title: Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers.
abstract: The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. Measurements of those transfer free energies will facilitate the identification of membrane protein sequences and aid in the understanding of how proteins interact with membranes during key biological events. We report the first water-to-bilayer transfer free energy scale (i.e., a "hydrophobicity scale") for the twenty natural amino acid side chains measured in the context of a native transmembrane protein and a phospholipid bilayer. Our measurements reveal parity for apolar side-chain contributions between soluble and membrane proteins and further demonstrate that an arginine side-chain placed near the middle of a lipid bilayer is accommodated with much less energetic cost than predicted by molecular dynamics simulations.
authors: Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
authors: C Preston
authors: CP
authors: Moon
authors: Karen G
authors: KG
authors: Fleming
references: Protein Sci. 2006 Jun;15(6):1318-33
references: 16731967
references: Proc Natl Acad Sci U S A. 2007 May 8;104(19):7893-8
references: 17483464
references: J Mol Biol. 2007 Jul 27;370(5):912-24
references: 17555765
references: J Gen Physiol. 2007 May;129(5):371-7
references: 17438118
references: Science. 2005 Mar 4;307(5714):1427
references: 15681341
references: J Mol Biol. 1982 May 5;157(1):105-32
references: 7108955
references: Cell. 2005 Nov 4;123(3):463-75
references: 16269337
references: J Gen Physiol. 2007 Aug;130(2):233-6
references: 17635960
references: Annu Rev Biophys Biomol Struct. 1999;28:319-65
references: 10410805
references: Nature. 2003 May 1;423(6935):33-41
references: 12721618
references: Nature. 2007 Dec 13;450(7172):1026-30
references: 18075582
references: J Biol Chem. 1997 Feb 7;272(6):3179-84
references: 9013551
references: Proc Natl Acad Sci U S A. 2010 Mar 2;107(9):4099-104
references: 20133664
references: Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):4943-8
references: 17360368
references: J Membr Biol. 2011 Jan;239(1-2):35-48
references: 21127848
references: J Am Chem Soc. 2007 Jul 4;129(26):8320-7
references: 17564441
references: Methods Enzymol. 2011;492:189-211
references: 21333792
references: Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15059-64
references: 16217012
references: Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4065-70
references: 14990786
references: Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6202-6
references: 1631109
references: J Biol Chem. 2008 Sep 26;283(39):26748-58
references: 18641391
references: Biochemistry. 1992 May 26;31(20):4901-7
references: 1591250
references: Biophys J. 2006 Oct 15;91(8):L75-7
references: 16891370
references: J Mol Biol. 2006 Mar 31;357(3):1009-25
references: 16473367
references: Nature. 2005 Jan 27;433(7024):377-81
references: 15674282
references: Biochemistry. 1996 Apr 23;35(16):5109-24
references: 8611495
references: Nature. 1999 Oct 14;401(6754):717-21
references: 10537112
references: Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2631-6
references: 17301243
references: Methods Cell Biol. 2008;84:295-325
references: 17964936
references: Science. 1978 Jun 2;200(4345):1012-8
references: 653353
references: Anal Biochem. 2000 Oct 15;285(2):235-45
references: 11017708
references: Biochemistry. 2008 Dec 2;47(48):12844-52
references: 18991402
references: Proc Natl Acad Sci U S A. 2008 May 20;105(20):7177-81
references: 18477697
references: Protein Sci. 2009 Dec;18(12):2624-8
references: 19785006
references: Biochim Biophys Acta. 2003 May 2;1612(1):1-40
references: 12729927
references: Nature. 1974 Mar 22;248(446):338-9
references: 4819639