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Volumn 5, Issue 3, 1997, Pages 325-336

New applications of simulated annealing in X-ray crystallography and solution NMR

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EID: 0031569392     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00190-1     Document Type: Short Survey
Times cited : (198)

References (82)
  • 4
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 5
    • 0000870109 scopus 로고
    • Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: Application to crambin
    • Brünger A.T., Clore, G.M., Gronenborn, A.M. & Karplus, M. (1986). Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin. Proc. Natl. Acad. Sci. USA 83, 3801-3805.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3801-3805
    • Brünger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Karplus, M.4
  • 7
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 8
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances Crystallographic structure refinement
    • Rice, L.M. & Brünger, A.T. (1994). Torsion angle dynamics: reduced variable conformational sampling enhances Crystallographic structure refinement. Proteins 19, 277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 9
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N.S. & Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Cryst. A 52, 659-668.
    • (1996) Acta Cryst. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 10
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances Crystallographic simulated annealing refinement
    • in press
    • Adams, P.D., Pannu, N.S., Read, R.J. & Brünger, A.T. (1997). Cross-validated maximum likelihood enhances Crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA, in press.
    • (1997) Proc. Natl. Acad. Sci. USA
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 11
    • 0027918891 scopus 로고
    • Assessment of the quality of solution nuclear magnetic resonance structures by complete cross-validation
    • Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R. & Nilges, M. (1993). Assessment of the quality of solution nuclear magnetic resonance structures by complete cross-validation. Science 261, 328-331.
    • (1993) Science , vol.261 , pp. 328-331
    • Brünger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Saffrich, R.4    Nilges, M.5
  • 12
    • 0030621858 scopus 로고    scopus 로고
    • Torsion angle molecular dynamics is a new, efficient tool for NMR structure calculation
    • Stein, E.G., Rice, L.M. & Brünger, A.T. (1997). Torsion angle molecular dynamics is a new, efficient tool for NMR structure calculation. J. Magn. Resonance Ser. B 124, 154-164.
    • (1997) J. Magn. Resonance Ser. B , vol.124 , pp. 154-164
    • Stein, E.G.1    Rice, L.M.2    Brünger, A.T.3
  • 13
    • 0022336792 scopus 로고
    • Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm
    • Braun, W. & Go, N. (1985). Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. J. Mol. Biol. 186, 611-626.
    • (1985) J. Mol. Biol. , vol.186 , pp. 611-626
    • Braun, W.1    Go, N.2
  • 14
    • 0023339433 scopus 로고
    • Distance geometry and related methods for protein structure determination from NMR data
    • Braun, W. (1987). Distance geometry and related methods for protein structure determination from NMR data. Quart. Rev. Biophys. 19, 115-157.
    • (1987) Quart. Rev. Biophys. , vol.19 , pp. 115-157
    • Braun, W.1
  • 15
    • 0023732144 scopus 로고
    • Determination of three dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988). Determination of three dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS lett. 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 17
  • 18
    • 85005537029 scopus 로고
    • Thermal motion and conformational disorder in protein crystal structures: Comparison of multi-conformer and time-averaging models
    • Burling, F.T. & Brünger, A.T. (1994). Thermal motion and conformational disorder in protein crystal structures: comparison of multi-conformer and time-averaging models. Isr. J. Chem. 34, 165-175.
    • (1994) Isr. J. Chem. , vol.34 , pp. 165-175
    • Burling, F.T.1    Brünger, A.T.2
  • 19
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F.T., Weis, W.I., Flaherty, K.M. & Brünger, A.T. (1996). Direct observation of protein solvation and discrete disorder with experimental crystallographic phases, Science 271, 72-77.
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brünger, A.T.4
  • 20
    • 0029022355 scopus 로고
    • Conformational variability of solution nuclear magnetic resonance structures
    • Bonvin, A.M.J.J. & Brünger, A.T. (1995). Conformational variability of solution nuclear magnetic resonance structures. J. Mol. Biol. 250, 80-93.
    • (1995) J. Mol. Biol. , vol.250 , pp. 80-93
    • Bonvin, A.M.J.J.1    Brünger, A.T.2
  • 21
    • 0029693351 scopus 로고    scopus 로고
    • Do NOE distances contain enough information to assess the relative populations of multi-conformer structures?
    • Bonvin, A.M.J.J. & Brünger, A.T. (1996). Do NOE distances contain enough information to assess the relative populations of multi-conformer structures? J. Biomol. NMR 7, 72-76.
    • (1996) J. Biomol. NMR , vol.7 , pp. 72-76
    • Bonvin, A.M.J.J.1    Brünger, A.T.2
  • 22
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W.A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 23
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 25
    • 11644328584 scopus 로고
    • Systematic analysis of structural data as a research technique in organic chemistry
    • Allen, F.H., Kennard, O. & Taylor, R. (1983). Systematic analysis of structural data as a research technique in organic chemistry. Accounts Chem. Res. 16, 146-153.
    • (1983) Accounts Chem. Res. , vol.16 , pp. 146-153
    • Allen, F.H.1    Kennard, O.2    Taylor, R.3
  • 27
    • 0030059610 scopus 로고    scopus 로고
    • Ribonuclease from Streptomyces aureofaciens at atomic resolution
    • Sevcik, J., Dauter, Z., Lamzin, V.S. & Wilson, K.S. (1996). Ribonuclease from Streptomyces aureofaciens at atomic resolution, Acta Cryst. D 52, 327-344.
    • (1996) Acta Cryst. D , vol.52 , pp. 327-344
    • Sevcik, J.1    Dauter, Z.2    Lamzin, V.S.3    Wilson, K.S.4
  • 28
    • 0028887396 scopus 로고
    • Full-matrix refinement of the protein crambin at 0.83Å and 130K
    • Stec, B., Zhou, R. & Teeter, M.M. (1995). Full-matrix refinement of the protein crambin at 0.83Å and 130K. Acta Cryst. D 51, 663-681.
    • (1995) Acta Cryst. D , vol.51 , pp. 663-681
    • Stec, B.1    Zhou, R.2    Teeter, M.M.3
  • 29
    • 0025186647 scopus 로고
    • Atomic charges for DNA constituents derived from single-crystal X-ray diffraction data
    • Pearlman, D.A. & Kim, S.-H. (1990). Atomic charges for DNA constituents derived from single-crystal X-ray diffraction data. J. Mol. Biol. 211, 171-187.
    • (1990) J. Mol. Biol. , vol.211 , pp. 171-187
    • Pearlman, D.A.1    Kim, S.-H.2
  • 30
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. & Petsko, G.A. (1990). Molecular dynamics simulations in biology. Nature 347, 631-639.
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 31
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988). Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229, 317-324.
    • (1988) FEBS Lett. , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 32
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to a 1.5Å resolution structure of crambin
    • Brünger, A.T., Karplus, M. & Petsko, G.A. (1989). Crystallographic refinement by simulated annealing: application to a 1.5Å resolution structure of crambin. Acta Cryst. A 45, 50-61.
    • (1989) Acta Cryst. A , vol.45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 33
    • 0025304137 scopus 로고
    • Refinement of the influenza virus haemagglutinin by simulated annealing
    • Weis, W.I., Brünger, A.T., Skehel, J.J. & Wiley, D.C. (1989). Refinement of the influenza virus haemagglutinin by simulated annealing. J. Mol. Biol. 212, 737-761.
    • (1989) J. Mol. Biol. , vol.212 , pp. 737-761
    • Weis, W.I.1    Brünger, A.T.2    Skehel, J.J.3    Wiley, D.C.4
  • 34
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T., Krukowski, A. & Erickson, J. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A 46, 585-593.
    • (1990) Acta Cryst. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.3
  • 35
    • 0009550579 scopus 로고
    • Testing the method of crystallographic refinement using molecular dynamics
    • Fujinaga, M., Gros, P. & van Gunsteren, W.F. (1989). Testing the method of crystallographic refinement using molecular dynamics. J. Appl. Cryst. 22, 1-8.
    • (1989) J. Appl. Cryst. , vol.22 , pp. 1-8
    • Fujinaga, M.1    Gros, P.2    Van Gunsteren, W.F.3
  • 36
    • 84977296485 scopus 로고
    • The refinement of southern bean mosaic virus in reciprocal space
    • Silva, A.M. & Rossmann, M.G. (1985). The refinement of southern bean mosaic virus in reciprocal space. Acta Cryst. B 41, 147-157.
    • (1985) Acta Cryst. B , vol.41 , pp. 147-157
    • Silva, A.M.1    Rossmann, M.G.2
  • 37
    • 0000771669 scopus 로고
    • Structure-factor probabilities for related structures
    • Read, R.J. (1990). Structure-factor probabilities for related structures. Acta Cryst. A 46, 900-912.
    • (1990) Acta Cryst. A , vol.46 , pp. 900-912
    • Read, R.J.1
  • 38
    • 0000801550 scopus 로고
    • A multisolution method of phase determination by combined maximization of entropy and likelihood. III. Extension to powder diffraction data
    • Bricogne, G. (1991). A multisolution method of phase determination by combined maximization of entropy and likelihood. III. Extension to powder diffraction data. Acta Cryst. A 47, 803-829.
    • (1991) Acta Cryst. A , vol.47 , pp. 803-829
    • Bricogne, G.1
  • 39
    • 0001936036 scopus 로고
    • Direct phase determination by entropy maximization and likelihood ranking: Status report and perspectives
    • Bricogne, G. (1993). Direct phase determination by entropy maximization and likelihood ranking: status report and perspectives. Acta Cryst. D 49, 37-60.
    • (1993) Acta Cryst. D , vol.49 , pp. 37-60
    • Bricogne, G.1
  • 40
    • 0030586823 scopus 로고    scopus 로고
    • Cross-validation in crystallography: Practice and applications
    • Kleywegt, G.J. & Brünger, A.T. (1996). Cross-validation in crystallography: practice and applications. Structure 4, 897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 41
    • 0000939457 scopus 로고
    • The three-dimensional structure of a-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G.M., Nilges, M., Sukumaran, D.K., Brünger, A.T., Karplus, M. & Gronenborn, A.M. (1986). The three-dimensional structure of a-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. EMBO J. 5, 2729-2735.
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Sukumaran, D.K.3    Brünger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 42
    • 0030271733 scopus 로고    scopus 로고
    • Structure calculation from NMR data
    • Nilges, M. (1996). Structure calculation from NMR data. Curr. Opin. Struct. Biol. 6, 617-623.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 617-623
    • Nilges, M.1
  • 43
    • 12244297937 scopus 로고
    • Vicinal proton coupling in nuclear magnetic resonance
    • Karplus, M. (1963). Vicinal proton coupling in nuclear magnetic resonance. J. Am. Chem. Soc. 85, 2870-2871.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2870-2871
    • Karplus, M.1
  • 44
    • 0242330905 scopus 로고
    • Three-dimensional protein structure by NMR
    • Wiley, NY
    • Wüthrich, K. (1986). Three-dimensional protein structure by NMR. In NMR of Proteins and Nucleic Acids, pp. 176-199, Wiley, NY.
    • (1986) NMR of Proteins and Nucleic Acids , pp. 176-199
    • Wüthrich, K.1
  • 45
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulfide connectivities
    • Nilges, M. (1995). Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulfide connectivities. J. Mol. Biol. 245, 645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 46
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim, Y. & Prestegard, J.H. (1990). Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins 8, 377-385.
    • (1990) Proteins , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 47
    • 0028432974 scopus 로고
    • The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR
    • Garrett, D.S., et al., & Clore, G.M. (1994). The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR. J Magn. Resonance Ser. B 104, 99-103.
    • (1994) J Magn. Resonance Ser. B , vol.104 , pp. 99-103
    • Garrett, D.S.1    Clore, G.M.2
  • 48
    • 0028379642 scopus 로고
    • Coupling constants again: Experimental restraints in structure refinement
    • Mierke, D.F., Huber, T. & Kessler, H. J. (1994). Coupling constants again: experimental restraints in structure refinement. Comput. Aided Mol. Des. 8, 29-40.
    • (1994) Comput. Aided Mol. Des. , vol.8 , pp. 29-40
    • Mierke, D.F.1    Huber, T.2    Kessler, H.J.3
  • 49
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by NMR
    • Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1995). The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J. Magn. Resonance Ser. B 107, 293-297.
    • (1995) J. Magn. Resonance Ser. B , vol.107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 51
    • 0029283884 scopus 로고
    • Chemical shifts and three-dimensional protein structures
    • Oldfield, E. (1995). Chemical shifts and three-dimensional protein structures. J. Biomol. NMR 5, 217-225.
    • (1995) J. Biomol. NMR , vol.5 , pp. 217-225
    • Oldfield, E.1
  • 52
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988). Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints: application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38.
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 53
    • 0001549117 scopus 로고
    • Structure-factor least-squares refinement procedure for macromolecular structure using constrained and restrained parameters
    • Sussman, J.L., Holbrook, S.R., Church, G.M. & Kim, S.-H. (1977). Structure-factor least-squares refinement procedure for macromolecular structure using constrained and restrained parameters. Acta Cryst. A 33, 800-804.
    • (1977) Acta Cryst. A , vol.33 , pp. 800-804
    • Sussman, J.L.1    Holbrook, S.R.2    Church, G.M.3    Kim, S.-H.4
  • 54
    • 0000651098 scopus 로고
    • A real-space refinement procedure for proteins
    • Diamond, R. (1971). A real-space refinement procedure for proteins. Acta Cryst. A 27, 436-452.
    • (1971) Acta Cryst. A , vol.27 , pp. 436-452
    • Diamond, R.1
  • 55
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic structures by means of a conformational potential derived from structure databases
    • Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1996). Improving the quality of NMR and crystallographic structures by means of a conformational potential derived from structure databases. Protein Sci. 5, 1067-1080.
    • (1996) Protein Sci. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 56
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to a 2.8Å resolution structure of aspartate aminotransferase
    • Brünger, A.T. (1988). Crystallographic refinement by simulated annealing: application to a 2.8Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203, 803-816.
    • (1988) J. Mol. Biol. , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 57
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 58
    • 84944816485 scopus 로고
    • The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure
    • Arnold, E. & Rossmann, M.G. (1988). The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure. Acta Cryst. A 44, 270-282.
    • (1988) Acta Cryst. A , vol.44 , pp. 270-282
    • Arnold, E.1    Rossmann, M.G.2
  • 59
    • 12644262227 scopus 로고
    • Crystallographic refinement
    • (van Gunsteren, W.F., Weiner, P.K. & Wilkinsin, A.J., eds), ESCOM Science Publishers B.V., Leiden, Netherlands
    • Fujinaga, M. (1993). Crystallographic refinement. In Computer Simulation of Biomolecular Systems: Theoretical and Experimental Applications, (van Gunsteren, W.F., Weiner, P.K. & Wilkinsin, A.J., eds), pp. 371-381, ESCOM Science Publishers B.V., Leiden, Netherlands.
    • (1993) Computer Simulation of Biomolecular Systems: Theoretical and Experimental Applications , pp. 371-381
    • Fujinaga, M.1
  • 61
    • 22944467757 scopus 로고
    • Computer experiments on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules
    • Verlet, L. (1967). Computer experiments on classical fluids. I. Thermodynamical properties of Lennard-Jones molecules. Phys. Rev. 159, 98-105.
    • (1967) Phys. Rev. , vol.159 , pp. 98-105
    • Verlet, L.1
  • 62
    • 0003235926 scopus 로고
    • Computer simulation of multiple chain systems-the effect of density on the average chain dimension
    • Curro, J. (1974). Computer simulation of multiple chain systems-the effect of density on the average chain dimension. J. Chem. Phys. 61, 1203-1207.
    • (1974) J. Chem. Phys. , vol.61 , pp. 1203-1207
    • Curro, J.1
  • 63
    • 0027661179 scopus 로고
    • Metropolis Monte Carlo calculations of DNA structure using internal coordinates and NMR distance restraints: An alternative method for generating a high-resolution solution structure
    • Ulyanov, N.B., Schmitz, U. & James, T.L. (1993). Metropolis Monte Carlo calculations of DNA structure using internal coordinates and NMR distance restraints: an alternative method for generating a high-resolution solution structure. J. Biomol. NMR 3, 547-568.
    • (1993) J. Biomol. NMR , vol.3 , pp. 547-568
    • Ulyanov, N.B.1    Schmitz, U.2    James, T.L.3
  • 64
    • 0029353627 scopus 로고
    • Structure determination from NOESY intensities using a metropolis simulated-annealing (MSA) refinement of dihedral angles
    • Xu, Y. & Krishna, N.R. (1995). Structure determination from NOESY intensities using a metropolis simulated-annealing (MSA) refinement of dihedral angles. J. Mag. Resonance Ser. B. 108, 192-196.
    • (1995) J. Mag. Resonance Ser. B , vol.108 , pp. 192-196
    • Xu, Y.1    Krishna, N.R.2
  • 65
    • 11744387198 scopus 로고
    • Stochastic exploration of molecular mechanics energy surfaces. Hunting for the global minimum
    • Saunders, M. (1987). Stochastic exploration of molecular mechanics energy surfaces. Hunting for the global minimum. J. Am. Chem. Soc. 109, 3150-3152.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3150-3152
    • Saunders, M.1
  • 66
    • 0023430366 scopus 로고
    • Monte Carlo-minimization approach to the multiple-minima problem in protein folding
    • Li, Z. & Scheraga, H.A. (1987). Monte Carlo-minimization approach to the multiple-minima problem in protein folding. Proc. Natl. Acad. Sci. USA 84, 6611-6615.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.A.2
  • 67
    • 0026681839 scopus 로고
    • Optimal protocol and trajectory visualization for conformational searches of peptides and proteins
    • Abagyan, R. & Argos, P. (1992). Optimal protocol and trajectory visualization for conformational searches of peptides and proteins. J. Mol. Biol. 225, 519-532.
    • (1992) J. Mol. Biol. , vol.225 , pp. 519-532
    • Abagyan, R.1    Argos, P.2
  • 69
    • 84950199216 scopus 로고
    • A recursive formulation for constrained mechanical system dynamics: Part I. Open loop systems
    • Bae, D.-S. & Haug, E.J. (1987). A recursive formulation for constrained mechanical system dynamics: Part I. Open loop systems. Mech. Struct. Mach. 15, 359-382.
    • (1987) Mech. Struct. Mach. , vol.15 , pp. 359-382
    • Bae, D.-S.1    Haug, E.J.2
  • 70
    • 84941502604 scopus 로고
    • A recursive formulation for constrained mechanical system dynamics: Part II. Closed loop systems
    • Bae, D.-S. & Haug, E.J. (1988). A recursive formulation for constrained mechanical system dynamics: Part II. Closed loop systems. Mech. Struct. Mach. 15, 481-506.
    • (1988) Mech. Struct. Mach. , vol.15 , pp. 481-506
    • Bae, D.-S.1    Haug, E.J.2
  • 71
    • 0000040038 scopus 로고
    • A fast recursive algorithm for molecular dynamics simulation
    • Jain, A., Vaidehi, N. & Rodriguez, G. (1983). A fast recursive algorithm for molecular dynamics simulation. J. Comp. Phys. 106, 258-68.
    • (1983) J. Comp. Phys. , vol.106 , pp. 258-268
    • Jain, A.1    Vaidehi, N.2    Rodriguez, G.3
  • 72
    • 0028063256 scopus 로고
    • Protein simulations using techniques suitable for very large systems: The cell mulipole method for nonbond interactions and the Newton-Euler inverse mass operator method for internal coordinate dynamics
    • Mathiowetz, A.M., Jain, A., Karasawa, N. & Goddard, W.A. (1994). Protein simulations using techniques suitable for very large systems: the cell mulipole method for nonbond interactions and the Newton-Euler inverse mass operator method for internal coordinate dynamics. Proteins 20, 227-247.
    • (1994) Proteins , vol.20 , pp. 227-247
    • Mathiowetz, A.M.1    Jain, A.2    Karasawa, N.3    Goddard, W.A.4
  • 75
    • 0000443232 scopus 로고
    • Die Faltmolekülmethode - Eine neue Methode zur Bestimmung der Kristallstruktur bei ganz oder teilweise bekannter Molekülstruktur
    • Hoppe, W. (1957). Die Faltmolekülmethode - eine neue Methode zur Bestimmung der Kristallstruktur bei ganz oder teilweise bekannter Molekülstruktur. Acta Cryst. 10, 750-751.
    • (1957) Acta Cryst. , vol.10 , pp. 750-751
    • Hoppe, W.1
  • 76
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann, M.G. & Blow, D.M. (1962). The detection of sub-units within the crystallographic asymmetric unit. Acta Cryst. A 15, 24-51.
    • (1962) Acta Cryst. A , vol.15 , pp. 24-51
    • Rossmann, M.G.1    Blow, D.M.2
  • 77
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA-binding domains of human hnRNP A1 at 1.75Å resolution
    • in press
    • Shamoo, Y., Krueger, U., Rice, L.M., Williams, K.R. & Steitz, T.A. (1997). Crystal structure of the two RNA-binding domains of human hnRNP A1 at 1.75Å resolution. Nat. Struct. Biol., in press.
    • (1997) Nat. Struct. Biol.
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 78
    • 0025173665 scopus 로고
    • Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics
    • Gros, P., van Gunsteren, W.F. & Hol, W.G.J. (1990). Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics. Science 249, 1149-1152.
    • (1990) Science , vol.249 , pp. 1149-1152
    • Gros, P.1    Van Gunsteren, W.F.2    Hol, W.G.J.3
  • 79
    • 0023053635 scopus 로고
    • Effect of anisotropy and anharmonicity on protein crystallographic refinement
    • Kuriyan, J., Petsko, G.A., Levy, R.M. & Karplus, M. (1986). Effect of anisotropy and anharmonicity on protein crystallographic refinement. J. Mol. Biol. 190, 227-254.
    • (1986) J. Mol. Biol. , vol.190 , pp. 227-254
    • Kuriyan, J.1    Petsko, G.A.2    Levy, R.M.3    Karplus, M.4
  • 80
    • 0022486526 scopus 로고
    • Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A
    • Pflugrath, J.W., Wiegand, G., Huber, R. & Vertesey, L. (1986). Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. J. Mol. Biol. 189, 383-386.
    • (1986) J. Mol. Biol. , vol.189 , pp. 383-386
    • Pflugrath, J.W.1    Wiegand, G.2    Huber, R.3    Vertesey, L.4
  • 81
    • 0024300819 scopus 로고
    • Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)2 containing a stable purine-thymine base pair: Combined use of nuclear magnetic resonance and restrained molecular dynamics
    • Clore, G.M., et al., & Gronenborn, A.M. (1988). Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)2 containing a stable purine-thymine base pair: combined use of nuclear magnetic resonance and restrained molecular dynamics. Biochemistry 27, 4185-4197.
    • (1988) Biochemistry , vol.27 , pp. 4185-4197
    • Clore, G.M.1    Gronenborn, A.M.2
  • 82
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.