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Volumn 47, Issue 32, 2008, Pages 8292-8300

The helical structure of surfactant peptide KL4 when bound to POPC: POPG lipid vesicles

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AMINES;

EID: 49449098835     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702551c     Document Type: Article
Times cited : (19)

References (71)
  • 2
    • 0036667738 scopus 로고    scopus 로고
    • Pulmonary surfactant: Phase behavior and function
    • Piknova, B., Schram, V., and Hall, S. B. (2002) Pulmonary surfactant: phase behavior and function. Curr. Opin. Struct. Biol. 12, 487-494.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 487-494
    • Piknova, B.1    Schram, V.2    Hall, S.B.3
  • 3
    • 0037180829 scopus 로고    scopus 로고
    • Mechanisms of disease: Hydrophobic surfactant proteins in lung function and disease
    • Whitsett, J. A., and Weaver, T. E. (2002) Mechanisms of disease: Hydrophobic surfactant proteins in lung function and disease. New Engl. J. Med. 347, 2141-2148.
    • (2002) New Engl. J. Med , vol.347 , pp. 2141-2148
    • Whitsett, J.A.1    Weaver, T.E.2
  • 4
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright, J. R. (2005) Immunoregulatory functions of surfactant proteins. Nature Rev. Immunol. 5, 58-68.
    • (2005) Nature Rev. Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 5
    • 33646555466 scopus 로고    scopus 로고
    • Protein-lipid interactions and surface activity in the pulmonary surfactant system
    • Serrano, A. G., and Perez-Gil, J. (2006) Protein-lipid interactions and surface activity in the pulmonary surfactant system. Chem. Phys. Lipids 141, 105-118.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 105-118
    • Serrano, A.G.1    Perez-Gil, J.2
  • 6
    • 0029096591 scopus 로고
    • Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice
    • Clark, J. C., Wert, S. E., Bachurski, C. J., Stahlman, M. T., Stripp, B. R., Weaver, T. E., and Whitsett, J. A. (1995) Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. U.S.A. 92, 7794-7798.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 7794-7798
    • Clark, J.C.1    Wert, S.E.2    Bachurski, C.J.3    Stahlman, M.T.4    Stripp, B.R.5    Weaver, T.E.6    Whitsett, J.A.7
  • 8
    • 0031897104 scopus 로고    scopus 로고
    • Lung surfactant and neonatal respiratory distress syndrome
    • Clements, J. A., and Avery, M. E. (1998) Lung surfactant and neonatal respiratory distress syndrome. Am. J. Respir. Crit. Care Med. 157, S59-66.
    • (1998) Am. J. Respir. Crit. Care Med , vol.157
    • Clements, J.A.1    Avery, M.E.2
  • 9
    • 0023874380 scopus 로고
    • Use of human surfactant low-molecular weight apoproteins in the reconstitution of surfactant biologic activity
    • Revak, S. D., Merritt, T. A., Degryse, E., Stefani, L., Courtney, M., Hallman, M., and Cochrane, C. G. (1988) Use of human surfactant low-molecular weight apoproteins in the reconstitution of surfactant biologic activity. J. Clin. Invest. 81, 826-833.
    • (1988) J. Clin. Invest , vol.81 , pp. 826-833
    • Revak, S.D.1    Merritt, T.A.2    Degryse, E.3    Stefani, L.4    Courtney, M.5    Hallman, M.6    Cochrane, C.G.7
  • 11
    • 23244441455 scopus 로고    scopus 로고
    • History of surfactant up to 1980
    • Obladen, M. (2005) History of surfactant up to 1980. Biol Neonate 87, 308-316.
    • (2005) Biol Neonate , vol.87 , pp. 308-316
    • Obladen, M.1
  • 13
    • 0030942158 scopus 로고    scopus 로고
    • Molecular structures and interactions of pulmonary surfactant components
    • Johansson, J., and Curstedt, T. (1997) Molecular structures and interactions of pulmonary surfactant components. Eur. J. Biochem. 244, 675-693.
    • (1997) Eur. J. Biochem , vol.244 , pp. 675-693
    • Johansson, J.1    Curstedt, T.2
  • 14
    • 0034744529 scopus 로고    scopus 로고
    • Function of surfactant proteins B and C
    • Weaver, T. E., and Conkright, J. J. (2001) Function of surfactant proteins B and C. Annu. Rev. Physiol. 63, 555-578.
    • (2001) Annu. Rev. Physiol , vol.63 , pp. 555-578
    • Weaver, T.E.1    Conkright, J.J.2
  • 15
    • 0034060802 scopus 로고    scopus 로고
    • Synthetic surfactants to treat neonatal lung disease
    • Robertson, B., Johansson, J., and Curstedt, T. (2000) Synthetic surfactants to treat neonatal lung disease. Mol. Med. Today 6, 119-124.
    • (2000) Mol. Med. Today , vol.6 , pp. 119-124
    • Robertson, B.1    Johansson, J.2    Curstedt, T.3
  • 16
    • 4143049017 scopus 로고    scopus 로고
    • Exogenous surfactant replacement in ARDS-one day, someday, or never?
    • Baudouin, S. V. (2004) Exogenous surfactant replacement in ARDS-one day, someday, or never? N. Engl. J. Med. 351, 853-855.
    • (2004) N. Engl. J. Med , vol.351 , pp. 853-855
    • Baudouin, S.V.1
  • 17
    • 12344251969 scopus 로고    scopus 로고
    • Simple, helical peptoid analogs of lung surfactant protein B
    • Seurynck, S. L., Patch, J. A., and Barron, A. E. (2005) Simple, helical peptoid analogs of lung surfactant protein B. Chem. Biol. 12, 77-88.
    • (2005) Chem. Biol , vol.12 , pp. 77-88
    • Seurynck, S.L.1    Patch, J.A.2    Barron, A.E.3
  • 18
    • 0026347862 scopus 로고
    • Pulmonary surfactant protein B (SP-B): Structure-function relationships
    • Cochrane, C. G., and Revak, S. D. (1991) Pulmonary surfactant protein B (SP-B): structure-function relationships. Science 254, 566-568.
    • (1991) Science , vol.254 , pp. 566-568
    • Cochrane, C.G.1    Revak, S.D.2
  • 22
    • 23244442451 scopus 로고    scopus 로고
    • A multicenter, randomized, controlled trial of lucinactant versus poractant alfa among very premature infants at high risk for respiratory distress syndrome
    • Sinha, S. K., Lacaze-Masmonteil, T., Soler, A. V. I., Wiswell, T. E., Gadzinowski, J., Hajdu, J., Bernstein, G., d'Agostino, R., and Dist, S. T. A. R. (2005) A multicenter, randomized, controlled trial of lucinactant versus poractant alfa among very premature infants at high risk for respiratory distress syndrome. Pediatrics 115, 1030-1038.
    • (2005) Pediatrics , vol.115 , pp. 1030-1038
    • Sinha, S.K.1    Lacaze-Masmonteil, T.2    Soler, A.V.I.3    Wiswell, T.E.4    Gadzinowski, J.5    Hajdu, J.6    Bernstein, G.7    d'Agostino, R.8    Dist, S.T.A.R.9
  • 23
    • 0028347631 scopus 로고
    • Protein-phospholipid interactions in pulmonary surfactant. The Parker B. Francis Lectureship
    • Cochrane, C. G., and Revak, S. D. (1994) Protein-phospholipid interactions in pulmonary surfactant. The Parker B. Francis Lectureship. Chest 105, 57S-62S.
    • (1994) Chest , vol.105
    • Cochrane, C.G.1    Revak, S.D.2
  • 25
    • 0026795207 scopus 로고
    • Secondary structure and orientation of the surfactant protein Sp-B in a lipid environment - a Fourier-transform infrared-spectroscopy study
    • Vandenbussche, G., Clercx, A., Clercx, M., Curstedt, T., Johansson, J., Jornvall, H., and Ruysschaert, J. M. (1992) Secondary structure and orientation of the surfactant protein Sp-B in a lipid environment - a Fourier-transform infrared-spectroscopy study. Biochemistry 31, 9169-9176.
    • (1992) Biochemistry , vol.31 , pp. 9169-9176
    • Vandenbussche, G.1    Clercx, A.2    Clercx, M.3    Curstedt, T.4    Johansson, J.5    Jornvall, H.6    Ruysschaert, J.M.7
  • 27
    • 0037343160 scopus 로고    scopus 로고
    • Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C
    • Wustneck, N., Wustneck, R., Perez-Gil, J., and Pison, U. (2003) Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C. Biophys. J. 84, 1940-1949.
    • (2003) Biophys. J , vol.84 , pp. 1940-1949
    • Wustneck, N.1    Wustneck, R.2    Perez-Gil, J.3    Pison, U.4
  • 29
    • 0042572532 scopus 로고    scopus 로고
    • 4K, a therapeutic agent for respiratory distress syndrome, in aqueous monolayers with phospholipids
    • 4K, a therapeutic agent for respiratory distress syndrome, in aqueous monolayers with phospholipids. Biochemistry 42, 9446-9452.
    • (2003) Biochemistry , vol.42 , pp. 9446-9452
    • Cai, P.1    Flach, C.R.2    Mendelsohn, R.3
  • 30
    • 33646694763 scopus 로고    scopus 로고
    • Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4
    • Saenz, A., Canadas, O., Bagatolli, L. A., Johnson, M. E., and Casals, C. (2006) Physical properties and surface activity of surfactant-like membranes containing the cationic and hydrophobic peptide KL4. FEBS J. 273, 2515-2527.
    • (2006) FEBS J , vol.273 , pp. 2515-2527
    • Saenz, A.1    Canadas, O.2    Bagatolli, L.A.3    Johnson, M.E.4    Casals, C.5
  • 31
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm, L. K., and Tatulian, S. A. (1997) Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 30, 365-429.
    • (1997) Q. Rev. Biophys , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 32
    • 49449117170 scopus 로고    scopus 로고
    • Coligan, J. E, Dunn, B. M, Speicher, D. W, and Wingfield, P. T, Eds, Chapter 26, John Wiley and Sons, Inc, Brooklyn, NY
    • Samuel-Landtiser, M., Zachariah, C., Williams, C. R., Edison, A. S., and Long, J. R. (2007) In Current Protocols in Protein Science (Coligan, J. E., Dunn, B. M., Speicher, D. W., and Wingfield, P. T., Eds.) Chapter 26, part 3, pp 1-49, John Wiley and Sons, Inc., Brooklyn, NY.
    • (2007) Current Protocols in Protein Science , Issue.PART 3 , pp. 1-49
    • Samuel-Landtiser, M.1    Zachariah, C.2    Williams, C.R.3    Edison, A.S.4    Long, J.R.5
  • 34
    • 0031188840 scopus 로고    scopus 로고
    • Determination of local structure in solid nucleic acids using double quantum nuclear magnetic resonance spectroscopy
    • Gregory, D. M., Mehta, M. A., Shiels, J. C., and Drobny, G. P. (1997) Determination of local structure in solid nucleic acids using double quantum nuclear magnetic resonance spectroscopy. J. Chem. Phys. 107, 28-42.
    • (1997) J. Chem. Phys , vol.107 , pp. 28-42
    • Gregory, D.M.1    Mehta, M.A.2    Shiels, J.C.3    Drobny, G.P.4
  • 35
    • 0001173761 scopus 로고    scopus 로고
    • Double-quantum filtering in magic-angle-spinning NMR spectroscopy applied to DNA oligomers
    • Gregory, D. M., Wolfe, G. M., Jarvie, T. P., Sheils, J. C., and Drobny, G. P. (1996) Double-quantum filtering in magic-angle-spinning NMR spectroscopy applied to DNA oligomers. Mol. Phys. 89, 1835-1849.
    • (1996) Mol. Phys , vol.89 , pp. 1835-1849
    • Gregory, D.M.1    Wolfe, G.M.2    Jarvie, T.P.3    Sheils, J.C.4    Drobny, G.P.5
  • 36
    • 0033568334 scopus 로고    scopus 로고
    • Determination of torsion angles in proteins and peptides using solid state NMR
    • Bower, P. V., Oyler, N., Mehta, M. A., Long, J. R., Stayton, P. S., and Drobny, G. P. (1999) Determination of torsion angles in proteins and peptides using solid state NMR. J. Am. Chem. Soc. 121, 8373-8375.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 8373-8375
    • Bower, P.V.1    Oyler, N.2    Mehta, M.A.3    Long, J.R.4    Stayton, P.S.5    Drobny, G.P.6
  • 37
    • 0000758857 scopus 로고
    • C-13 Chemical-shift and C-13-N-15 dipolar tensors for the peptide-bond in [1-C-13]glycyl[N-15]glycinehydrochloride monohydrate
    • Stark, R. E., Jelinski, L. W., Ruben, D. J., Torchia, D. A., and Griffin, R. G. (1983) C-13 Chemical-shift and C-13-N-15 dipolar tensors for the peptide-bond in [1-C-13]glycyl[N-15]glycinehydrochloride monohydrate. J. Magn. Reson. 55, 266-273.
    • (1983) J. Magn. Reson , vol.55 , pp. 266-273
    • Stark, R.E.1    Jelinski, L.W.2    Ruben, D.J.3    Torchia, D.A.4    Griffin, R.G.5
  • 38
    • 0000940338 scopus 로고
    • The carbonyl C-13 chemical-shift tensors of 5 peptides determined from N-15 dipole-coupled chemical-shift powder patterns
    • Oas, T. G., Hartzell, C. J., Mcmahon, T. J., Drobny, G. P., and Dahlquist, F. W. (1987) The carbonyl C-13 chemical-shift tensors of 5 peptides determined from N-15 dipole-coupled chemical-shift powder patterns. J. Am. Chem. Soc. 109, 5956-5962.
    • (1987) J. Am. Chem. Soc , vol.109 , pp. 5956-5962
    • Oas, T.G.1    Hartzell, C.J.2    Mcmahon, T.J.3    Drobny, G.P.4    Dahlquist, F.W.5
  • 39
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-Ray protein-structure refinement
    • Engh, R. A., and Huber, R. (1991) Accurate bond and angle parameters for X-Ray protein-structure refinement. Acta Crystallogr., Sect. A 47, 392-400.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 40
    • 0000387787 scopus 로고
    • Determination of the C-13 chemical-shift and N-14 electric-field gradient tensor orientations with respect to the molecular frame in a polypeptide
    • Teng, Q., Iqbal, M., and Cross, T. A. (1992) Determination of the C-13 chemical-shift and N-14 electric-field gradient tensor orientations with respect to the molecular frame in a polypeptide. J. Am. Chem. Soc. 114, 5312-5321.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 5312-5321
    • Teng, Q.1    Iqbal, M.2    Cross, T.A.3
  • 41
    • 0038026916 scopus 로고    scopus 로고
    • Analysis of local conformation of membrane-bound and polycrystalline peptides by two-dimensional slow-spinning rotor-synchronized MAS exchange spectroscopy
    • Gabrys, C. M., Yang, J., and Weliky, D. P. (2003) Analysis of local conformation of membrane-bound and polycrystalline peptides by two-dimensional slow-spinning rotor-synchronized MAS exchange spectroscopy. J. Biomol. NMR 26, 49-68.
    • (2003) J. Biomol. NMR , vol.26 , pp. 49-68
    • Gabrys, C.M.1    Yang, J.2    Weliky, D.P.3
  • 42
    • 0034571935 scopus 로고    scopus 로고
    • SIMPSON: A general simulation program for solid-state NMR spectroscopy
    • Bak, M., Rasmussen, J. T., and Nielsen, N. C. (2000) SIMPSON: A general simulation program for solid-state NMR spectroscopy. J. Magn. Reson. 147, 296-330.
    • (2000) J. Magn. Reson , vol.147 , pp. 296-330
    • Bak, M.1    Rasmussen, J.T.2    Nielsen, N.C.3
  • 43
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circulardichroism spectra using an unsupervised learning neural-network
    • Andrade, M. A., Chacon, P., Merelo, J. J., and Moran, F. (1993) Evaluation of secondary structure of proteins from UV circulardichroism spectra using an unsupervised learning neural-network. Protein Eng. 6, 383-390.
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 44
    • 0001115298 scopus 로고
    • Magic-angle C-13 NMR analysis of motion in solid glassy polymers
    • Schaefer, J., Stejskal, E. O., and Buchdahl, R. (1977) Magic-angle C-13 NMR analysis of motion in solid glassy polymers. Macromolecules 10, 384-405.
    • (1977) Macromolecules , vol.10 , pp. 384-405
    • Schaefer, J.1    Stejskal, E.O.2    Buchdahl, R.3
  • 45
    • 0035951086 scopus 로고    scopus 로고
    • Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR
    • Long, J. R., Shaw, W. J., Stayton, P. S., and Drobny, G. P. (2001) Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR. Biochemistry 40, 15451-15455.
    • (2001) Biochemistry , vol.40 , pp. 15451-15455
    • Long, J.R.1    Shaw, W.J.2    Stayton, P.S.3    Drobny, G.P.4
  • 46
    • 0034718060 scopus 로고    scopus 로고
    • A solid state NMR study of dynamics in a hydrated salivary peptide adsorbed to hydroxyapatite
    • Shaw, W. J., Long, J. R., Campbell, A. A., Stayton, P. S., and Drobny, G. P. (2000) A solid state NMR study of dynamics in a hydrated salivary peptide adsorbed to hydroxyapatite. J. Am. Chem. Soc. 122, 7118-7119.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 7118-7119
    • Shaw, W.J.1    Long, J.R.2    Campbell, A.A.3    Stayton, P.S.4    Drobny, G.P.5
  • 47
    • 0000842453 scopus 로고
    • Hydrogen-bonding effect on C-13 NMR chemical-shifts of L-alanine residue carbonyl carbons of peptides in the solid-state
    • Asakawa, N., Kuroki, S., Kurosu, H., Ando, I., Shoji, A., and Ozaki, T. (1992) Hydrogen-bonding effect on C-13 NMR chemical-shifts of L-alanine residue carbonyl carbons of peptides in the solid-state. J. Am. Chem. Soc. 114, 3261-3265.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 3261-3265
    • Asakawa, N.1    Kuroki, S.2    Kurosu, H.3    Ando, I.4    Shoji, A.5    Ozaki, T.6
  • 48
    • 0032579582 scopus 로고    scopus 로고
    • Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift
    • Ando, I., Kameda, T., Asakawa, N., Kuroki, S., and Kurosu, H. (1998) Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift. J. Mol. Struct. 441, 213-230.
    • (1998) J. Mol. Struct , vol.441 , pp. 213-230
    • Ando, I.1    Kameda, T.2    Asakawa, N.3    Kuroki, S.4    Kurosu, H.5
  • 49
    • 39549090438 scopus 로고    scopus 로고
    • Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy
    • Mehta, M. A., Eddy, M. T., McNeill, S. A., Mills, F. D., and Long, J. R. (2008) Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy. J. Am. Chem. Soc. 130, 2202-2212.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 2202-2212
    • Mehta, M.A.1    Eddy, M.T.2    McNeill, S.A.3    Mills, F.D.4    Long, J.R.5
  • 52
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin
    • Ramamoorthy, A., Thennarasu, S., Lee, D. K., Tan, A., and Maloy, L. (2006) Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys. J. 91, 206-216.
    • (2006) Biophys. J , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.4    Maloy, L.5
  • 53
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • Hwang, P. M., and Vogel, H. J. (1998) Structure-function relationships of antimicrobial peptides. Biochem. Cell Biol. 76, 235-246.
    • (1998) Biochem. Cell Biol , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 54
    • 0037960262 scopus 로고    scopus 로고
    • Direct comparison of membrane interactions of model peptides composed of only Leu and Lys residues
    • Epand, R. F., Lehrer, R. I., Waring, A., Wang, W., Maget-Dana, R., Lelievre, D., and Epand, R. M. (2003) Direct comparison of membrane interactions of model peptides composed of only Leu and Lys residues. Biopolymers 71, 2-16.
    • (2003) Biopolymers , vol.71 , pp. 2-16
    • Epand, R.F.1    Lehrer, R.I.2    Waring, A.3    Wang, W.4    Maget-Dana, R.5    Lelievre, D.6    Epand, R.M.7
  • 55
    • 0029797094 scopus 로고    scopus 로고
    • Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid-and bio-membranes
    • Kiyota, T., Lee, S., and Sugihara, G. (1996) Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid-and bio-membranes. Biochemistry 35, 13196-13204.
    • (1996) Biochemistry , vol.35 , pp. 13196-13204
    • Kiyota, T.1    Lee, S.2    Sugihara, G.3
  • 56
    • 0037062590 scopus 로고    scopus 로고
    • 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., Liskamp, R. M. J., van der Wel, P. C. A., and Killian, J. A. (2002) Lipid dependence of membrane anchoring properties and snorkeling behavior of aromatic and charged residues in transmembrane peptides. Biochemistry 41, 7190-7198.
    • (2002) Biochemistry , vol.41 , pp. 7190-7198
    • Strandberg, E.1    Morein, S.2    Rijkers, D.T.S.3    Liskamp, R.M.J.4    van der Wel, P.C.A.5    Killian, J.A.6
  • 57
    • 0033783447 scopus 로고    scopus 로고
    • Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: A CD,N-15 and P-31 solid-state NMR spectroscopy investigation
    • Harzer, U., and Bechinger, B. (2000) Alignment of lysine-anchored membrane peptides under conditions of hydrophobic mismatch: A CD,N-15 and P-31 solid-state NMR spectroscopy investigation. Biochemistry 39, 13106-13114.
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 58
    • 0000562064 scopus 로고
    • Induction of peptide conformation at apolar water interfaces. 1. A study with model peptides of defined hydrophobic periodicity
    • Degrado, W. F., and Lear, J. D. (1985) Induction of peptide conformation at apolar water interfaces. 1. A study with model peptides of defined hydrophobic periodicity. J. Am. Chem. Soc. 107, 7684-7689.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 7684-7689
    • Degrado, W.F.1    Lear, J.D.2
  • 59
    • 0037024166 scopus 로고    scopus 로고
    • Assembly of α-helical peptide coatings on hydrophobic surfaces
    • Long, J. R., Oyler, N., Drobny, G. P., and Stayton, P. S. (2002) Assembly of α-helical peptide coatings on hydrophobic surfaces. J. Am. Chem. Soc. 124, 6297-6303.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6297-6303
    • Long, J.R.1    Oyler, N.2    Drobny, G.P.3    Stayton, P.S.4
  • 61
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino-acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H. Y., Buckwalter, B. L., Shieh, H. M., and Hecht, M. H. (1995) Periodicity of polar and nonpolar amino-acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc. Natl. Acad. Sci. U.S.A. 92, 6349-6353.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 6349-6353
    • Xiong, H.Y.1    Buckwalter, B.L.2    Shieh, H.M.3    Hecht, M.H.4
  • 62
    • 0030047220 scopus 로고    scopus 로고
    • Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries
    • PerezPaya, E., Houghten, R. A., and Blondelle, S. E. (1996) Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries. J. Biol. Chem. 271, 4120-4126.
    • (1996) J. Biol. Chem , vol.271 , pp. 4120-4126
    • PerezPaya, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 63
    • 0032689764 scopus 로고    scopus 로고
    • Spherical self-assembly of a synthetic α-helical peptide in water
    • Fujita, K., Kimura, S., and Imanishi, Y. (1999) Spherical self-assembly of a synthetic α-helical peptide in water. Langmuir 15, 4377-4379.
    • (1999) Langmuir , vol.15 , pp. 4377-4379
    • Fujita, K.1    Kimura, S.2    Imanishi, Y.3
  • 64
    • 0033561626 scopus 로고    scopus 로고
    • Surface active properties of amphiphilic sequential isopeptides: Comparison between α-helical and β-sheet conformations
    • Maget-Dana, R., Lelievre, D., and Brack, A. (1999) Surface active properties of amphiphilic sequential isopeptides: comparison between α-helical and β-sheet conformations. Biopolymers 49, 415-423.
    • (1999) Biopolymers , vol.49 , pp. 415-423
    • Maget-Dana, R.1    Lelievre, D.2    Brack, A.3
  • 65
    • 0035977635 scopus 로고    scopus 로고
    • Medium-dependent self-assembly of an amphiphilic peptide: Direct observation of peptide phase domains at the air-water interface
    • Powers, E. T., and Kelly, J. W. (2001) Medium-dependent self-assembly of an amphiphilic peptide: direct observation of peptide phase domains at the air-water interface. J. Am. Chem. Soc. 123, 775-776.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 775-776
    • Powers, E.T.1    Kelly, J.W.2
  • 66
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3, 842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 67
    • 0000243829 scopus 로고
    • Procheck - a program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck - a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 68
    • 0026143161 scopus 로고
    • Theoretical CD studies of polypeptide helices - examination of important electronic and geometric factors
    • Manning, M. C., and Woody, R. W. (1991) Theoretical CD studies of polypeptide helices - examination of important electronic and geometric factors. Biopolymers 31, 569-586.
    • (1991) Biopolymers , vol.31 , pp. 569-586
    • Manning, M.C.1    Woody, R.W.2
  • 69
    • 0038694994 scopus 로고    scopus 로고
    • Snorkeling of lysine side chains in transmembrane helices: How easy can it get?
    • Strandberg, E., and Killian, J. A. (2003) Snorkeling of lysine side chains in transmembrane helices: how easy can it get? FEBS Lett. 544, 69-73.
    • (2003) FEBS Lett , vol.544 , pp. 69-73
    • Strandberg, E.1    Killian, J.A.2
  • 71
    • 0031820877 scopus 로고    scopus 로고
    • Phospholipid component volumes: Determination and application to bilayer structure calculations
    • Armen, R. S., Uitto, O. D., and Feller, S. E. (1998) Phospholipid component volumes: determination and application to bilayer structure calculations. Biophys. J. 75, 734-744.
    • (1998) Biophys. J , vol.75 , pp. 734-744
    • Armen, R.S.1    Uitto, O.D.2    Feller, S.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.