polymer
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 β I strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. { 1 H}‐ 15 N NOE revealed that β f , β g , and β H 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.