268
M. Melicherčík et al.
brane peptides can dominate over hydrophobic matching effects in peptide–lipid interactions.
Biochemistry 42(18):5341–5348
42. Vander Wel PCA, Strandberg E, Killian JA, Koeppe II RE (2002) Geometry and intrinsic
tilt of a tryptophan-anchored transmembrane α-helix determined by
2
H-NMR. Biophys J
83(3):1479–1488
43. Belohorcová K, Davis JH, Woolf TB, Roux B (1997) Structure and dynamics of an amphiphilic peptide in a lipid bilayer: a molecular dynamics study. Biophys J 73(6):3039–3055
44. Maurits RR, de Planque JA, Kruijtzer W, Rob M, Liskamp J, Marsh D, Greathouse DV,
Koeppe II RE, de Kruijff B, Killian JA (1999) Different membrane anchoring positions
of tryptophan and lysine in synthetic transmembrane α-helical peptides. J Biol Chem
274(30):20839–20846
45. De Jesus AJ, Allen TW (2013) The role of tryptophan side chains in membrane protein anchoring and hydrophobic mismatch. Biochim Biophys Acta 1828(2):864–876
46. De Jesus AJ, Allen TW (2013) The determinants of hydrophobic mismatch response for
transmembrane helices. Biochim Biophys Acta 1828(2):851–863
47. Daily AE, Greathouse DV, van der Wel PCA, Koeppe II RE (2008) Helical distortion in
tryptophan- and lysine-anchored membrane-spanning α-helices as a function of hydrophobic
mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled
alanines method. Biophys J 94(2):480–491
48. Lewis RNAH, Zhang YP, Liu F, McElhaney RN (2002) Mechanisms of the interaction of
α-helical transmembrane peptides with phospholipid bilayers.Bioelectrochemistry 56(1–
2):135–140
49. Fares C, Qian J, Davis JH (2005) Magic angle spinning and static oriented sample NMR studies of the relaxation in the rotating frame of membrane peptides. J Chem Phys 122(19):Art.
No. 194908. doi:10.1063/1.1899645
50. Davis JH, Auger M, Hodges RS (1995) High resolution 1 H nuclear magnetic resonance of a
transmembrane peptide. Biophys J 69(5):1917–1932
51. Pan J, Tieleman DP, Nagle JF, Kučerka N, Tristram-Nagle S (2009) Alamethicin in lipid
bilayers: combined use of X-ray scattering and MD simulations. Biochim Biophys Acta
1788(6):1387–1397
52. Sani M-A, Whitwell TC, Separovic F (2012) Lipid composition regulates the conformation
and insertion of the antimicrobial peptide maculatin 1.1. Biochim Biophys Acta 1818(2):205–
211
53. Hoernke M, Schwieger C, Kerth A, Blume A (2012) Binding of cationic pentapeptides with
modified side chain lengths to negatively charged lipid membranes: complex interplay of
electrostatic and hydrophobic interactions. Biochim Biophys Acta 1818(7):1663–1672
54. Johansson ACV, Lindahl E (2006) Amino-acid solvation structure in transmembrane helices
from molecular dynamics simulations. Biophys J 91(12):4450–4463
55. Li LB, Vorobyov I, Allen TW (2012) The role of membrane thickness in charged protein–
lipid interactions. Biochim Biophys Acta 1818(2):135–145
56. Lewis BA, Engelman DM (1983) Lipid bilayer thickness varies linearly with acyl chainlength in fluid phosphatidylcholine vesicles. J Mol Biol 166(2):211–217
57. Lam KLH, Wang H, Siaw TA, Chapman MR, Waring AJ, Kindt JT, Lee KYC (2012) Mechanism of structural transformations induced by antimicrobial peptides in lipid membranes.
Biochim Biophys Acta 1818(2):194–204
58. MacCallum JL, Bennett WFD, Tieleman DP (2008) Distribution of amino acids in a lipid
bilayer from computer simulations. Biophys J 94(9):3393–3404
59. Yoo J, Cui Q (2008) Does arginine remain protonated in the lipid membrane? Insights from
microscopic pK a calculations. Biophys J: Biophys Lett 94(8):L61–L63. doi:10.1529/biophysj.107.122945
60. Kim T, Im W (2010) Revisiting hydrophobic mismatch with free energy simulation studies of
transmembrane helix tilt and rotation. Biophys J 99(1):175–183
M. Melicherčík et al.
brane peptides can dominate over hydrophobic matching effects in peptide–lipid interactions.
Biochemistry 42(18):5341–5348
42. Vander Wel PCA, Strandberg E, Killian JA, Koeppe II RE (2002) Geometry and intrinsic
tilt of a tryptophan-anchored transmembrane α-helix determined by
2
H-NMR. Biophys J
83(3):1479–1488
43. Belohorcová K, Davis JH, Woolf TB, Roux B (1997) Structure and dynamics of an amphiphilic peptide in a lipid bilayer: a molecular dynamics study. Biophys J 73(6):3039–3055
44. Maurits RR, de Planque JA, Kruijtzer W, Rob M, Liskamp J, Marsh D, Greathouse DV,
Koeppe II RE, de Kruijff B, Killian JA (1999) Different membrane anchoring positions
of tryptophan and lysine in synthetic transmembrane α-helical peptides. J Biol Chem
274(30):20839–20846
45. De Jesus AJ, Allen TW (2013) The role of tryptophan side chains in membrane protein anchoring and hydrophobic mismatch. Biochim Biophys Acta 1828(2):864–876
46. De Jesus AJ, Allen TW (2013) The determinants of hydrophobic mismatch response for
transmembrane helices. Biochim Biophys Acta 1828(2):851–863
47. Daily AE, Greathouse DV, van der Wel PCA, Koeppe II RE (2008) Helical distortion in
tryptophan- and lysine-anchored membrane-spanning α-helices as a function of hydrophobic
mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled
alanines method. Biophys J 94(2):480–491
48. Lewis RNAH, Zhang YP, Liu F, McElhaney RN (2002) Mechanisms of the interaction of
α-helical transmembrane peptides with phospholipid bilayers.Bioelectrochemistry 56(1–
2):135–140
49. Fares C, Qian J, Davis JH (2005) Magic angle spinning and static oriented sample NMR studies of the relaxation in the rotating frame of membrane peptides. J Chem Phys 122(19):Art.
No. 194908. doi:10.1063/1.1899645
50. Davis JH, Auger M, Hodges RS (1995) High resolution 1 H nuclear magnetic resonance of a
transmembrane peptide. Biophys J 69(5):1917–1932
51. Pan J, Tieleman DP, Nagle JF, Kučerka N, Tristram-Nagle S (2009) Alamethicin in lipid
bilayers: combined use of X-ray scattering and MD simulations. Biochim Biophys Acta
1788(6):1387–1397
52. Sani M-A, Whitwell TC, Separovic F (2012) Lipid composition regulates the conformation
and insertion of the antimicrobial peptide maculatin 1.1. Biochim Biophys Acta 1818(2):205–
211
53. Hoernke M, Schwieger C, Kerth A, Blume A (2012) Binding of cationic pentapeptides with
modified side chain lengths to negatively charged lipid membranes: complex interplay of
electrostatic and hydrophobic interactions. Biochim Biophys Acta 1818(7):1663–1672
54. Johansson ACV, Lindahl E (2006) Amino-acid solvation structure in transmembrane helices
from molecular dynamics simulations. Biophys J 91(12):4450–4463
55. Li LB, Vorobyov I, Allen TW (2012) The role of membrane thickness in charged protein–
lipid interactions. Biochim Biophys Acta 1818(2):135–145
56. Lewis BA, Engelman DM (1983) Lipid bilayer thickness varies linearly with acyl chainlength in fluid phosphatidylcholine vesicles. J Mol Biol 166(2):211–217
57. Lam KLH, Wang H, Siaw TA, Chapman MR, Waring AJ, Kindt JT, Lee KYC (2012) Mechanism of structural transformations induced by antimicrobial peptides in lipid membranes.
Biochim Biophys Acta 1818(2):194–204
58. MacCallum JL, Bennett WFD, Tieleman DP (2008) Distribution of amino acids in a lipid
bilayer from computer simulations. Biophys J 94(9):3393–3404
59. Yoo J, Cui Q (2008) Does arginine remain protonated in the lipid membrane? Insights from
microscopic pK a calculations. Biophys J: Biophys Lett 94(8):L61–L63. doi:10.1529/biophysj.107.122945
60. Kim T, Im W (2010) Revisiting hydrophobic mismatch with free energy simulation studies of
transmembrane helix tilt and rotation. Biophys J 99(1):175–183