Premium
Mutant bovine odorant‐binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations
Author(s) -
Marabotti Anna,
Lefèvre Thierry,
Staiano Maria,
Crescenzo Roberta,
Varriale Antonio,
Rossi Mosè,
Pézolet Michel,
D'Auria Sabato
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21966
Subject(s) - chemistry , molecular dynamics , dimer , crystallography , protein structure , biophysics , mutant , lipocalin , monomer , mutant protein , circular dichroism , computational chemistry , biochemistry , biology , organic chemistry , gene , polymer
Bovine odorant‐binding protein (bOBP), a member of the lipocalin family, presents the so‐called 3D “domain‐swapped” protein structure. In fact, in solution, it appears as a dimer in which each monomer is composed by the classical lipocalin fold, with a central β‐barrel followed by a stretch of residues and the α‐helix domain protruding out of the barrel and crossing the dimer interface. Recently, a deswapped mutant form of bOBP was obtained, in which a Gly residue was inserted after position 121 and the two residues in position 64 and 156 were replaced by Cys residues for restoring the disulfide bridge common to the lipocalin family. In this work, we used Fourier transform infrared spectroscopy and molecular dynamics simulations to investigate the effect of temperature on the structural stability and conformational dynamics of the mutant bOBP. The spectroscopic and molecular simulation data pointed out that the hydrophobic regions of the protein matrix appear to be an important factor for the protein stability and integrity. In addition, it was also found that the mutant bOBP is significantly stabilized by the binding of the ligand, which may have an impact on the biological function of bOBP. The obtained results will allow for a better use of this protein as probe for the design of advanced protein‐based biosensors for the detection of compounds used in the fabrication of explosive powders. Proteins 2008. © 2008 Wiley‐Liss, Inc.