메뉴 건너뛰기




Volumn 41, Issue 3, 2004, Pages 435-449

AFM as a high-resolution imaging tool and a molecular bond force probe

Author keywords

hemolysin; Choleratoxin; DNA imaging; Force microscopy; Molecular force probe

Indexed keywords

HEMOLYSIN; PHOSPHATIDYLCHOLINE;

EID: 24644441240     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:41:3:435     Document Type: Review
Times cited : (19)

References (80)
  • 1
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao, Z. and Yang, J. (1995) Progress in high resolution atomic force microscopy in biology. Q. Rev. Biophys. 28, 195-251.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 2
    • 0029563227 scopus 로고
    • Biological atomic force microscopy: From microns to nanometers and beyond
    • Shao, Z., Yang, J., and Somlyo, AP (1995) Biological atomic force microscopy: from microns to nanometers and beyond. Ann. Rev. Cell Dev. Biol. 11, 241-265.
    • (1995) Ann. Rev. Cell Dev. Biol. , vol.11 , pp. 241-265
    • Shao, Z.1    Yang, J.2    Somlyo, A.P.3
  • 3
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Shao, Z., Mou, J., Czajkowsky, D. M., Yang, J., and Yuan, J-J. (1996) Biological atomic force microscopy: what is achieved and what is needed. Adv. Physics 45, 1-86.
    • (1996) Adv. Physics , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.-J.5
  • 4
    • 0030951962 scopus 로고    scopus 로고
    • High-resolution imaging of native biological sample surfaces using scanning probe microscopy
    • Engel, A., Schoenenberger, C.-A., and Muller, D. J. (1997) High-resolution imaging of native biological sample surfaces using scanning probe microscopy. Curr. Opin. Struct. Biol. 7, 279-284.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 279-284
    • Engel, A.1    Schoenenberger, C.-A.2    Muller, D.J.3
  • 6
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: A review
    • Muller, D. J., Schoenenberger, C-A., Schabert, F., and Engel, A. (1997) Structural changes in native membrane proteins monitored at subnanometer resolution with the atomic force microscope: a review. J. Struct. Biol. 119, 149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Muller, D.J.1    Schoenenberger, C.-A.2    Schabert, F.3    Engel, A.4
  • 7
    • 0032560585 scopus 로고    scopus 로고
    • Submolecular resolution of single macromolecules with atomic force microscopy
    • Czajkowsky, D. M. and Shao, Z. (1998) Submolecular resolution of single macromolecules with atomic force microscopy. FEBS Lett. 430, 51-54.
    • (1998) FEBS Lett. , vol.430 , pp. 51-54
    • Czajkowsky, D.M.1    Shao, Z.2
  • 8
    • 11944275288 scopus 로고
    • Scanning force microscopy in biology
    • Bustamante, C. and Keller, D. (1995) Scanning force microscopy in biology. Physics Today 48, 32-38.
    • (1995) Physics Today , vol.48 , pp. 32-38
    • Bustamante, C.1    Keller, D.2
  • 9
    • 0028364295 scopus 로고
    • Biomolecular imaging with the atomic force microscope
    • Hansma, H. G. and Hoh, J. (1994) Biomolecular imaging with the atomic force microscope. Ann. Rev. Biophys. Biomol. Struct. 23, 115-128.
    • (1994) Ann. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 115-128
    • Hansma, H.G.1    Hoh, J.2
  • 10
    • 0034530126 scopus 로고    scopus 로고
    • Single molecule force spectroscopy in biology using the atomic force microscope
    • Zlatanova, J., Lindsay, S. M., and Leuba, S. H. (2000) Single molecule force spectroscopy in biology using the atomic force microscope. Prog. Biophys. Mol. Biol. 74, 37-61.
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 37-61
    • Zlatanova, J.1    Lindsay, S.M.2    Leuba, S.H.3
  • 11
    • 0024977453 scopus 로고
    • Imaging crystals, polymers, and processes in water with the atomic force microscope
    • Drake, B., Prater, C. B., Weisenhorn, A. L., Gould, S. A. C., Albrecht, T. R., Quate, C. F., et al. (1989) Imaging crystals, polymers, and processes in water with the atomic force microscope. Science 243, 15861589.
    • (1989) Science , vol.243 , pp. 15861589
    • Drake, B.1    Prater, C.B.2    Weisenhorn, A.L.3    Gould, S.A.C.4    Albrecht, T.R.5    Quate, C.F.6
  • 12
    • 0033400944 scopus 로고    scopus 로고
    • A analysis of the Protein Data Bank in search of the temporal and global trends
    • Wessig, H. and Borne, P. E. (1999) A analysis of the Protein Data Bank in search of the temporal and global trends. Bioinformatics 15, 807-831.
    • (1999) Bioinformatics , vol.15 , pp. 807-831
    • Wessig, H.1    Borne, P.E.2
  • 13
    • 0030043696 scopus 로고    scopus 로고
    • The effect of deformation on the lateral resolution of atomic force microscopy
    • Yang, J., Mou, J., Yuan, J-Y., and Shao, Z. (1996) The effect of deformation on the lateral resolution of atomic force microscopy. J. Microscopy 182, 106-113.
    • (1996) J. Microscopy , vol.182 , pp. 106-113
    • Yang, J.1    Mou, J.2    Yuan, J.-Y.3    Shao, Z.4
  • 14
    • 11944250146 scopus 로고
    • Atomic force microscopy
    • Rugar, D. and Hansma, P, (1990) Atomic force microscopy. Physics Today 43, 23-30.
    • (1990) Physics Today , vol.43 , pp. 23-30
    • Rugar, D.1    Hansma, P.2
  • 16
    • 0032474758 scopus 로고    scopus 로고
    • Covalently functionalized nanotubes as nanometresized probes in chemistry and biology
    • Wong, S. S., Joselevich, E., Woolley, A. T., Cheung, C-L., and Lieber, C. M. (1998) Covalently functionalized nanotubes as nanometresized probes in chemistry and biology. Nature 394, 53-55.
    • (1998) Nature , vol.394 , pp. 53-55
    • Wong, S.S.1    Joselevich, E.2    Woolley, A.T.3    Cheung, C.-L.4    Lieber, C.M.5
  • 18
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh, J. H., Lal, R., John, S. A., Revel, J-P., and Arnsdorf, M. F. (1991) Atomic force microscopy and dissection of gap junctions. Science 253, 1405-1408.
    • (1991) Science , vol.253 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.-P.4    Arnsdorf, M.F.5
  • 19
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins
    • Yang, J., Tamm, L. K., Tillack, T. W., and Shao, Z. (1993) New approach for atomic force microscopy of membrane proteins. J. Mol. Biol. 229, 286-290.
    • (1993) J. Mol. Biol. , vol.229 , pp. 286-290
    • Yang, J.1    Tamm, L.K.2    Tillack, T.W.3    Shao, Z.4
  • 20
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids
    • Mou, J. X., Yang, J., and Shao, Z. F. (1995) Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J. Mol. Biol. 248, 507-512.
    • (1995) J. Mol. Biol. , vol.248 , pp. 507-512
    • Mou, J.X.1    Yang, J.2    Shao, Z.F.3
  • 21
    • 0033105888 scopus 로고    scopus 로고
    • Heptameric structures of two α-hemolysin mutants imaged with in situ atomic force microscopy
    • Malghani, M. S., Fang, Y., Cheley, S., Bayley, H., and Yang, J. (1999) Heptameric structures of two α-hemolysin mutants imaged with in situ atomic force microscopy. Microscopy Res. Tech. 44, 353-356.
    • (1999) Microscopy Res. Tech. , vol.44 , pp. 353-356
    • Malghani, M.S.1    Fang, Y.2    Cheley, S.3    Bayley, H.4    Yang, J.5
  • 22
    • 0030741317 scopus 로고    scopus 로고
    • The heptameric prepore of a staphylococcal α-hemolysin mutant in lipid bilayers imaged by atomic force microscopy
    • Fang, Y., Cheley, S., Bayley, H., and Yang, J. (1997) The heptameric prepore of a staphylococcal α-hemolysin mutant in lipid bilayers imaged by atomic force microscopy. Biochemistry 36, 9518-9522.
    • (1997) Biochemistry , vol.36 , pp. 9518-9522
    • Fang, Y.1    Cheley, S.2    Bayley, H.3    Yang, J.4
  • 23
    • 0031404458 scopus 로고    scopus 로고
    • Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel
    • Cheley, S., Malghani, M. S., Song, L., Hobaugh, M., Gouaux, J. E., Yang, J., et al. (1997) Spontaneous oligomerization of a staphylococcal α-hemolysin conformationally constrained by removal of residues that form the transmembrane β-barrel. Protein Eng. 10, 1433-1443.
    • (1997) Protein Eng. , vol.10 , pp. 1433-1443
    • Cheley, S.1    Malghani, M.S.2    Song, L.3    Hobaugh, M.4    Gouaux, J.E.5    Yang, J.6
  • 24
    • 0028013352 scopus 로고
    • Structure and stability of pertussis toxin studied by in situ atomic force microscopy
    • Yang, J., Mou, J., and Shao, Z. (1994) Structure and stability of pertussis toxin studied by in situ atomic force microscopy. FEBS Lett. 338, 89-92.
    • (1994) FEBS Lett. , vol.338 , pp. 89-92
    • Yang, J.1    Mou, J.2    Shao, Z.3
  • 26
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Muller, D. J., Amrein, M., and Engel, A. (1997) Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119, 172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Muller, D.J.1    Amrein, M.2    Engel, A.3
  • 27
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert, F. A., Henn, C., and Engel, A. (1995) Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy, Science 268, 92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 29
    • 0030822454 scopus 로고    scopus 로고
    • Two-dimensional condensation of DNA molecules on cationic lipid membranes
    • Fang, Y. and Yang, J. (1997) Two-dimensional condensation of DNA molecules on cationic lipid membranes. J. Phys. Chem. 101, 441-449.
    • (1997) J. Phys. Chem. , vol.101 , pp. 441-449
    • Fang, Y.1    Yang, J.2
  • 32
    • 0026031974 scopus 로고
    • Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measure with specular reflection of neutrons
    • Johnson, S. J., Bayerl, T. M., McDermott, D. C., Adam, G. W., Rennie, A. R., Thomas, R .K., et al. (1991) Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measure with specular reflection of neutrons. Biophys. J. 59, 289-294.
    • (1991) Biophys. J. , vol.59 , pp. 289-294
    • Johnson, S.J.1    Bayerl, T.M.2    McDermott, D.C.3    Adam, G.W.4    Rennie, A.R.5    Thomas, R.K.6
  • 33
    • 0034247718 scopus 로고    scopus 로고
    • The main phase transition of mica-supported phosphatidylcholine membranes
    • Yang, J. and Appleyard, J. (2000) The main phase transition of mica-supported phosphatidylcholine membranes. J. Phys. Chem. 104, 8097-8100.
    • (2000) J. Phys. Chem. , vol.104 , pp. 8097-8100
    • Yang, J.1    Appleyard, J.2
  • 34
    • 0026785678 scopus 로고
    • Assembly of oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis
    • Walker, B., Krishnasastry, M., Zorn, L., and Bayley, H. (1992) Assembly of oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267, 21782-21786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 36
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker, B., Braha, O., Cheley, S., and Bayley, H. (1995) An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem. Biol. 2, 99-105.
    • (1995) Chem. Biol. , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 37
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J. E., Braha, O., Hobaugh, M. R., Song, L., Cheley, S., Shustak, C., et al. (1994) Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. U S A 91, 12828-12831.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6
  • 38
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Baley, H., and Gouaux, J. E. (1996) Structure of Staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1865.
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Baley, H.5    Gouaux, J.E.6
  • 39
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., Sheng, S., and Shao, Z. (1998). Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276, 325-330.
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 40
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • Gu, L-Q., Braha, O., Conlan, S., Cheley, S., and Bayley, H. (1999) Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature 398, 686-690.
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.-Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 41
    • 0035951448 scopus 로고    scopus 로고
    • Capture of a single molecule in a nanocavity
    • Gu, L-Q., Cheley, S., and Bayley, H. (2001) Capture of a single molecule in a nanocavity. Science 291, 636-640.
    • (2001) Science , vol.291 , pp. 636-640
    • Gu, L.-Q.1    Cheley, S.2    Bayley, H.3
  • 42
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley, H. and Cremer, P. S. (2001) Stochastic sensors inspired by biology. Nature 413, 226-230.
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 43
    • 0034930381 scopus 로고    scopus 로고
    • Sequence-specific detection of individual DNA strands using engineered nanopores
    • Howorka, S., Cheley, S., and Bayley, H. (2001) Sequence-specific detection of individual DNA strands using engineered nanopores. Nat. Biotechnol. 19, 636-639.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 636-639
    • Howorka, S.1    Cheley, S.2    Bayley, H.3
  • 45
    • 0002822783 scopus 로고    scopus 로고
    • The close-packing and the pitch-variance of membrane-bound DNA in solution
    • Yang, J., Wang, L., and Camerini-Otero, R. D. (1996) The close-packing and the pitch-variance of membrane-bound DNA in solution. Nanobiology 4, 93-100.
    • (1996) Nanobiology , vol.4 , pp. 93-100
    • Yang, J.1    Wang, L.2    Camerini-Otero, R.D.3
  • 46
    • 0029127492 scopus 로고
    • High-resolution atomic-force microscopy of DNA: The pitch of the double helix
    • Mou, J., Czajkowsky, D. M., Zhang, Y., and Shao, Z. (1995) High-resolution atomic-force microscopy of DNA: the pitch of the double helix. FEBS Lett. 371, 279-282.
    • (1995) FEBS Lett. , vol.371 , pp. 279-282
    • Mou, J.1    Czajkowsky, D.M.2    Zhang, Y.3    Shao, Z.4
  • 47
    • 0001447503 scopus 로고    scopus 로고
    • Stable binding of DNA to zwitterionic lipid bilayers in aqueous solutions
    • Malghani, M. S. and Yang, J. (1998) Stable binding of DNA to zwitterionic lipid bilayers in aqueous solutions. J. Phys. Chem. 44, 8930-8933.
    • (1998) J. Phys. Chem. , vol.44 , pp. 8930-8933
    • Malghani, M.S.1    Yang, J.2
  • 48
    • 0022106012 scopus 로고
    • Low-frequency motions in protein molecules, β-sheet and β-barrel
    • Chou, K-C. (1985) Low-frequency motions in protein molecules, β-sheet and β-barrel. Biophys. J. 48, 289-297.
    • (1985) Biophys. J. , vol.48 , pp. 289-297
    • Chou, K.-C.1
  • 49
    • 0014702697 scopus 로고
    • Vibrational frequencies and modes of α-helix
    • Itoh, K. and Shimanouchi, T. (1970) Vibrational frequencies and modes of α-helix. Biopolymers 9, 383-399.
    • (1970) Biopolymers , vol.9 , pp. 383-399
    • Itoh, K.1    Shimanouchi, T.2
  • 50
    • 0021245237 scopus 로고
    • Biological functions of low-frequency vibrations (phonons): III. helical structures and microenvironment
    • Chou, K-C. (1984) Biological functions of low-frequency vibrations (phonons): III. helical structures and microenvironment. Biophys. J. 45, 881-890.
    • (1984) Biophys. J. , vol.45 , pp. 881-890
    • Chou, K.-C.1
  • 51
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? A protein dynamics force constant measured by neutron scattering
    • Zaccai, G. (2001) How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science 288, 1604-1607.
    • (2001) Science , vol.288 , pp. 1604-1607
    • Zaccai, G.1
  • 52
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from the dynamical transition: A force constant analysis
    • Bicout, D. J. and Zaccai, G. (2001) Protein flexibility from the dynamical transition: a force constant analysis. Biophys. J. 80, 1115-1123.
    • (2001) Biophys. J. , vol.80 , pp. 1115-1123
    • Bicout, D.J.1    Zaccai, G.2
  • 54
    • 0025804295 scopus 로고
    • Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli
    • Sixma, T. K., Pronk, S. E., Kalk, K. H., Wartna, E. S., van Zanten, B. A. M., Witholt, B., et al. (1991) Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature 351, 371-377.
    • (1991) Nature , vol.351 , pp. 371-377
    • Sixma, T.K.1    Pronk, S.E.2    Kalk, K.H.3    Wartna, E.S.4    Van Zanten, B.A.M.5    Witholt, B.6
  • 58
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - and chemistry in single molecular bonds
    • Evans, E. (2001) Probing the relation between force - lifetime - and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30, 105-128.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 59
    • 0035423783 scopus 로고    scopus 로고
    • Force as a probe of membrane protein structure and function
    • Leckband, D. (2001) Force as a probe of membrane protein structure and function. Curr. Opin. Struct. Biol. 11, 433-439.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 433-439
    • Leckband, D.1
  • 61
    • 0029073021 scopus 로고
    • Direct measurement of hydrogen bonding in DNA nucleotide bases by atomic force microscopy
    • Boland, T. and Ratner, B. D. (1995) Direct measurement of hydrogen bonding in DNA nucleotide bases by atomic force microscopy. Proc. Natl. Acad. Sci. U S A 92, 5297-5301.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 5297-5301
    • Boland, T.1    Ratner, B.D.2
  • 62
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E-L., Moy, V. T., and Gaub, H. (1994) Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.3
  • 64
    • 0028007197 scopus 로고
    • Direct measurement of the forces between complementary strands of DNA
    • Lee, G. U., Chrisey, L. A., and Colton, R. J. (1994) Direct measurement of the forces between complementary strands of DNA. Science 266, 771-773.
    • (1994) Science , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 65
    • 0032514687 scopus 로고    scopus 로고
    • Force-mediated kinetics of single P-selectin ligand complexes observed by atomic force microscopy
    • Fritz, J., Katopodis, A. G., Kolbinger, F., and Anselmetti, D. (1998) Force-mediated kinetics of single P-selectin ligand complexes observed by atomic force microscopy Proc. Natl. Acad. Sci. U S A 95, 12283-12288.
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 12283-12288
    • Fritz, J.1    Katopodis, A.G.2    Kolbinger, F.3    Anselmetti, D.4
  • 66
    • 0032542229 scopus 로고    scopus 로고
    • Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring
    • Marszalek, P. E., Oberhauser, A. F., Pang, Y. P., and Fernandez, J. M. (1998) Polysaccharide elasticity governed by chair-boat transitions of the glucopyranose ring. Nature 396, 661-664.
    • (1998) Nature , vol.396 , pp. 661-664
    • Marszalek, P.E.1    Oberhauser, A.F.2    Pang, Y.P.3    Fernandez, J.M.4
  • 67
    • 0036231598 scopus 로고    scopus 로고
    • Determination of elastic moduli of thin layers of soft material using the atomic force microscope
    • Dimitriadis, E. K., Horkay, F., Maresca, J., Kachar, B., and Chadwick, R. S. (2002) Determination of elastic moduli of thin layers of soft material using the atomic force microscope. Biophys. J. 82, 2798-2810.
    • (2002) Biophys. J. , vol.82 , pp. 2798-2810
    • Dimitriadis, E.K.1    Horkay, F.2    Maresca, J.3    Kachar, B.4    Chadwick, R.S.5
  • 68
    • 0347193736 scopus 로고
    • Reaction-rate theory: Fifty years after Kramers
    • Hanggi, P., Talkner, P., and Borkovec, M. (1990) Reaction-rate theory: fifty years after Kramers. Rev. Mod. Phys. 62, 251-341.
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 251-341
    • Hanggi, P.1    Talkner, P.2    Borkovec, M.3
  • 69
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R., Nassoy, P., Leung, A., Ritchie, K., and Evans, E. (1999) Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397, 60-63.
    • (1999) Nature , vol.397 , pp. 60-63
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 70
  • 71
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher, T. E., Marszalek, P. E., and Fernandez, J. M. (2000) Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7, 719-724.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 72
    • 0036221849 scopus 로고    scopus 로고
    • Molecular forces for the binding and condensation of DNA molecules
    • Cai, X-E. and Yang, J. (2002) Molecular forces for the binding and condensation of DNA molecules. Biophys. J. 82, 357-365.
    • (2002) Biophys. J. , vol.82 , pp. 357-365
    • Cai, X.-E.1    Yang, J.2
  • 73
    • 0343100861 scopus 로고
    • Preparation of polyacrylamide gel filled capillaries for ultrahigh resolution of polynucleotides by capillary gel electrophoresis
    • Baba, Y., Matsuura, T., Wakamoto, K., Morita, Y., Nishitsu, Y., and Tsuhako, M. (1992) Preparation of polyacrylamide gel filled capillaries for ultrahigh resolution of polynucleotides by capillary gel electrophoresis. Anal. Chem. 64, 1221-1226.
    • (1992) Anal. Chem. , vol.64 , pp. 1221-1226
    • Baba, Y.1    Matsuura, T.2    Wakamoto, K.3    Morita, Y.4    Nishitsu, Y.5    Tsuhako, M.6
  • 74
    • 0031001349 scopus 로고    scopus 로고
    • Dynamics of molecular adhesion bonds
    • Evans, E. and Ritchie, K. (1997) Dynamics of molecular adhesion bonds. Biophys. J. 72, 1541-1555.
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 76
    • 0035957434 scopus 로고    scopus 로고
    • Free energy reconstruction from nonequilibrium single-molecule pulling experiments
    • Hummer, G. and Szabo, A. (2001) Free energy reconstruction from nonequilibrium single-molecule pulling experiments. Proc. Natl. Acad. Sci. U S A 98, 3658-3661.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 3658-3661
    • Hummer, G.1    Szabo, A.2
  • 77
    • 0037446757 scopus 로고    scopus 로고
    • The binding potential between the cholera toxin B-oligomer and its receptor
    • Cai, X-E. and Yang, J. (2003) The binding potential between the cholera toxin B-oligomer and its receptor. Biochemistry 42, 4028-4034.
    • (2003) Biochemistry , vol.42 , pp. 4028-4034
    • Cai, X.-E.1    Yang, J.2
  • 78
    • 0031642993 scopus 로고    scopus 로고
    • Electrostatics of DNA-cationic lipid complexes: Isoelectric instability
    • Bruinsma, R. (1998) Electrostatics of DNA-cationic lipid complexes: isoelectric instability. Eur. Phys. J. B4, 75-88.
    • (1998) Eur. Phys. J. B , vol.4 , pp. 75-88
    • Bruinsma, R.1
  • 79
    • 0028140707 scopus 로고
    • Intermolecular forces and energies
    • Moy, V. T., Florin, E. L., and Gaub, H. E. (1994) Intermolecular forces and energies. Science 266, 257-260.
    • (1994) Science , vol.266 , pp. 257-260
    • Moy, V.T.1    Florin, E.L.2    Gaub, H.E.3
  • 80
    • 35448992145 scopus 로고    scopus 로고
    • Isothermal titration calorimetry for studying interactions between peptides and lipid membranes
    • (Simon, S. A. and McIntosh, T. J., eds.), Academic Press, San Diego
    • Wieprecht, T. and Seelig, J. (2002) Isothermal titration calorimetry for studying interactions between peptides and lipid membranes. In Peptide-Lipid Interactions, Current Topics in Membranes, Vol. 52 (Simon, S. A. and McIntosh, T. J., eds.), Academic Press, San Diego, pp. 31-56.
    • (2002) Peptide-Lipid Interactions, Current Topics in Membranes , vol.52 , pp. 31-56
    • Wieprecht, T.1    Seelig, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.