Mutant bovine odorant-binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations

2008 ◽  
Vol 72 (2) ◽  
pp. 769-778 ◽  
Author(s):  
Anna Marabotti ◽  
Thierry Lefèvre ◽  
Maria Staiano ◽  
Roberta Crescenzo ◽  
Antonio Varriale ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Infrared Spectroscopy ◽  
Protein Stability ◽  
Molecular Dynamics Simulations ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Dynamics Simulations ◽  
Odorant Binding

Molecular dynamics simulations of palmitate entry into the hydrophobic pocket of the fatty acid binding protein

FEBS Letters ◽  
2007 ◽  
Vol 581 (6) ◽  
pp. 1243-1247 ◽  
Author(s):  
Yossi Tsfadia ◽  
Ran Friedman ◽  
Jonathan Kadmon ◽  
Anna Selzer ◽  
Esther Nachliel ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Fatty Acid ◽  
Molecular Dynamics Simulations ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Hydrophobic Pocket ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Dynamics Simulations

How does human odorant binding protein bind odorants? The case of aldehydes studied by molecular dynamics

2009 ◽  
Vol 12 (8) ◽  
pp. 905-910 ◽  
Author(s):  
Landry Charlier ◽  
Daniel Cabrol-Bass ◽  
Jérome Golebiowski
Keyword(s):  
Molecular Dynamics ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding

scholarly journals Brain fatty acid binding protein exhibits non-preferential and mutation-resistant binding towards fatty acids

2021 ◽  
Author(s):  
Iulia Bodnariuc ◽  
Stefan Lenz ◽  
Margaret Renaud-Young ◽  
Tanille Shandro ◽  
Hiroaki Ishida ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Molecular Dynamics Simulations ◽  
Nuclear Localization ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein ◽  
Dynamics Simulations

Members of the fatty acid binding protein (FABP) family function as intracellular transporters of long chain fatty acids and other hydrophobic molecules to different cellular compartments. Brain fatty acid binding protein (FABP7) exhibits ligand-directed differences in cellular transport behavior. For example, when FABP7 binds to docosahexaenoic acid (DHA), the complex relocates to the nucleus and influences transcriptional activity, whereas FABP7 bound with monosaturated fatty acids remain in the cytosol. We used a variety of biophysical techniques to enhance understanding of ligand-directed transport. Specifically, we examine how FABP7 binds to fatty acids, including saturated stearic acid (SA), monounsaturated oleic acid (OA), and polyunsaturated DHA. We find that at 37°C FABP7 has near equivalent binding affinities for the fatty acids, while at lower temperatures, FABP7 exhibits a preference for the unsaturated fatty acids. Therefore, nuclear localization of the FABP7-DHA complex cannot be explained by binding preferences. Using NMR spectroscopy and molecular dynamics simulations, we observe that DHA uniquely affects the portal region of FABP7, which could enhance the complex's nuclear localization. Mutations to purported critical binding residues (R126L and Y128F) have little effect on fatty acid binding, with molecular dynamics simulations revealing that the bound fatty acid can adopt binding poses that can accommodate the mutations.

scholarly journals Structural dynamics of an excited donor–acceptor complex from ultrafast polarized infrared spectroscopy, molecular dynamics simulations, and quantum chemical calculations

2019 ◽  
Vol 21 (22) ◽  
pp. 11797-11809 ◽  
Author(s):  
Christopher A. Rumble ◽  
Eric Vauthey
Keyword(s):  
Molecular Dynamics ◽  
Infrared Spectroscopy ◽  
Molecular Dynamics Simulations ◽  
Structural Dynamics ◽  
Quantum Chemical ◽  
Large Scale ◽  
Acceptor Complex ◽  
Polarized Infrared Spectroscopy ◽  
Donor Acceptor ◽  
Dynamics Simulations

Infrared anisotropy experiments and mixed quantum/classical computations demonstrate large scale reorientation following excitation of a donor/acceptor complex.

Sign in / Sign up

Export Citation Format

Share Document