메뉴 건너뛰기




Volumn 517, Issue 7534, 2015, Pages 347-350

Neuroscience: Dragonflies predict and plan their hunts

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; ARGININE; GUANIDINE; ION; LYSINE; OLIGOPEPTIDE; AMMONIUM DERIVATIVE; BUFFER; CATION; COLLOID; ETHANOLAMINE DERIVATIVE; METHANOL; PEPTIDE; PROTON; TRIETHANOLAMINE;

EID: 84922608590     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14018     Document Type: Article
Times cited : (166)

References (43)
  • 1
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. Interfaces and the driving force of hydrophobic assembly. Nature 437, 640-647 (2005).
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 3
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • Whitesides, G. M. & Grzybowski, B. Self-assembly at all scales. Science 295, 2418-2421 (2002).
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 4
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson, H. J., Wright, P. E. & Scheraga, H. A. The role of hydrophobic interactions in initiation and propagation of protein folding. Proc. Natl Acad. Sci. USA 103, 13057-13061 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3
  • 5
    • 84869842324 scopus 로고    scopus 로고
    • Water structural transformation at molecular hydrophobic interfaces
    • Davis, J. G., Gierszal, K. P., Wang, P. & Ben-Amotz, D. Water structural transformation at molecular hydrophobic interfaces. Nature 491, 582-585 (2012).
    • (2012) Nature , vol.491 , pp. 582-585
    • Davis, J.G.1    Gierszal, K.P.2    Wang, P.3    Ben-Amotz, D.4
  • 6
    • 0034682487 scopus 로고    scopus 로고
    • Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
    • Huang, D. M. & Chandler, D. Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding. Proc. Natl Acad. Sci. USA 97, 8324-8327 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8324-8327
    • Huang, D.M.1    Chandler, D.2
  • 7
    • 80053634226 scopus 로고    scopus 로고
    • Signature of hydrophobic hydration in a single polymer
    • Li, I. T. S. & Walker, G. C. Signature of hydrophobic hydration in a single polymer. Proc. Natl Acad. Sci. USA 108, 16527-16532 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 16527-16532
    • Li, I.T.S.1    Walker, G.C.2
  • 8
    • 77955179167 scopus 로고    scopus 로고
    • Mapping hydrophobicity at the nanoscale: Applications to heterogeneous surfaces and proteins
    • Acharya, H.,Vembanur, S., Jamadagni, S. N.&Garde, S.Mapping hydrophobicity at the nanoscale: applications to heterogeneous surfaces and proteins. Faraday Discuss. 146, 353-365 (2010).
    • (2010) Faraday Discuss. , vol.146 , pp. 353-365
    • Acharya, H.1    Vembanur, S.2    Jamadagni, S.N.3    Garde, S.4
  • 9
    • 75749108542 scopus 로고    scopus 로고
    • Fluctuations of water near extended hydrophobic and hydrophilic surfaces
    • Patel, A. J., Varilly, P. & Chandler, D. Fluctuations of water near extended hydrophobic and hydrophilic surfaces. J. Phys. Chem. B 114, 1632-1637 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 1632-1637
    • Patel, A.J.1    Varilly, P.2    Chandler, D.3
  • 10
    • 84857761874 scopus 로고    scopus 로고
    • Sitting at the edge: How biomolecules use hydrophobicity to tune their interactions and function
    • Patel, A. J. et al. Sitting at the edge: how biomolecules use hydrophobicity to tune their interactions and function. J. Phys. Chem. B 116, 2498-2503 (2012).
    • (2012) J. Phys. Chem. B , vol.116 , pp. 2498-2503
    • Patel, A.J.1
  • 11
    • 33847230717 scopus 로고    scopus 로고
    • Hydration behavior under confinement by nanoscale surfaces with patterned hydrophobicity and hydrophilicity
    • Giovambattista, N., Debenedetti, P. G. & Rossky, P. J. Hydration behavior under confinement by nanoscale surfaces with patterned hydrophobicity and hydrophilicity. J. Phys. Chem. C 111, 1323-1332 (2007).
    • (2007) J. Phys. Chem. C , vol.111 , pp. 1323-1332
    • Giovambattista, N.1    Debenedetti, P.G.2    Rossky, P.J.3
  • 12
    • 84899987510 scopus 로고    scopus 로고
    • Field-SEA: A model for computing the solvation free energies of nonpolar, polar, and charged solutes in water
    • Li, L., Fennell, C. J. & Dill, K. A. Field-SEA: a model for computing the solvation free energies of nonpolar, polar, and charged solutes in water. J. Phys. Chem. B 118, 6431-6437 (2014).
    • (2014) J. Phys. Chem. B , vol.118 , pp. 6431-6437
    • Li, L.1    Fennell, C.J.2    Dill, K.A.3
  • 14
    • 0003098343 scopus 로고
    • An essay on the cohesion of fluids
    • Young, T. An essay on the cohesion of fluids. Philos. Trans. R. Soc. Lond. 95, 65-87 (1805).
    • (1805) Philos. Trans. R. Soc. Lond. , vol.95 , pp. 65-87
    • Young, T.1
  • 15
    • 79952748332 scopus 로고    scopus 로고
    • Singlemolecule force spectroscopy of beta-peptides that display well-defined threedimensional chemical patterns
    • Acevedo-Vélez, C., Andre, G., Dufrene, Y. F., Gellman, S. H. & Abbott, N. L. Singlemolecule force spectroscopy of beta-peptides that display well-defined threedimensional chemical patterns. J. Am. Chem. Soc. 133, 3981-3988 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3981-3988
    • Acevedo-Vélez, C.1    Andre, G.2    Dufrene, Y.F.3    Gellman, S.H.4    Abbott, N.L.5
  • 16
    • 79958176947 scopus 로고    scopus 로고
    • Methanol strengthens hydrogen bonds and weakens hydrophobic interactions in proteins-a combined molecular dynamics and NMR study
    • Hwang, S., Shao, Q., Williams, H., Hilty, C. & Gao, Y. Q. Methanol strengthens hydrogen bonds and weakens hydrophobic interactions in proteins-a combined molecular dynamics and NMR study. J. Phys. Chem. B 115, 6653-6660 (2011).
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6653-6660
    • Hwang, S.1    Shao, Q.2    Williams, H.3    Hilty, C.4    Gao, Y.Q.5
  • 17
    • 48849117719 scopus 로고    scopus 로고
    • Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides
    • Pomerantz, W. C., Grygiel, T. L. R., Lai, J. R. & Gellman, S. H. Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides. Org. Lett. 10, 1799-1802 (2008).
    • (2008) Org. Lett. , vol.10 , pp. 1799-1802
    • Pomerantz, W.C.1    Grygiel, T.L.R.2    Lai, J.R.3    Gellman, S.H.4
  • 18
    • 0037019548 scopus 로고    scopus 로고
    • Chemical force spectroscopy in heterogeneous systems: Intermolecular interactions involving epoxy polymer, mixed monolayers, and polar solvents
    • Vezenov, D. V., Zhuk, A. V., Whitesides, G. M. & Lieber, C. M. Chemical force spectroscopy in heterogeneous systems: intermolecular interactions involving epoxy polymer, mixed monolayers, and polar solvents. J. Am. Chem. Soc. 124, 10578-10588 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10578-10588
    • Vezenov, D.V.1    Zhuk, A.V.2    Whitesides, G.M.3    Lieber, C.M.4
  • 19
    • 84861951757 scopus 로고    scopus 로고
    • Surface forces in thin liquid films of n-alcohols and of water-ethanol mixtures confined between hydrophobic surfaces
    • Wang, J. L., Li, Z. L., Yoon, R. H. & Eriksson, J. C. Surface forces in thin liquid films of n-alcohols and of water-ethanol mixtures confined between hydrophobic surfaces. J. Colloid Interface Sci. 379, 114-120 (2012).
    • (2012) J. Colloid Interface Sci. , vol.379 , pp. 114-120
    • Wang, J.L.1    Li, Z.L.2    Yoon, R.H.3    Eriksson, J.C.4
  • 20
    • 0037959630 scopus 로고    scopus 로고
    • Environment-independent 14-helix formation in short b-peptides: Striking a balance between shape control and functional diversity
    • Raguse, T. L., Lai, J. R. & Gellman, S. H. Environment-independent 14-helix formation in short b-peptides: striking a balance between shape control and functional diversity. J. Am. Chem. Soc. 125, 5592-5593 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5592-5593
    • Raguse, T.L.1    Lai, J.R.2    Gellman, S.H.3
  • 22
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P. & Dufrene, Y. F. Detection and localization of single molecular recognition events using atomic force microscopy. Nature Methods 3, 347-355 (2006).
    • (2006) Nature Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 23
    • 77649101458 scopus 로고    scopus 로고
    • Unfolding of hydrophobic polymers in guanidinium chloride solutions
    • Godawat, R., Jamadagni, S. N. & Garde, S. Unfolding of hydrophobic polymers in guanidinium chloride solutions. J. Phys. Chem. B 114, 2246-2254 (2010).
    • (2010) J. Phys. Chem. , pp. 2246-2254
    • Godawat, R.1    Jamadagni, S.N.2    Garde, S.3
  • 24
    • 84858420806 scopus 로고    scopus 로고
    • Hofmeister phenomena: An update on ion specificity in biology
    • LoNostro, P.&Ninham, B. W.Hofmeister phenomena: an update on ion specificity in biology. Chem. Rev. 112, 2286-2322 (2012).
    • (2012) Chem. Rev. , vol.112 , pp. 2286-2322
    • Lo Nostro, P.1    Ninham, B.W.2
  • 25
    • 34548822158 scopus 로고    scopus 로고
    • Sequence dependent behavior of amphiphilic b-peptides on gold surfaces
    • Pomerantz, W. C., Cadwell, K. D., Hsu, Y. J., Gellman, S. H. & Abbott, N. L. Sequence dependent behavior of amphiphilic b-peptides on gold surfaces. Chem. Mater. 19, 4436-4441 (2007).
    • (2007) Chem. Mater. , vol.19 , pp. 4436-4441
    • Pomerantz, W.C.1    Cadwell, K.D.2    Hsu, Y.J.3    Gellman, S.H.4    Abbott, N.L.5
  • 27
    • 22644434404 scopus 로고    scopus 로고
    • Chemical force microscopy: Probing chemical origin of interfacial forces and adhesion
    • Vezenov, D. V., Noy, A. & Ashby, P. Chemical force microscopy: probing chemical origin of interfacial forces and adhesion. J. Adhes. Sci. Technol. 19, 313-364 (2005).
    • (2005) J. Adhes. Sci. Technol. , vol.19 , pp. 313-364
    • Vezenov, D.V.1    Noy, A.2    Ashby, P.3
  • 28
    • 7944225677 scopus 로고    scopus 로고
    • Determination of solid surface tension from particle-substrate pull-off forces measured with the atomic force microscope
    • Drelich, J., Tormoen, G. W. & Beach, E. R. Determination of solid surface tension from particle-substrate pull-off forces measured with the atomic force microscope. J. Colloid Interface Sci. 280, 484-497 (2004).
    • (2004) J. Colloid Interface Sci. , vol.280 , pp. 484-497
    • Drelich, J.1    Tormoen, G.W.2    Beach, E.R.3
  • 29
    • 36649013657 scopus 로고    scopus 로고
    • Direct measurement of hydrophobic forces on cell surfaces using AFM
    • Alsteens, D., Dague, E., Rouxhet, P. G., Baulard, A. R. & Dufrene, Y. F. Direct measurement of hydrophobic forces on cell surfaces using AFM. Langmuir 23, 11977-11979 (2007).
    • (2007) Langmuir , vol.23 , pp. 11977-11979
    • Alsteens, D.1    Dague, E.2    Rouxhet, P.G.3    Baulard, A.R.4    Dufrene, Y.F.5
  • 30
    • 0034225506 scopus 로고    scopus 로고
    • Rupture of hydrophobic microcontacts in water: Correlation of pull-off force with AFMtip radius
    • Skulason, H. & Frisbie, C. D. Rupture of hydrophobic microcontacts in water: correlation of pull-off force with AFMtip radius. Langmuir 16, 6294-6297 (2000).
    • (2000) Langmuir , vol.16 , pp. 6294-6297
    • Skulason, H.1    Frisbie, C.D.2
  • 31
    • 24944548354 scopus 로고    scopus 로고
    • Quantitative determination of surface energy using atomic force microscopy: The case of hydrophobic/hydrophobic contact and hydrophilic/hydrophilic contact
    • Awada, H., Castelein, G. & Brogly, M. Quantitative determination of surface energy using atomic force microscopy: the case of hydrophobic/hydrophobic contact and hydrophilic/hydrophilic contact. Surf. Interface Anal. 37, 755-764 (2005).
    • (2005) Surf. Interface Anal. , vol.37 , pp. 755-764
    • Awada, H.1    Castelein, G.2    Brogly, M.3
  • 33
    • 0034605439 scopus 로고    scopus 로고
    • Probing intermolecular forces and potentials with magnetic feedback chemical force microscopy
    • Ashby, P. D., Chen, L. & Lieber, C. M. Probing intermolecular forces and potentials with magnetic feedback chemical force microscopy. J. Am. Chem. Soc. 122, 9467-9472 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9467-9472
    • Ashby, P.D.1    Chen, L.2    Lieber, C.M.3
  • 34
    • 0037008080 scopus 로고    scopus 로고
    • Direct measurement of glycosaminoglycan intermolecular interactions via high-resolution force spectroscopy
    • Seog, J. et al. Direct measurement of glycosaminoglycan intermolecular interactions via high-resolution force spectroscopy. Macromolecules 35, 5601-5615 (2002).
    • (2002) Macromolecules , vol.35 , pp. 5601-5615
    • Seog, J.1
  • 35
    • 70349336064 scopus 로고    scopus 로고
    • Structure and charging of hydrophobic material/water interfaces studied by phase-sensitive sum-frequency vibrational spectroscopy
    • Tian, C. S. & Shen, Y. R. Structure and charging of hydrophobic material/water interfaces studied by phase-sensitive sum-frequency vibrational spectroscopy. Proc. Natl Acad. Sci. USA 106, 15148-15153 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15148-15153
    • Tian, C.S.1    Shen, Y.R.2
  • 36
    • 13944258422 scopus 로고    scopus 로고
    • Physisorption of hydroxide ions from aqueous solution to a hydrophobic surface
    • Zangi, R. & Engberts, J. B. F. N. Physisorption of hydroxide ions from aqueous solution to a hydrophobic surface. J. Am. Chem. Soc. 127, 2272-2276 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2272-2276
    • Zangi, R.1    Engberts, J.B.F.N.2
  • 37
    • 79959882215 scopus 로고    scopus 로고
    • The orientation and charge of water at the hydrophobic oil dropletwater interface
    • Vácha, R. et al. The orientation and charge of water at the hydrophobic oil dropletwater interface. J. Am. Chem. Soc. 133, 10204-10210 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10204-10210
    • Vácha, R.1
  • 38
    • 27744587245 scopus 로고    scopus 로고
    • Force measurements with the atomic force microscope: Technique, interpretation and applications
    • Butt, H. J., Cappella, B. & Kappl, M. Force measurements with the atomic force microscope: technique, interpretation and applications. Surf. Sci. Rep. 59, 1-152 (2005).
    • (2005) Surf. Sci. Rep. , vol.59 , pp. 1-152
    • Butt, H.J.1    Cappella, B.2    Kappl, M.3
  • 39
    • 0345045336 scopus 로고    scopus 로고
    • Molecular level friction as revealed with a novel scanning probe
    • Burns, A. R., Houston, J. E., Carpick, R. W. & Michalske, T. A. Molecular level friction as revealed with a novel scanning probe. Langmuir 15, 2922-2930 (1999).
    • (1999) Langmuir , vol.15 , pp. 2922-2930
    • Burns, A.R.1    Houston, J.E.2    Carpick, R.W.3    Michalske, T.A.4
  • 40
    • 0142007154 scopus 로고    scopus 로고
    • The effect of liquid-induced adhesion changes on the interfacial shear strength between self-assembled monolayers
    • Vezenov, D. V., Noy, A. & Lieber, C. M. The effect of liquid-induced adhesion changes on the interfacial shear strength between self-assembled monolayers. J. Adhes. Sci. Technol. 17, 1385-1401 (2003).
    • (2003) J. Adhes. Sci. Technol. , vol.17 , pp. 1385-1401
    • Vezenov, D.V.1    Noy, A.2    Lieber, C.M.3
  • 41
    • 0035471135 scopus 로고    scopus 로고
    • B-Peptides: Fromstructure to function
    • Cheng, R. P., Gellman, S. H.&DeGrado, W. F. b-Peptides: fromstructure to function. Chem. Rev. 101, 3219-3232 (2001).
    • (2001) Chem. Rev. , vol.101 , pp. 3219-3232
    • Cheng, R.P.1    Gellman, S.H.2    Degrado, W.F.3
  • 42
    • 80052094249 scopus 로고    scopus 로고
    • Lyotropic liquid crystals formed from ACHC-rich betapeptides
    • Pomerantz, W. C. et al. Lyotropic liquid crystals formed from ACHC-rich betapeptides. J. Am. Chem. Soc. 133, 13604-13613 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13604-13613
    • Pomerantz, W.C.1
  • 43
    • 0032495430 scopus 로고    scopus 로고
    • Molecular conformation in oligo(ethylene glycol)-terminated self-assembled monolayers on gold and silver surfaces determines their ability to resist protein adsorption
    • Harder, P., Grunze, M., Dahint, R., Whitesides, G. M. & Laibinis, P. E. Molecular conformation in oligo(ethylene glycol)-terminated self-assembled monolayers on gold and silver surfaces determines their ability to resist protein adsorption. J. Phys. Chem. B 102, 426-436 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 426-436
    • Harder, P.1    Grunze, M.2    Dahint, R.3    Whitesides, G.M.4    Laibinis, P.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.