-
1
-
-
7044241302
-
How lipids affect the activities of integral membrane proteins
-
Lee A.G. How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta 1666 (2004) 62-87
-
(2004)
Biochim Biophys Acta
, vol.1666
, pp. 62-87
-
-
Lee, A.G.1
-
2
-
-
33745041479
-
Roles of bilayer material properties in function and distribution of membrane proteins
-
McIntosh T.J., and Simon S.A. Roles of bilayer material properties in function and distribution of membrane proteins. Annu Rev Biophys Biomol Struct 35 (2006) 177-198
-
(2006)
Annu Rev Biophys Biomol Struct
, vol.35
, pp. 177-198
-
-
McIntosh, T.J.1
Simon, S.A.2
-
3
-
-
0242659352
-
Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring
-
de Planque M.R.R., and Killian J.A. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol Membr Biol 20 (2003) 271-284
-
(2003)
Mol Membr Biol
, vol.20
, pp. 271-284
-
-
de Planque, M.R.R.1
Killian, J.A.2
-
4
-
-
16344390562
-
Properties of integral membrane protein structures: derivation of an implicit membrane potential
-
Ulmschneider M.B., Sansom M.S.P., and Di Nola A. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins 59 (2005) 252-265
-
(2005)
Proteins
, vol.59
, pp. 252-265
-
-
Ulmschneider, M.B.1
Sansom, M.S.P.2
Di Nola, A.3
-
5
-
-
11244346029
-
Molecular dynamics simulation of transmembrane polypeptide orientational fluctuations
-
Goodyear D.J., Sharpe S., Grant C.W., and Morrow M.R. Molecular dynamics simulation of transmembrane polypeptide orientational fluctuations. Biophys J 88 (2005) 105-117
-
(2005)
Biophys J
, vol.88
, pp. 105-117
-
-
Goodyear, D.J.1
Sharpe, S.2
Grant, C.W.3
Morrow, M.R.4
-
6
-
-
0037133485
-
Hydrophobic matching mechanism investigated by molecular dynamics simulations
-
Petrache H.I., Zuckerman D.M., Sachs J.N., Killian J.A., Koeppe II R.E., and Woolf T.B. Hydrophobic matching mechanism investigated by molecular dynamics simulations. Langmuir 18 (2002) 1340-1351
-
(2002)
Langmuir
, vol.18
, pp. 1340-1351
-
-
Petrache, H.I.1
Zuckerman, D.M.2
Sachs, J.N.3
Killian, J.A.4
Koeppe II, R.E.5
Woolf, T.B.6
-
7
-
-
33646198955
-
Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch
-
The authors present an extensive simulation study in which they investigate different consequences of both positive and negative mismatch by varying the hydrophobic length of KALP peptides and the bilayer thickness. The results enable comparison with various experimental results on similar systems.
-
Kandasamy S.K., and Larson R.G. Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys J 90 (2006) 2326-2343. The authors present an extensive simulation study in which they investigate different consequences of both positive and negative mismatch by varying the hydrophobic length of KALP peptides and the bilayer thickness. The results enable comparison with various experimental results on similar systems.
-
(2006)
Biophys J
, vol.90
, pp. 2326-2343
-
-
Kandasamy, S.K.1
Larson, R.G.2
-
8
-
-
0033783447
-
31P solid-state NMR spectroscopy investigation
-
31P solid-state NMR spectroscopy investigation. Biochemistry 39 (2000) 13106-13114
-
(2000)
Biochemistry
, vol.39
, pp. 13106-13114
-
-
Harzer, U.1
Bechinger, B.2
-
9
-
-
8344287531
-
Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain
-
Spruijt R.B., Wolfs C.J., and Hemminga M.A. Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain. Biochemistry 43 (2004) 13972-13980
-
(2004)
Biochemistry
, vol.43
, pp. 13972-13980
-
-
Spruijt, R.B.1
Wolfs, C.J.2
Hemminga, M.A.3
-
10
-
-
20444366208
-
Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch
-
The authors determined the tilt angles of the transmembrane helix of VpU in lipid bilayers by solid-state NMR experiments. Their results show that the tilt angle increases with positive mismatch to as much as 51° in the thinnest bilayers, indicating that, in this system, the changes in tilt angle fully compensate for hydrophobic mismatch.
-
Park S.H., and Opella S.J. Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch. J Mol Biol 350 (2005) 310-318. The authors determined the tilt angles of the transmembrane helix of VpU in lipid bilayers by solid-state NMR experiments. Their results show that the tilt angle increases with positive mismatch to as much as 51° in the thinnest bilayers, indicating that, in this system, the changes in tilt angle fully compensate for hydrophobic mismatch.
-
(2005)
J Mol Biol
, vol.350
, pp. 310-318
-
-
Park, S.H.1
Opella, S.J.2
-
12
-
-
12344266698
-
2H NMR study
-
This study reports a comparison of the tilt and rotation angles of peptides with different flanking residues and different composition of the transmembrane segment. Small but highly systematic adaptations of tilt angles were found for all peptides, but the direction of tilt was insensitive to mismatch and seemed to be determined mainly by the nature of the flanking residues.
-
2H NMR study. Biochemistry 44 (2005) 1004-1012. This study reports a comparison of the tilt and rotation angles of peptides with different flanking residues and different composition of the transmembrane segment. Small but highly systematic adaptations of tilt angles were found for all peptides, but the direction of tilt was insensitive to mismatch and seemed to be determined mainly by the nature of the flanking residues.
-
(2005)
Biochemistry
, vol.44
, pp. 1004-1012
-
-
Özdirekcan, S.1
Rijkers, D.T.S.2
Killian, J.A.3
-
13
-
-
21244431672
-
Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins
-
This study focuses on the importance of the cross-sectional diameter of membrane proteins to protein-lipid interactions. The simulations showed that small peptides have a higher tendency to tilt, whereas larger proteins cause more adaptations of the lipids under mismatch conditions.
-
Venturoli M., Smit B., and Sperotto M.M. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins. Biophys J 88 (2005) 1778-1798. This study focuses on the importance of the cross-sectional diameter of membrane proteins to protein-lipid interactions. The simulations showed that small peptides have a higher tendency to tilt, whereas larger proteins cause more adaptations of the lipids under mismatch conditions.
-
(2005)
Biophys J
, vol.88
, pp. 1778-1798
-
-
Venturoli, M.1
Smit, B.2
Sperotto, M.M.3
-
14
-
-
0033522486
-
Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length
-
Ren J., Lew S., Wang J., and London E. Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length. Biochemistry 38 (1999) 5905-5912
-
(1999)
Biochemistry
, vol.38
, pp. 5905-5912
-
-
Ren, J.1
Lew, S.2
Wang, J.3
London, E.4
-
15
-
-
0035899991
-
Self-association of model transmembrane alpha-helices is modulated by lipid structure
-
Mall S., Broadbridge R., Sharma R.P., East J.M., and Lee A.G. Self-association of model transmembrane alpha-helices is modulated by lipid structure. Biochemistry 40 (2001) 12379-12386
-
(2001)
Biochemistry
, vol.40
, pp. 12379-12386
-
-
Mall, S.1
Broadbridge, R.2
Sharma, R.P.3
East, J.M.4
Lee, A.G.5
-
16
-
-
28244458040
-
Self-association of transmembrane α-helices in model membranes: importance of helix orientation and role of hydrophobic mismatch
-
The authors show that helices without an apparent recognition motif form antiparallel dimers. Modelling was used to show that dipole-dipole interactions are responsible for the favourable packing of antiparallel helices.
-
Sparr E., Ash W.L., Nazarov P.V., Rijkers D.T.S., Hemminga M.A., Tieleman D.P., and Killian J.A. Self-association of transmembrane α-helices in model membranes: importance of helix orientation and role of hydrophobic mismatch. J Biol Chem 280 (2005) 39324-39331. The authors show that helices without an apparent recognition motif form antiparallel dimers. Modelling was used to show that dipole-dipole interactions are responsible for the favourable packing of antiparallel helices.
-
(2005)
J Biol Chem
, vol.280
, pp. 39324-39331
-
-
Sparr, E.1
Ash, W.L.2
Nazarov, P.V.3
Rijkers, D.T.S.4
Hemminga, M.A.5
Tieleman, D.P.6
Killian, J.A.7
-
17
-
-
33644849922
-
Measurement of thermodynamic parameters for hydrophobic mismatch 1: self-association of a transmembrane helix
-
Using fluorescence resonance energy transfer, the authors obtained, for the first time, a complete set of thermodynamic parameters for the formation of antiparallel dimers by an inert hydrophobic model transmembrane helix in bilayers with different thickness.
-
Yano Y., and Matsuzaki K. Measurement of thermodynamic parameters for hydrophobic mismatch 1: self-association of a transmembrane helix. Biochemistry 45 (2006) 3370-3378. Using fluorescence resonance energy transfer, the authors obtained, for the first time, a complete set of thermodynamic parameters for the formation of antiparallel dimers by an inert hydrophobic model transmembrane helix in bilayers with different thickness.
-
(2006)
Biochemistry
, vol.45
, pp. 3370-3378
-
-
Yano, Y.1
Matsuzaki, K.2
-
19
-
-
0030932407
-
A transmembrane helix dimer: structure and implications
-
MacKenzie K.R., Prestegard J.H., and Engelman D.M. A transmembrane helix dimer: structure and implications. Science 276 (1997) 131-133
-
(1997)
Science
, vol.276
, pp. 131-133
-
-
MacKenzie, K.R.1
Prestegard, J.H.2
Engelman, D.M.3
-
20
-
-
33744965940
-
Evidence for assembly of small multidrug resistance proteins by a "two-faced" transmembrane helix
-
The authors studied helix-helix association using synthetic peptides that correspond to transmembrane helices of drug/proton antiporters that must oligomerize to function. The results suggest that one of the helices has two recognition surfaces, which are involved in folding and oligomerization of the protein.
-
Rath A., Melnyk R.A., and Deber C.M. Evidence for assembly of small multidrug resistance proteins by a "two-faced" transmembrane helix. J Biol Chem 281 (2006) 15546-15553. The authors studied helix-helix association using synthetic peptides that correspond to transmembrane helices of drug/proton antiporters that must oligomerize to function. The results suggest that one of the helices has two recognition surfaces, which are involved in folding and oligomerization of the protein.
-
(2006)
J Biol Chem
, vol.281
, pp. 15546-15553
-
-
Rath, A.1
Melnyk, R.A.2
Deber, C.M.3
-
21
-
-
0035942298
-
Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation
-
de Planque M.R.R., Goormaghtigh E., Greathouse D.V., Koeppe R.E., Kruijtzer J.A.W., Liskamp R.M.J., de Kruijff B., and Killian J.A. Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry 40 (2001) 5000-5010
-
(2001)
Biochemistry
, vol.40
, pp. 5000-5010
-
-
de Planque, M.R.R.1
Goormaghtigh, E.2
Greathouse, D.V.3
Koeppe, R.E.4
Kruijtzer, J.A.W.5
Liskamp, R.M.J.6
de Kruijff, B.7
Killian, J.A.8
-
22
-
-
1842482773
-
Model systems, lipid rafts, and cell membranes
-
Simons K., and Vaz W.L. Model systems, lipid rafts, and cell membranes. Annu Rev Biophys Biomol Struct 33 (2004) 269-295
-
(2004)
Annu Rev Biophys Biomol Struct
, vol.33
, pp. 269-295
-
-
Simons, K.1
Vaz, W.L.2
-
23
-
-
0029165107
-
An investigation of the role of transmembrane domains in Golgi protein retention
-
Munro S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J 14 (1995) 4695-4704
-
(1995)
EMBO J
, vol.14
, pp. 4695-4704
-
-
Munro, S.1
-
24
-
-
0037125228
-
Influence of hydrophobic mismatch and palmitoylation on the partitioning of transmembrane α-helical peptides into detergent resistant domains
-
van Duyl B., Rijkers D.T.S., de Kruijff B., and Killian J.A. Influence of hydrophobic mismatch and palmitoylation on the partitioning of transmembrane α-helical peptides into detergent resistant domains. FEBS Lett 523 (2002) 79-84
-
(2002)
FEBS Lett
, vol.523
, pp. 79-84
-
-
van Duyl, B.1
Rijkers, D.T.S.2
de Kruijff, B.3
Killian, J.A.4
-
25
-
-
23244449276
-
Transbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy
-
Vidal A., and McIntosh T.J. Transbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy. Biophys J 89 (2005) 1102-1108
-
(2005)
Biophys J
, vol.89
, pp. 1102-1108
-
-
Vidal, A.1
McIntosh, T.J.2
-
26
-
-
0142063411
-
Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: extension of quenching analysis to account for the effects of domain size and domain boundaries
-
Fastenberg M.E., Shogomori H., Xu X., Brown D.A., and London E. Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: extension of quenching analysis to account for the effects of domain size and domain boundaries. Biochemistry 42 (2003) 12376-12390
-
(2003)
Biochemistry
, vol.42
, pp. 12376-12390
-
-
Fastenberg, M.E.1
Shogomori, H.2
Xu, X.3
Brown, D.A.4
London, E.5
-
27
-
-
0021474573
-
Mattress model of lipid-protein interactions in membranes
-
Mouritsen O.G., and Bloom M. Mattress model of lipid-protein interactions in membranes. Biophys J 46 (1984) 141-153
-
(1984)
Biophys J
, vol.46
, pp. 141-153
-
-
Mouritsen, O.G.1
Bloom, M.2
-
29
-
-
12244255728
-
Hydrophobic mismatch between helices and lipid bilayers
-
Weiss T.M., van der Wel P., Killian J.A., Koeppe II R.E., and Huang H. Hydrophobic mismatch between helices and lipid bilayers. Biophys J 84 (2003) 379-385
-
(2003)
Biophys J
, vol.84
, pp. 379-385
-
-
Weiss, T.M.1
van der Wel, P.2
Killian, J.A.3
Koeppe II, R.E.4
Huang, H.5
-
30
-
-
0033597858
-
Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides
-
de Planque M.R.R., Kruijtzer J.A.W., Liskamp R.M.J., Marsh D., Greathouse D.V., Koeppe II R.E., de Kruijff B., and Killian J.A. Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides. J Biol Chem 274 (1999) 20839-20846
-
(1999)
J Biol Chem
, vol.274
, pp. 20839-20846
-
-
de Planque, M.R.R.1
Kruijtzer, J.A.W.2
Liskamp, R.M.J.3
Marsh, D.4
Greathouse, D.V.5
Koeppe II, R.E.6
de Kruijff, B.7
Killian, J.A.8
-
31
-
-
0037062590
-
Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides
-
Strandberg E., Morein S., Rijkers D.T.S., van der Wel P.C.A., Liskamp R.M.J., and Killian J.A. Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry 41 (2002) 7190-7198
-
(2002)
Biochemistry
, vol.41
, pp. 7190-7198
-
-
Strandberg, E.1
Morein, S.2
Rijkers, D.T.S.3
van der Wel, P.C.A.4
Liskamp, R.M.J.5
Killian, J.A.6
-
32
-
-
33646143773
-
Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion
-
Siegel D.P., Cherezov V., Greathouse D.V., Koeppe II R.E., Killian J.A., and Caffrey M. Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion. Biophys J 90 (2006) 200-211
-
(2006)
Biophys J
, vol.90
, pp. 200-211
-
-
Siegel, D.P.1
Cherezov, V.2
Greathouse, D.V.3
Koeppe II, R.E.4
Killian, J.A.5
Caffrey, M.6
-
33
-
-
6944226446
-
De novo design of conformationally flexible transmembrane peptides driving membrane fusion
-
Hofmann M.W., Weise K., Ollesch J., Agrawal P., Stalz H., Stelzer W., Hulsbergen F., de Groot H., Gerwert K., Reed J., and Langosch D. De novo design of conformationally flexible transmembrane peptides driving membrane fusion. Proc Natl Acad Sci USA 101 (2004) 14776-14781
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 14776-14781
-
-
Hofmann, M.W.1
Weise, K.2
Ollesch, J.3
Agrawal, P.4
Stalz, H.5
Stelzer, W.6
Hulsbergen, F.7
de Groot, H.8
Gerwert, K.9
Reed, J.10
Langosch, D.11
-
34
-
-
7244251137
-
Photocrosslinking analysis of preferential interactions between a transmembrane peptide and matching lipids
-
A new method is presented for determining preferential interactions between proteins and lipids.
-
Ridder A.N.J.A., Spelbrink R.E.J., Demmers J.A.A., Rijkers D.T.S., Liskamp R.M.J., Brunner J., Heck A.J.R., de Kruijff B., and Killian J.A. Photocrosslinking analysis of preferential interactions between a transmembrane peptide and matching lipids. Biochemistry 43 (2004) 4482-4489. A new method is presented for determining preferential interactions between proteins and lipids.
-
(2004)
Biochemistry
, vol.43
, pp. 4482-4489
-
-
Ridder, A.N.J.A.1
Spelbrink, R.E.J.2
Demmers, J.A.A.3
Rijkers, D.T.S.4
Liskamp, R.M.J.5
Brunner, J.6
Heck, A.J.R.7
de Kruijff, B.8
Killian, J.A.9
-
35
-
-
0032512417
-
Hydrophobic mismatch and the incorporation of peptides in lipid bilayers: a possible mechanism for retention in the Golgi
-
Webb R.J., East J.M., Sharma R.P., and Lee A.G. Hydrophobic mismatch and the incorporation of peptides in lipid bilayers: a possible mechanism for retention in the Golgi. Biochemistry 37 (1998) 673-679
-
(1998)
Biochemistry
, vol.37
, pp. 673-679
-
-
Webb, R.J.1
East, J.M.2
Sharma, R.P.3
Lee, A.G.4
-
36
-
-
0041589300
-
Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
-
Kol M.A., van Dalen A., de Kroon A.I.P.M., and de Kruijff B. Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane. J Biol Chem 278 (2003) 24586-24593
-
(2003)
J Biol Chem
, vol.278
, pp. 24586-24593
-
-
Kol, M.A.1
van Dalen, A.2
de Kroon, A.I.P.M.3
de Kruijff, B.4
-
37
-
-
16644377766
-
Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers
-
Liu F., Lewis R.N., Hodges R.S., and McElhaney R.N. Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine bilayers. Biophys J 87 (2004) 2470-2482
-
(2004)
Biophys J
, vol.87
, pp. 2470-2482
-
-
Liu, F.1
Lewis, R.N.2
Hodges, R.S.3
McElhaney, R.N.4
-
38
-
-
0038694994
-
Snorkeling of lysine side chains in transmembrane helices: how easy can it get?
-
Strandberg E., and Killian J.A. Snorkeling of lysine side chains in transmembrane helices: how easy can it get?. FEBS Lett 544 (2003) 69-73
-
(2003)
FEBS Lett
, vol.544
, pp. 69-73
-
-
Strandberg, E.1
Killian, J.A.2
-
39
-
-
0037881905
-
Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic mismatch effects in peptide-lipid interactions
-
de Planque M.R.R., Demmers J.A.A., Bonev B.B., Koeppe II R.E., Greathouse D.V., Separovic F., Watts A., and Killian J.A. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic mismatch effects in peptide-lipid interactions. Biochemistry 42 (2003) 5341-5348
-
(2003)
Biochemistry
, vol.42
, pp. 5341-5348
-
-
de Planque, M.R.R.1
Demmers, J.A.A.2
Bonev, B.B.3
Koeppe II, R.E.4
Greathouse, D.V.5
Separovic, F.6
Watts, A.7
Killian, J.A.8
-
40
-
-
0033609498
-
The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane
-
Braun P., and Von Heijne G. The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 38 (1999) 9778-9782
-
(1999)
Biochemistry
, vol.38
, pp. 9778-9782
-
-
Braun, P.1
Von Heijne, G.2
-
41
-
-
0036284109
-
Organization of model helical peptides in lipid bilayers: insight into the behavior of single-span protein transmembrane domains
-
Sharpe S., Barber K.R., Grant C.W.M., Goodyear D., and Morrow M.R. Organization of model helical peptides in lipid bilayers: insight into the behavior of single-span protein transmembrane domains. Biophys J 83 (2002) 345-358
-
(2002)
Biophys J
, vol.83
, pp. 345-358
-
-
Sharpe, S.1
Barber, K.R.2
Grant, C.W.M.3
Goodyear, D.4
Morrow, M.R.5
-
43
-
-
0041320842
-
The distribution of lipid attached spin probes in bilayers: application to membrane protein topology
-
Vogel A., Scheidt H.A., and Huster D. The distribution of lipid attached spin probes in bilayers: application to membrane protein topology. Biophys J 85 (2003) 1691-1701
-
(2003)
Biophys J
, vol.85
, pp. 1691-1701
-
-
Vogel, A.1
Scheidt, H.A.2
Huster, D.3
-
44
-
-
18244390978
-
A ruler for determining the position of proteins in membranes
-
The authors used EPR to determine the relaxation gradient of oxygen in lipid bilayers by attaching nitroxide probes to WALP peptides. The results provide a calibrated ruler for determining the membrane depth of residues in transmembrane and surface-bound proteins.
-
Nielsen R.D., Che K., Gelb M.H., and Robinson B.H. A ruler for determining the position of proteins in membranes. J Am Chem Soc 127 (2005) 6430-6442. The authors used EPR to determine the relaxation gradient of oxygen in lipid bilayers by attaching nitroxide probes to WALP peptides. The results provide a calibrated ruler for determining the membrane depth of residues in transmembrane and surface-bound proteins.
-
(2005)
J Am Chem Soc
, vol.127
, pp. 6430-6442
-
-
Nielsen, R.D.1
Che, K.2
Gelb, M.H.3
Robinson, B.H.4
-
45
-
-
19944428721
-
Probing membrane protein orientation and structure under fast magic-angle-spinning solid-state NMR
-
Andronesi O.C., Pfeifer J.R., Al-Momani L., Özdirekcan S., Rijkers D.T.S., Angerstein B., Luca S., Koert U., Killian J.A., and Baldus M. Probing membrane protein orientation and structure under fast magic-angle-spinning solid-state NMR. J Biomol NMR 30 (2004) 253-265
-
(2004)
J Biomol NMR
, vol.30
, pp. 253-265
-
-
Andronesi, O.C.1
Pfeifer, J.R.2
Al-Momani, L.3
Özdirekcan, S.4
Rijkers, D.T.S.5
Angerstein, B.6
Luca, S.7
Koert, U.8
Killian, J.A.9
Baldus, M.10
-
46
-
-
9644273777
-
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes
-
Lemaitre V., de Planque M.R., Howes A.P., Smith M.E., Dupree R., and Watts A. Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes. J Am Chem Soc 126 (2004) 15320-15321
-
(2004)
J Am Chem Soc
, vol.126
, pp. 15320-15321
-
-
Lemaitre, V.1
de Planque, M.R.2
Howes, A.P.3
Smith, M.E.4
Dupree, R.5
Watts, A.6
-
47
-
-
9744250110
-
The strength of integration of a transmembrane α-helical peptide in a lipid bilayer as determined by dynamic atomic force spectroscopy
-
The authors determined, for the first time, the strength of integration of single peptides in lipid bilayers using a gold-coated atomic force microscope tip and cysteine-labelled WALP peptides. The peptides were found to be very stably integrated into the bilayer. The authors concluded that the bilayer interface region plays an important role in stably anchoring transmembrane proteins within membranes.
-
Ganchev D.N., Snel M.M.E., Killian J.A., Rijkers D.T.S., and de Kruijff B. The strength of integration of a transmembrane α-helical peptide in a lipid bilayer as determined by dynamic atomic force spectroscopy. Biochemistry 43 (2004) 14987-14993. The authors determined, for the first time, the strength of integration of single peptides in lipid bilayers using a gold-coated atomic force microscope tip and cysteine-labelled WALP peptides. The peptides were found to be very stably integrated into the bilayer. The authors concluded that the bilayer interface region plays an important role in stably anchoring transmembrane proteins within membranes.
-
(2004)
Biochemistry
, vol.43
, pp. 14987-14993
-
-
Ganchev, D.N.1
Snel, M.M.E.2
Killian, J.A.3
Rijkers, D.T.S.4
de Kruijff, B.5
-
48
-
-
0034616309
-
Unfolding pathways of individual bacteriorhodopsins
-
Oesterhelt F., Oesterhelt D., Pfeiffer M., Engel A., Gaub H.E., and Müller D.J. Unfolding pathways of individual bacteriorhodopsins. Science 288 (2000) 143-146
-
(2000)
Science
, vol.288
, pp. 143-146
-
-
Oesterhelt, F.1
Oesterhelt, D.2
Pfeiffer, M.3
Engel, A.4
Gaub, H.E.5
Müller, D.J.6
-
49
-
-
27744527489
-
Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations
-
Contera S.A., Lemaitre V., de Planque M.R., Watts A., and Ryan J.F. Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations. Biophys J 89 (2005) 3129-3140
-
(2005)
Biophys J
, vol.89
, pp. 3129-3140
-
-
Contera, S.A.1
Lemaitre, V.2
de Planque, M.R.3
Watts, A.4
Ryan, J.F.5
-
50
-
-
18744403982
-
Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
-
The authors explored the mechanism of membrane insertion of different model peptides by replica-exchange molecular dynamics. Starting with fully extended peptides, they observed that the peptides first become localized at the membrane-solvent interface, where they form helical secondary structure, and then insert into the membrane.
-
Im W., and Brooks III C.L. Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc Natl Acad Sci USA 102 (2005) 6771-6776. The authors explored the mechanism of membrane insertion of different model peptides by replica-exchange molecular dynamics. Starting with fully extended peptides, they observed that the peptides first become localized at the membrane-solvent interface, where they form helical secondary structure, and then insert into the membrane.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 6771-6776
-
-
Im, W.1
Brooks III, C.L.2
-
51
-
-
18844362955
-
Folding is not required for bilayer insertion: replica exchange simulations of an alpha-helical peptide with an explicit lipid bilayer
-
The authors studied the interactions of a WALP peptide with an explicitly represented lipid bilayer. They observed spontaneous insertion of the peptide into the bilayer and subsequent folding into a transbilayer α helix. This pathway disagrees with the dominant conceptual model of a surface-bound helix as an intermediate for the insertion of α-helical peptides into lipid bilayers.
-
Nymeyer H., Woolf T.B., and Garcia A.E. Folding is not required for bilayer insertion: replica exchange simulations of an alpha-helical peptide with an explicit lipid bilayer. Proteins 59 (2005) 783-790. The authors studied the interactions of a WALP peptide with an explicitly represented lipid bilayer. They observed spontaneous insertion of the peptide into the bilayer and subsequent folding into a transbilayer α helix. This pathway disagrees with the dominant conceptual model of a surface-bound helix as an intermediate for the insertion of α-helical peptides into lipid bilayers.
-
(2005)
Proteins
, vol.59
, pp. 783-790
-
-
Nymeyer, H.1
Woolf, T.B.2
Garcia, A.E.3
-
52
-
-
13444262028
-
Recognition of transmembrane helices by the endoplasmic reticulum translocon
-
The authors determined basic features of the code by which the translocon decides whether a membrane protein inserts into the membrane or not. They developed a 'biological' hydrophobicity scale, which corresponded well with biophysical hydrophobicity scales. The scale indicated that the protein interacts with lipids during translocon-mediated insertion.
-
Hessa T., Kim H., Bihlmaier K., Lundin C., Boekel J., Andersson H., Nilsson I., White S.H., and von Heijne G. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433 (2005) 377-381. The authors determined basic features of the code by which the translocon decides whether a membrane protein inserts into the membrane or not. They developed a 'biological' hydrophobicity scale, which corresponded well with biophysical hydrophobicity scales. The scale indicated that the protein interacts with lipids during translocon-mediated insertion.
-
(2005)
Nature
, vol.433
, pp. 377-381
-
-
Hessa, T.1
Kim, H.2
Bihlmaier, K.3
Lundin, C.4
Boekel, J.5
Andersson, H.6
Nilsson, I.7
White, S.H.8
von Heijne, G.9
|