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Letter

Contribution of Omega-3 Fatty Acids to the Thermodynamics of Membrane Protein Solvation

Supporting Info

Alan Grossfield,*^† Scott E. Feller,^‡ and Michael C. Pitman^†

IBM T. J. Watson Research Center, 1101 Kitchawan Rd., P.O. Box 218, Yorktown Heights, New York 10598, and Department of Chemistry, Wabash College, 301 West Wabash Avenue, Crawfordsville, Indiana 47933

J. Phys. Chem. B, 2006, 110 (18), pp 8907–8909

DOI: 10.1021/jp060405r

Publication Date (Web): April 18, 2006

Corresponding author. E-mail: agrossf@us.ibm.com

†

IBM.

‡

Wabash College.

Abstract

Recent NMR experiments and molecular dynamics simulations have indicated that rhodopsin is preferentially solvated by omega-3 fatty acids compared to saturated chains. However, to date no physical theory has been advanced to explain this phenomenon. The present work presents a novel thermodynamic explanation for this preferential solvation based on statistical analysis of 26 100 ns all-atom molecular dynamics simulations of rhodopsin in membranes rich in polyunsaturated chains. The results indicate that the preferential solvation by omega-3 chains is entropically driven; all chains experience an entropic penalty when associating with the protein, but the penalty is significantly larger for saturated chains.

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History

Published In Issue May 11, 2006
Received January 19, 2006
Revised March 20, 2006

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Letter

Contribution of Omega-3 Fatty Acids to the Thermodynamics of Membrane Protein Solvation

Abstract

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SciFinder Links

History

Recommend & Share

Related Content

Role of Cholesterol and Polyunsaturated Chains in Lipid−Protein Interactions: Molecular Dynamics Simulation of Rhodopsin in a Realistic Membrane Environment

Describing Protein Folding Kinetics by Molecular Dynamics Simulations. 1. Theory

Thermal Denaturing of Mutant Lysozyme with Both the OPLSAA and the CHARMM Force Fields

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