410 related articles for article (PubMed ID: 23975773)
1. Analyzing the effects of hydrophobic mismatch on transmembrane α-helices using tryptophan fluorescence spectroscopy.
Caputo GA
Methods Mol Biol; 2013; 1063():95-116. PubMed ID: 23975773
[TBL] [Abstract][Full Text] [Related]
2. A fluorescence method to define transmembrane alpha-helices in membrane proteins: studies with bacterial diacylglycerol kinase.
Jittikoon J; East JM; Lee AG
Biochemistry; 2007 Sep; 46(38):10950-9. PubMed ID: 17722884
[TBL] [Abstract][Full Text] [Related]
3. Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylglycerol bilayers.
Liu F; Lewis RN; Hodges RS; McElhaney RN
Biochemistry; 2004 Mar; 43(12):3679-87. PubMed ID: 15035638
[TBL] [Abstract][Full Text] [Related]
4. The determinants of hydrophobic mismatch response for transmembrane helices.
de Jesus AJ; Allen TW
Biochim Biophys Acta; 2013 Feb; 1828(2):851-63. PubMed ID: 22995244
[TBL] [Abstract][Full Text] [Related]
5. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions.
de Planque MR; Bonev BB; Demmers JA; Greathouse DV; Koeppe RE; Separovic F; Watts A; Killian JA
Biochemistry; 2003 May; 42(18):5341-8. PubMed ID: 12731875
[TBL] [Abstract][Full Text] [Related]
6. Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration.
Ren J; Lew S; Wang Z; London E
Biochemistry; 1997 Aug; 36(33):10213-20. PubMed ID: 9254619
[TBL] [Abstract][Full Text] [Related]
7. Control of the transmembrane orientation and interhelical interactions within membranes by hydrophobic helix length.
Ren J; Lew S; Wang J; London E
Biochemistry; 1999 May; 38(18):5905-12. PubMed ID: 10231543
[TBL] [Abstract][Full Text] [Related]
8. Transmembrane helices of membrane proteins may flex to satisfy hydrophobic mismatch.
Yeagle PL; Bennett M; Lemaître V; Watts A
Biochim Biophys Acta; 2007 Mar; 1768(3):530-7. PubMed ID: 17223071
[TBL] [Abstract][Full Text] [Related]
9. Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.
Koehorst RB; Spruijt RB; Vergeldt FJ; Hemminga MA
Biophys J; 2004 Sep; 87(3):1445-55. PubMed ID: 15345527
[TBL] [Abstract][Full Text] [Related]
10. Position and ionization state of Asp in the core of membrane-inserted alpha helices control both the equilibrium between transmembrane and nontransmembrane helix topography and transmembrane helix positioning.
Caputo GA; London E
Biochemistry; 2004 Jul; 43(27):8794-806. PubMed ID: 15236588
[TBL] [Abstract][Full Text] [Related]
11. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring.
de Planque MR; Killian JA
Mol Membr Biol; 2003; 20(4):271-84. PubMed ID: 14578043
[TBL] [Abstract][Full Text] [Related]
12. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins.
Venturoli M; Smit B; Sperotto MM
Biophys J; 2005 Mar; 88(3):1778-98. PubMed ID: 15738466
[TBL] [Abstract][Full Text] [Related]
13. Analyzing transmembrane protein and hydrophobic helix topography by dual fluorescence quenching.
Caputo GA; London E
Methods Mol Biol; 2013; 974():279-95. PubMed ID: 23404281
[TBL] [Abstract][Full Text] [Related]
14. Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation.
de Planque MR; Goormaghtigh E; Greathouse DV; Koeppe RE; Kruijtzer JA; Liskamp RM; de Kruijff B; Killian JA
Biochemistry; 2001 Apr; 40(16):5000-10. PubMed ID: 11305916
[TBL] [Abstract][Full Text] [Related]
15. Revisiting hydrophobic mismatch with free energy simulation studies of transmembrane helix tilt and rotation.
Kim T; Im W
Biophys J; 2010 Jul; 99(1):175-83. PubMed ID: 20655845
[TBL] [Abstract][Full Text] [Related]
16. Potential of mean force analysis of the self-association of leucine-rich transmembrane α-helices: difference between atomistic and coarse-grained simulations.
Nishizawa M; Nishizawa K
J Chem Phys; 2014 Aug; 141(7):075101. PubMed ID: 25149815
[TBL] [Abstract][Full Text] [Related]
17. Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch.
Park SH; Opella SJ
J Mol Biol; 2005 Jul; 350(2):310-8. PubMed ID: 15936031
[TBL] [Abstract][Full Text] [Related]
18. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans.
Killian JA; Salemink I; de Planque MR; Lindblom G; Koeppe RE; Greathouse DV
Biochemistry; 1996 Jan; 35(3):1037-45. PubMed ID: 8547239
[TBL] [Abstract][Full Text] [Related]
19. Orientation and dynamics of transmembrane peptides: the power of simple models.
Holt A; Killian JA
Eur Biophys J; 2010 Mar; 39(4):609-21. PubMed ID: 20020122
[TBL] [Abstract][Full Text] [Related]
20. The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition.
Meijberg W; Booth PJ
J Mol Biol; 2002 Jun; 319(3):839-53. PubMed ID: 12054874
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
