메뉴 건너뛰기




Volumn 1278, Issue , 1997, Pages 62-71

Recent advances in molecular distance geometry

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84929624438     PISSN: 03029743     EISSN: 16113349     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (1)

References (20)
  • 2
    • 3743105692 scopus 로고
    • P. Siegerist, H. R. Haegi, and A. S. Dreiding
    • ed. A. Maruani and J. Serre, chapter From Mobile Molecules to their Symmetry Groups: A Computer Implemented Method, Elsevier Scientific Pubł. Co., Amsterdam, Holland
    • P. Floersheim, K. Wirth, M. K. Huber, D. Pazis. P. Siegerist, H. R. Haegi, and A. S. Dreiding. Symmetries and Properties of Non-Rigid Molecules, volume 23 of Studies in Physical and Theoretical Chemistry, ed. A. Maruani and J. Serre, chapter From Mobile Molecules to their Symmetry Groups: A Computer Implemented Method, pages 59-80. Elsevier Scientific Pubł. Co., Amsterdam, Holland, 1983.
    • (1983) Symmetries and Properties of Non-Rigid Molecules, volume 23 of Studies in Physical and Theoretical Chemistry , pp. 59-80
    • Floersheim, P.1    Wirth, K.2    Huber, M.K.3    Pazis, D.4
  • 4
    • 0000892481 scopus 로고
    • Stable calculation of coordinates from distance information
    • G. M. Crippen and T. F. Havel, Stable calculation of coordinates from distance information. Acta CrysŁ, A34:282-284, 1978.
    • (1978) Acta CrysŁ , vol.A34 , pp. 282-284
    • Crippen, G.M.1    Havel, T.F.2
  • 5
    • 49049123546 scopus 로고
    • Theory and practice of distance geometry
    • T. F. Havel, I. D. Kuntz, and G. M. Crippen. Theory and practice of distance geometry. Bull. Math. Biol., 45:665-720, 1983.
    • (1983) Bull. Math. Biol , vol.45 , pp. 665-720
    • Havel, T.F.1    Kuntz, I.D.2    Crippen, G.M.3
  • 6
    • 0011962258 scopus 로고
    • Chemical distance geometry: Current realization and future projection
    • G. M. Crippen. Chemical distance geometry: Current realization and future projection. J. Math. Chem., 6:307-324, 1991.
    • (1991) J. Math. Chem , vol.6 , pp. 307-324
    • Crippen, G.M.1
  • 8
    • 0026651557 scopus 로고
    • NMR structure determination in solution: A critique and comparison with X-ray crystallography
    • G. Wagner, S. Hyberts, and T. F. Havel. NMR structure determination in solution: A critique and comparison with X-ray crystallography. Ann. Rev. Biophys. Biomol. Struct., 21:167-198, 1992.
    • (1992) Ann. Rev. Biophys. Biomol. Struct , vol.21 , pp. 167-198
    • Wagner, G.1    Hyberts, S.2    Havel, T.F.3
  • 9
    • 0001761498 scopus 로고
    • Distance geometry in molecular modeling
    • K. B. Lipkowitz & D. B. Boyd, editor, F, VCH Publishers, New York, NY
    • J. M. Blaney and J. S. Dixon. Distance geometry in molecular modeling. In K. B. Lipkowitz & D. B. Boyd, editor, Reviews in Computational Chemistry, Vol. F, pages 299-335. VCH Publishers, New York, NY, 1994.
    • (1994) Reviews in Computational Chemistry, Vol , pp. 299-335
    • Blaney, J.M.1    Dixon, J.S.2
  • 10
    • 0026018780 scopus 로고
    • A new method for building protein conformations from sequence alignments with homologues of known structure
    • T. F. Havel and M. Snow. A new method for building protein conformations from sequence alignments with homologues of known structure. J. Mol. Biol., 217:1-7, 1991.
    • (1991) J. Mol. Biol , vol.217 , pp. 1-7
    • Havel, T.F.1    Snow, M.2
  • 11
    • 0027800451 scopus 로고
    • Predicting the structure of the flavodoxin from erchericia coli by homology modeling, distance geometry and molecular dynamics
    • T. F. Havel. Predicting the structure of the flavodoxin from erchericia coli by homology modeling, distance geometry and molecular dynamics. Molec. SimuL, 10:175-210, 1993.
    • (1993) Molec. SimuL , vol.10 , pp. 175-210
    • Havel, T.F.1
  • 12
    • 0025932859 scopus 로고
    • An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance
    • D. Nobel and T. L. Blundell, editors, Permagon Press, Oxford, England
    • T. F. Havel. An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. In D. Nobel and T. L. Blundell, editors, Progress in Biophysics and Molecular Biology, volume 56, pages 43-78. Permagon Press, Oxford, England, 1991.
    • (1991) Progress in Biophysics and Molecular Biology , vol.56 , pp. 43-78
    • Havel, T.F.1
  • 13
    • 84945617402 scopus 로고
    • The symmetry groups of nonrigid molecules
    • H. C. Longuet-Higgins. The symmetry groups of nonrigid molecules. Mol. Phys., 6:445-460, 1963.
    • (1963) Mol. Phys , vol.6 , pp. 445-460
    • Longuet-Higgins, H.C.1
  • 14
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded parallel coiled coil
    • E. K. O'Shea, J. D. Klemm, P. S. Kim, and T. Alber. X-ray structure of the GCN4 leucine zipper, a two-stranded parallel coiled coil. Science, 254:539-544, 1991.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 15
    • 0001518003 scopus 로고
    • Derivatives of the matrix exponential Mid their computation
    • I. Najfeld and T. F. Havel. Derivatives of the matrix exponential Mid their computation. Adv. Appl. Math., 16:321-375, 1995.
    • (1995) Adv. Appl. Math , vol.16 , pp. 321-375
    • Najfeld, I.1    Havel, T.F.2
  • 16
    • 0020441466 scopus 로고
    • Crystal structures of escherichia coli and lactobacillus casei dihydrofolate reductase refined at 1.7å resolution
    • J. T. Bolin, D. J. Filman, D. A, Matthews, R. C. Hamlin, and J. Kraut. Crystal structures of escherichia coli and lactobacillus casei dihydrofolate reductase refined at 1.7å resolution. J. Biol. Chem., 257:13650-13662, 1982.
    • (1982) J. Biol. Chem , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 17
    • 0001612915 scopus 로고
    • Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.δå resolution
    • J. Deisenhofer and W. Steigemann. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.δå resolution. Acta Cryst. B, 31:238-240, 1975.
    • (1975) Acta Cryst. B , vol.31 , pp. 238-240
    • Deisenhofer, J.1    Steigemann, W.2
  • 18
    • 0024821250 scopus 로고
    • Molecular dynamics simulation techniques for determination of molecular structures from nuclear magnetic resonance data
    • R. M. Scheek, W. F. van Gunsteren, and R. Kaptein. Molecular dynamics simulation techniques for determination of molecular structures from nuclear magnetic resonance data. Meth. Enzymol., 177:204-218, 1989.
    • (1989) Meth. Enzymol , vol.177 , pp. 204-218
    • Scheek, R.M.1    van Gunsteren, W.F.2    Kaptein, R.3
  • 19
    • 0000397955 scopus 로고
    • Why energy embedding works
    • G. M. Crippen. Why energy embedding works. J. Phys. Chem., 91:6341-6343, 1987.
    • (1987) J. Phys. Chem , vol.91 , pp. 6341-6343
    • Crippen, G.M.1
  • 20
    • 0022721330 scopus 로고
    • An approach to the multiple-minima problem by relaxing dimensionality
    • E. O. Purisima and H. A. Scheraga. An approach to the multiple-minima problem by relaxing dimensionality. Proc. Natl. Acad. Sci. USA, 83:2782-2786, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2782-2786
    • Purisima, E.O.1    Scheraga, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.