메뉴 건너뛰기




Volumn 2, Issue 5, 1997, Pages 295-306

Recovery of protein structure from contact maps

Author keywords

Contact; Distance; Dynamics; Map; Protein; Reconstruction

Indexed keywords

ALGORITHM; ARTICLE; CHEMICAL STRUCTURE; FORECASTING; METHODOLOGY; PROTEIN CONFORMATION; PROTEIN FOLDING; STEREOISOMERISM; THEORETICAL MODEL;

EID: 0030627407     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00041-2     Document Type: Article
Times cited : (212)

References (37)
  • 1
    • 0018543443 scopus 로고
    • Antiparallel and parallel beta strands differ in amino acids residue preferences
    • Lifson, S. & Sander, C. (1979). Antiparallel and parallel beta strands differ in amino acids residue preferences. Nature 282, 109-111.
    • (1979) Nature , vol.282 , pp. 109-111
    • Lifson, S.1    Sander, C.2
  • 2
    • 84985641098 scopus 로고
    • Effect of distance constraints on macromolecular conformation. II. Simulation of experimental results and theoretical predictions
    • Havel, T.F., Grippen, G.M. & Kuntz, I.D. (1979). Effect of distance constraints on macromolecular conformation. II. Simulation of experimental results and theoretical predictions. Biopolymers 18, 73-81.
    • (1979) Biopolymers , vol.18 , pp. 73-81
    • Havel, T.F.1    Grippen, G.M.2    Kuntz, I.D.3
  • 3
    • 0030443368 scopus 로고    scopus 로고
    • Protein fold recognition and dynamics in the space of contact maps
    • Mirny, L & Domany, E. (1996). Protein fold recognition and dynamics in the space of contact maps. Proteins 26, 391 -410.
    • (1996) Proteins , vol.26 , pp. 391-410
    • Mirny, L.1    Domany, E.2
  • 4
    • 0022429234 scopus 로고
    • An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformation in solution
    • Havel, T.F. & Wiithrich, K. (1985). An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformation in solution. J. Mol. Biol. 182, 281-294.
    • (1985) J. Mol. Biol. , vol.182 , pp. 281-294
    • Havel, T.F.1    Wiithrich, K.2
  • 5
    • 0000870109 scopus 로고
    • Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: Application to crambin
    • Brunger, 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. NatlAcad. Sci. USA 83, 3801-3805.
    • (1986) Proc. NatlAcad. Sci. USA , vol.83 , pp. 3801-3805
    • Brunger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Karplus, M.4
  • 6
    • 0027228364 scopus 로고
    • Protein structures from distance inequalities
    • Bohr, J., et al., & Petersen, E.F. (1993). Protein structures from distance inequalities. J. Mol. Biol. 231, 861-869.
    • (1993) J. Mol. Biol. , vol.231 , pp. 861-869
    • Bohr, J.1    Petersen, E.F.2
  • 7
    • 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, 645-650.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-650
    • Nilges, M.1
  • 8
    • 0029846867 scopus 로고    scopus 로고
    • Relationship between protein structure and geometrical constraints
    • Lund, O., Hansen, J., Brunak, S. & Bohr, J. (1996). Relationship between protein structure and geometrical constraints. Protein Sci. 5, 2217-2225.
    • (1996) Protein Sci. , vol.5 , pp. 2217-2225
    • Lund, O.1    Hansen, J.2    Brunak, S.3    Bohr, J.4
  • 9
    • 0030322828 scopus 로고    scopus 로고
    • Homology modelling by distance geometry
    • Aszódi, A. & Taylor, W R. (1996). Homology modelling by distance geometry. Fold. Des. 1, 325-334.
    • (1996) Fold. Des. , vol.1 , pp. 325-334
    • Aszódi, A.1    Taylor, W.R.2
  • 10
    • 0029610793 scopus 로고    scopus 로고
    • Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry
    • Mumenthaler, C. & Braun, W. (1996). Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry. J. Mol. Biol. 254, 465-480.
    • (1996) J. Mol. Biol. , vol.254 , pp. 465-480
    • Mumenthaler, C.1    Braun, W.2
  • 11
    • 0031575423 scopus 로고    scopus 로고
    • MONSSTER: A method for folding globular proteins with a small number of distance restraints
    • Skolnick, J., Kolinski, A. & Ortiz, A.R. (1997). MONSSTER: a method for folding globular proteins with a small number of distance restraints. J. Mol. Biol. 265, 217-241.
    • (1997) J. Mol. Biol. , vol.265 , pp. 217-241
    • Skolnick, J.1    Kolinski, A.2    Ortiz, A.R.3
  • 14
    • 0024821250 scopus 로고
    • Molecular dynamics simulation techniques fro determination of molecular structures from nuclear magnetic resonance data
    • Scheek, R.M., Van Gunsteren, W.F. & Kaptein, R. (1989). Molecular dynamics simulation techniques fro determination of molecular structures from nuclear magnetic resonance data. Methods Enzymol. 177, 204-218.
    • (1989) Methods Enzymol. , vol.177 , pp. 204-218
    • Scheek, R.M.1    Van Gunsteren, W.F.2    Kaptein, R.3
  • 15
    • 0031569392 scopus 로고    scopus 로고
    • New applications of simulated annealing in X-ray crystallography and solution NMR
    • Brünger, A.T., Adams, P.D. & Rice, U.M. (1997). New applications of simulated annealing in X-ray crystallography and solution NMR. Curr. Opin. Struct Biol. 5, 325-336.
    • (1997) Curr. Opin. Struct Biol. , vol.5 , pp. 325-336
    • Brünger, A.T.1    Adams, P.D.2    Rice, U.M.3
  • 16
    • 36849137515 scopus 로고
    • Monte Carlo calculation of the average extension of molecular chains
    • Rosenbluth, M.N. & Rosenbluth, A.W. (1955). Monte Carlo calculation of the average extension of molecular chains. J. Chem. Phys. 23, 356-359.
    • (1955) J. Chem. Phys. , vol.23 , pp. 356-359
    • Rosenbluth, M.N.1    Rosenbluth, A.W.2
  • 19
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V.I., Gutin, A.M. & Shakhnovich, E.I. (1995). Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 252, 460-471.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 21
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen, C. & Scheraga, H. (1975). Experimental and theoretical aspects of protein folding. Adv. Protein Chem. 29; 205-300.
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.1    Scheraga, H.2
  • 22
    • 0000787540 scopus 로고    scopus 로고
    • Modified configurational bias Monte Carlo for simulation of polymer systems
    • Vendruscolo, M. (1997). Modified configurational bias Monte Carlo for simulation of polymer systems. J. Chem. Phys. 106, 2970-2976.
    • (1997) J. Chem. Phys. , vol.106 , pp. 2970-2976
    • Vendruscolo, M.1
  • 23
    • 12944249776 scopus 로고
    • A discussion of the solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1978). A discussion of the solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 34, 827-828.
    • (1978) Acta Crystallogr. A , vol.34 , pp. 827-828
    • Kabsch, W.1
  • 24
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976). A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A 32, 922-923.
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 25
    • 0018350099 scopus 로고
    • Gene duplications in the structural evolution of chymotrypsin
    • McLachlan, A.D. (1979). Gene duplications in the structural evolution of chymotrypsin. J. Mol. Biol. 128, 49-79.
    • (1979) J. Mol. Biol. , vol.128 , pp. 49-79
    • McLachlan, A.D.1
  • 26
    • 33645655378 scopus 로고
    • On the prediction of protein structure: The significance of the root-mean-square deviation
    • Cohen, F.E. & Sternberg, M.J. (1980). On the prediction of protein structure: the significance of the root-mean-square deviation. J. Mol. Biol. 163, 613-621.
    • (1980) J. Mol. Biol. , vol.163 , pp. 613-621
    • Cohen, F.E.1    Sternberg, M.J.2
  • 29
    • 0023140044 scopus 로고
    • Multiple conformational states of proteins: Molecular dynamics of myoglobin
    • Eiber, R. & Karplus, M. (1987). Multiple conformational states of proteins: Molecular dynamics of myoglobin. Science 235, 318-321.
    • (1987) Science , vol.235 , pp. 318-321
    • Eiber, R.1    Karplus, M.2
  • 30
    • 0026320866 scopus 로고
    • The energy landscapes and motions in proteins
    • Frauenfelder, H., Sugar, S. & Wolynes, P.G. (1991). The energy landscapes and motions in proteins. Science 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sugar, S.2    Wolynes, P.G.3
  • 32
    • 3643138041 scopus 로고
    • Amorphous solid state of vulcanized macromolecules: A variational approach
    • Goldbart, P.M. & Zippelius, A. (1993). Amorphous solid state of vulcanized macromolecules: a variational approach. Phys. Rev. Lett. 71, 2256-2259.
    • (1993) Phys. Rev. Lett. , vol.71 , pp. 2256-2259
    • Goldbart, P.M.1    Zippelius, A.2
  • 33
    • 84957321964 scopus 로고
    • Distribution of localization lengths in randomly crosslinked macromolecular networks
    • Castillo, H.E., Goldbart, P.M. & Zippelius, A. (1994). Distribution of localization lengths in randomly crosslinked macromolecular networks. Europhys. Lett. 28, 519-524.
    • (1994) Europhys. Lett. , vol.28 , pp. 519-524
    • Castillo, H.E.1    Goldbart, P.M.2    Zippelius, A.3
  • 34
    • 6144238579 scopus 로고    scopus 로고
    • Entropie barriers, frustration and order: Basic ingredients in protein folding
    • Camacho, C.J. (1996). Entropie barriers, frustration and order: basic ingredients in protein folding. Phys. Rev. Lett. 77, 2324-2328.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 2324-2328
    • Camacho, C.J.1
  • 35
    • 0031579585 scopus 로고    scopus 로고
    • From collapse to freezing in random heteropolymers
    • Camacho, CJ. & Schanke, T. (1997)- From collapse to freezing in random heteropolymers. Europhys. Lett. 37, 603-608.
    • (1997) Europhys. Lett. , vol.37 , pp. 603-608
    • Camacho, C.J.1    Schanke, T.2
  • 36
    • 36448999542 scopus 로고
    • Statistical mechanics of polymers with distance constraints
    • Gutin, A.M. & Shakhnovich, E.I. (1994). Statistical mechanics of polymers with distance constraints. J. Chem. Phys. 100, 5290-5293.
    • (1994) J. Chem. Phys. , vol.100 , pp. 5290-5293
    • Gutin, A.M.1    Shakhnovich, E.I.2
  • 37
    • 3643104728 scopus 로고    scopus 로고
    • Internal constraints induce localization in an isolated polymer molecule
    • Bryngelson, J.D. & Thirumalai, D. Internal constraints induce localization in an isolated polymer molecule. Phys. Rev. Lett. 76, 542-546.
    • Phys. Rev. Lett. , vol.76 , pp. 542-546
    • Bryngelson, J.D.1    Thirumalai, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.