메뉴 건너뛰기




Volumn 265, Issue 2, 1997, Pages 217-241

MONSSTER: A method for folding globular proteins with a small number of distance restraints

Author keywords

Lattice models; NMR structure refinement; Protein folding; Protein modeling; Reduced protein models

Indexed keywords

FLAVODOXIN; GLOBULAR PROTEIN; MYOGLOBIN; PLASTOCYANIN;

EID: 0031575423     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0720     Document Type: Article
Times cited : (234)

References (34)
  • 1
    • 0029097099 scopus 로고
    • Global fold determination from a small number of distance restraints
    • Aszodi A., Gradwell M. J., Taylor W. R. Global fold determination from a small number of distance restraints. J. Mol. Biol. 248:1995;308-326.
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-326
    • Aszodi, A.1    Gradwell, M.J.2    Taylor, W.R.3
  • 3
    • 0022336792 scopus 로고
    • Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm
    • Braun W., Go N. Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. J. Mol. Biol. 186:1985;611-626.
    • (1985) J. Mol. Biol. , vol.186 , pp. 611-626
    • Braun, W.1    Go, N.2
  • 4
    • 0025277191 scopus 로고
    • The classification and origins of protein folding patterns
    • Chothia C., Finkelstein A. The classification and origins of protein folding patterns. Annu. Rev. Biochem. 59:1990;1007-1039.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 1007-1039
    • Chothia, C.1    Finkelstein, A.2
  • 5
    • 0027172878 scopus 로고
    • Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy
    • Clore G. M., Robien M. A., Gronenborn A. M. Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 231:1993;82-102.
    • (1993) J. Mol. Biol. , vol.231 , pp. 82-102
    • Clore, G.M.1    Robien, M.A.2    Gronenborn, A.M.3
  • 6
    • 0001222580 scopus 로고
    • Lattice representation of globular proteins: How good are they?
    • Godzik A., Kolinski A., Skolnick J. Lattice representation of globular proteins: how good are they? J. Comp. Chem. 14:1993;1194-1202.
    • (1993) J. Comp. Chem. , vol.14 , pp. 1194-1202
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 9
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the suporting programs CALIBA, HABAS and GLOMSA
    • Guentert P., Braun W., Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the suporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:1991;517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Guentert, P.1    Braun, W.2    Wuthrich, K.3
  • 10
    • 0021104996 scopus 로고
    • Structure of oxidized poplar plastocyanin at 1.6 Å resolution
    • Guss J. M., Freeman H. C. Structure of oxidized poplar plastocyanin at 1.6 Å resolution. J. Mol. Biol. 169:1983;521-563.
    • (1983) J. Mol. Biol. , vol.169 , pp. 521-563
    • Guss, J.M.1    Freeman, H.C.2
  • 11
    • 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., Wuthrich K. An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformation in solution. J. Mol. Biol. 182:1985;281-294.
    • (1985) J. Mol. Biol. , vol.182 , pp. 281-294
    • Havel, T.F.1    Wuthrich, K.2
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 0026581777 scopus 로고
    • Left handed topology of supersecondary structure formed by aligned α-helix and β-hairpin
    • Kajava A. V. Left handed topology of supersecondary structure formed by aligned α-helix and β-hairpin. FEBS Letters. 302:1992;8-10.
    • (1992) FEBS Letters , vol.302 , pp. 8-10
    • Kajava, A.V.1
  • 14
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti S. K., LeMaster D. M., Eklund H. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol. 212:1990;167-184.
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    Lemaster, D.M.2    Eklund, H.3
  • 15
    • 0028326042 scopus 로고
    • Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin
    • Kolinski A., Skolnick J. Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin. Proteins: Struct. Funct. Genet. 18:1994a;353-366.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 353-366
    • Kolinski, A.1    Skolnick, J.2
  • 16
    • 0028203492 scopus 로고
    • Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme
    • Kolinski A., Skolnick J. Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme. Proteins: Struct. Funct. Genet. 18:1994b;338-352.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 338-352
    • Kolinski, A.1    Skolnick, J.2
  • 18
    • 0011382187 scopus 로고    scopus 로고
    • A method for the prediction of surface "U"-turns and transglobular connections in small proteins
    • Kolinski A., Skolnick J., Godzik A. A method for the prediction of surface "U"-turns and transglobular connections in small proteins. Proteins: Struct. Funct. Genet. 1996;In the press.
    • (1996) Proteins: Struct. Funct. Genet
    • Kolinski, A.1    Skolnick, J.2    Godzik, A.3
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0023644998 scopus 로고
    • Structure of the C-terminal domain of the ribosomal protein 17/L12 from Escherichia coli at 1.7 Å resolution
    • Leijonmarck M., Liljas A. Structure of the C-terminal domain of the ribosomal protein 17/L12 from Escherichia coli at 1.7 Å resolution. J. Mol. Biol. 195:1987;555-579.
    • (1987) J. Mol. Biol. , vol.195 , pp. 555-579
    • Leijonmarck, M.1    Liljas, A.2
  • 21
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • Levitt M., Greer J. Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114:1977;181-293.
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-293
    • Levitt, M.1    Greer, J.2
  • 23
    • 0029610793 scopus 로고
    • Automated assignment of simulated and experimental NOESY spectra of proteins by feedback littering and self-correcting distance geometry
    • Mumenthaler C., Braun W. Automated assignment of simulated and experimental NOESY spectra of proteins by feedback littering and self-correcting distance geometry. J. Mol. Biol. 254:1995;465-480.
    • (1995) J. Mol. Biol. , vol.254 , pp. 465-480
    • Mumenthaler, C.1    Braun, W.2
  • 24
    • 0029987096 scopus 로고    scopus 로고
    • Does a backwardly read sequence have a unique native state?
    • Olszewski K. A., Kolinski A., Skolnick J. Does a backwardly read sequence have a unique native state? Protein Eng. 9:1996a;5-14.
    • (1996) Protein Eng. , vol.9 , pp. 5-14
    • Olszewski, K.A.1    Kolinski, A.2    Skolnick, J.3
  • 25
    • 0030018099 scopus 로고    scopus 로고
    • Folding simulations and computer redesign of protein A three helix bundle motifs
    • Olszewski K. A., Kolinski A., Skolnick J. Folding simulations and computer redesign of protein A three helix bundle motifs. Proteins: Struct. Funct. Genet. 25:1996b;286-299.
    • (1996) Proteins: Struct. Funct. Genet. , vol.25 , pp. 286-299
    • Olszewski, K.A.1    Kolinski, A.2    Skolnick, J.3
  • 27
    • 0027291015 scopus 로고
    • Prediction of secondary structure at better than 70% accuracy
    • Rost B., Sander C. Prediction of secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 28
    • 0017855552 scopus 로고
    • Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 Å resolution
    • Saul F. A., Amzel L. M., Poljak R. J. Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 Å resolution. J. Biol. Chem. 253:1978;585-597.
    • (1978) J. Biol. Chem. , vol.253 , pp. 585-597
    • Saul, F.A.1    Amzel, L.M.2    Poljak, R.J.3
  • 29
    • 85030284507 scopus 로고    scopus 로고
    • ftp.scripps.edu in directory /pub/skolnick/nmr
    • Skolnick, J. 1996, ftp.scripps.edu in directory /pub/skolnick/nmr.
    • (1996)
    • Skolnick, J.1
  • 30
    • 0011429236 scopus 로고    scopus 로고
    • Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation
    • Skolnick J., Jaroszewski L., Kolinski A., Godzik A. Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation. Protein Sci. 1996;In the press.
    • (1996) Protein Sci
    • Skolnick, J.1    Jaroszewski, L.2    Kolinski, A.3    Godzik, A.4
  • 31
    • 0017709121 scopus 로고
    • Structure of the semiquinone form of flavodoxin from Clostridium hp. Extension of 1.8 Å resolution and some comparisons of the oxidized state
    • Smith W. W., Burnett R. M., Darling G. D., Ludwig M. L. Structure of the semiquinone form of flavodoxin from Clostridium hp. Extension of 1.8 Å resolution and some comparisons of the oxidized state. J. Mol. Biol. 117:1977;195-225.
    • (1977) J. Mol. Biol. , vol.117 , pp. 195-225
    • Smith, W.W.1    Burnett, R.M.2    Darling, G.D.3    Ludwig, M.L.4
  • 32
    • 0027168790 scopus 로고
    • Global folding of proteins using a limited number of distance restraints
    • Smith-Brown M. J., Kominos D., Levy R. M. Global folding of proteins using a limited number of distance restraints. Protein Eng. 6:1993;605-614.
    • (1993) Protein Eng. , vol.6 , pp. 605-614
    • Smith-Brown, M.J.1    Kominos, D.2    Levy, R.M.3
  • 33
    • 0028290433 scopus 로고
    • Prediction of the folding pathways and structure of the GCN4 leucine zipper
    • Vieth M., Kolinski A., Brooks C. L., Skolnick J. Prediction of the folding pathways and structure of the GCN4 leucine zipper. J. Mol. Biol. 237:1994;361-367.
    • (1994) J. Mol. Biol. , vol.237 , pp. 361-367
    • Vieth, M.1    Kolinski, A.2    Brooks, C.L.3    Skolnick, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.