메뉴 건너뛰기




Volumn 11, Issue , 2010, Pages

A novel scoring function for discriminating hyperthermophilic and mesophilic proteins with application to predicting relative thermostability of protein mutants

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; HILL CLIMBING ALGORITHMS; IMPORTANT FEATURES; LINEAR COMBINATIONS; PREDICTION ACCURACY; RANDOM FOREST CLASSIFICATION; RELATIVE STABILITIES; THERMAL ADAPTATION;

EID: 77949517296     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-11-62     Document Type: Article
Times cited : (39)

References (53)
  • 2
    • 0033178831 scopus 로고    scopus 로고
    • In silico design for protein stabilization
    • 10.1016/S0958-1669(99)80070-6, 10449321
    • Dahiyat BI. In silico design for protein stabilization. Current Opinion in Biotechnology 1999, 10:387-390. 10.1016/S0958-1669(99)80070-6, 10449321.
    • (1999) Current Opinion in Biotechnology , vol.10 , pp. 387-390
    • Dahiyat, B.I.1
  • 3
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • 10.1126/science.1107387, 15879217
    • Korkegian A, Black ME, Baker D, Stoddard BL. Computational thermostabilization of an enzyme. Science 2005, 308:857-860. 10.1126/science.1107387, 15879217.
    • (2005) Science , vol.308 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 5
    • 59649107985 scopus 로고    scopus 로고
    • A Computational Approach for the Rational Design of Stable Proteins and Enzymes: Optimization of Surface Charge-Charge Interactions
    • Schweiker KL, Makhatadze GI. A Computational Approach for the Rational Design of Stable Proteins and Enzymes: Optimization of Surface Charge-Charge Interactions. Methods in Enzymology: Computer Methods 2009, 454(Pt A):175-211.
    • (2009) Methods in Enzymology: Computer Methods , vol.454 , Issue.PART A , pp. 175-211
    • Schweiker, K.L.1    Makhatadze, G.I.2
  • 7
    • 38149111171 scopus 로고    scopus 로고
    • Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins
    • 10.1007/s00726-007-0589-x, 17710363
    • Zhou XX, Wang YB, Pan YJ, Li WF. Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids 2008, 34:25-33. 10.1007/s00726-007-0589-x, 17710363.
    • (2008) Amino Acids , vol.34 , pp. 25-33
    • Zhou, X.X.1    Wang, Y.B.2    Pan, Y.J.3    Li, W.F.4
  • 8
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • 10.1110/ps.062130306, 2242557, 16815912
    • Razvi A, Scholtz JM. Lessons in stability from thermophilic proteins. Protein Science 2006, 15:1569-1578. 10.1110/ps.062130306, 2242557, 16815912.
    • (2006) Protein Science , vol.15 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 9
    • 0024974452 scopus 로고
    • Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices
    • 10.1016/0022-2836(89)90488-9, 2716053
    • Menendez-Arias L, Argos P. Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices. J Mol Biol 1989, 206:397-406. 10.1016/0022-2836(89)90488-9, 2716053.
    • (1989) J Mol Biol , vol.206 , pp. 397-406
    • Menendez-Arias, L.1    Argos, P.2
  • 10
    • 0034997442 scopus 로고    scopus 로고
    • Structural adaptation of enzymes to low temperatures
    • 10.1093/protein/14.3.141, 11342709
    • Gianese G, Argos P, Pascarella S. Structural adaptation of enzymes to low temperatures. Protein Eng 2001, 14:141-148. 10.1093/protein/14.3.141, 11342709.
    • (2001) Protein Eng , vol.14 , pp. 141-148
    • Gianese, G.1    Argos, P.2    Pascarella, S.3
  • 11
    • 0035027423 scopus 로고    scopus 로고
    • Patterns of temperature adaptation in proteins from the bacteria Deinococcus radiodurans and Thermus thermophilus
    • McDonald JH. Patterns of temperature adaptation in proteins from the bacteria Deinococcus radiodurans and Thermus thermophilus. Mol Biol Evol 2001, 18:741-749.
    • (2001) Mol Biol Evol , vol.18 , pp. 741-749
    • McDonald, J.H.1
  • 12
    • 0344687309 scopus 로고    scopus 로고
    • Analysis of thermal adaptation in the HSL enzyme family
    • 10.1016/j.jmb.2003.10.038, 14659763
    • Mandrich L, Pezzullo M, Del Vecchio P, Barone G, Rossi M, Manco G. Analysis of thermal adaptation in the HSL enzyme family. J Mol Biol 2004, 335:357-369. 10.1016/j.jmb.2003.10.038, 14659763.
    • (2004) J Mol Biol , vol.335 , pp. 357-369
    • Mandrich, L.1    Pezzullo, M.2    Del Vecchio, P.3    Barone, G.4    Rossi, M.5    Manco, G.6
  • 13
    • 62349120035 scopus 로고    scopus 로고
    • Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins
    • 10.1186/1471-2164-10-11, 2653534, 19133128
    • Metpally RP, Reddy BV. Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins. BMC Genomics 2009, 10:11. 10.1186/1471-2164-10-11, 2653534, 19133128.
    • (2009) BMC Genomics , vol.10 , pp. 11
    • Metpally, R.P.1    Reddy, B.V.2
  • 14
    • 33846519263 scopus 로고    scopus 로고
    • Protein and DNA sequence determinants of thermophilic adaptation
    • 10.1371/journal.pcbi.0030005, 1769408,1769408, 17222055
    • Zeldovich KB, Berezovsky IN, Shakhnovich EI. Protein and DNA sequence determinants of thermophilic adaptation. PLoS Comput Biol 2007, 3:e5. 10.1371/journal.pcbi.0030005, 1769408,1769408, 17222055.
    • (2007) PLoS Comput Biol , vol.3
    • Zeldovich, K.B.1    Berezovsky, I.N.2    Shakhnovich, E.I.3
  • 15
    • 34047232678 scopus 로고    scopus 로고
    • Positive and negative design in stability and thermal adaptation of natural proteins
    • Berezovsky IN, Zeldovich KB, Shakhnovich EI. Positive and negative design in stability and thermal adaptation of natural proteins. Plos Computational Biology 2007, 3:498-507.
    • (2007) Plos Computational Biology , vol.3 , pp. 498-507
    • Berezovsky, I.N.1    Zeldovich, K.B.2    Shakhnovich, E.I.3
  • 16
    • 0032715527 scopus 로고    scopus 로고
    • Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins
    • 10.1016/S0301-4622(99)00103-9, 10584295
    • Gromiha MM, Oobatake M, Sarai A. Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophysical Chemistry 1999, 82:51-67. 10.1016/S0301-4622(99)00103-9, 10584295.
    • (1999) Biophysical Chemistry , vol.82 , pp. 51-67
    • Gromiha, M.M.1    Oobatake, M.2    Sarai, A.3
  • 17
    • 0025369515 scopus 로고
    • A Comparative-Study of the Thermal-Stability of the Vertebrate Eye Lens - Antarctic Ice Fish to the Desert Iguana
    • 10.1016/0014-4835(90)90117-D, 2373164
    • Mcfallngai MJ, Horwitz J. A Comparative-Study of the Thermal-Stability of the Vertebrate Eye Lens - Antarctic Ice Fish to the Desert Iguana. Experimental Eye Research 1990, 50:703-709. 10.1016/0014-4835(90)90117-D, 2373164.
    • (1990) Experimental Eye Research , vol.50 , pp. 703-709
    • Mcfallngai, M.J.1    Horwitz, J.2
  • 18
    • 34247193011 scopus 로고    scopus 로고
    • Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles
    • 10.1186/1472-6807-7-18, 1851960, 17394655
    • Greaves RB, Warwicker J. Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles. Bmc Struct Biol 2007, 7:18. 10.1186/1472-6807-7-18, 1851960, 17394655.
    • (2007) Bmc Struct Biol , vol.7 , pp. 18
    • Greaves, R.B.1    Warwicker, J.2
  • 19
    • 60849137473 scopus 로고    scopus 로고
    • An expert system to predict protein thermostability using decision tree
    • Wu LC, Lee JX, Huang HD, Liu BJ, Horng JT. An expert system to predict protein thermostability using decision tree. Expert Syst Appl 2009, 36:9007-9014.
    • (2009) Expert Syst Appl , vol.36 , pp. 9007-9014
    • Wu, L.C.1    Lee, J.X.2    Huang, H.D.3    Liu, B.J.4    Horng, J.T.5
  • 20
    • 46249096540 scopus 로고    scopus 로고
    • Predicting protein thermostability changes from sequence upon multiple mutations
    • 10.1093/bioinformatics/btn166, 2718644, 18586713
    • Montanucci L, Fariselli P, Martelli PL, Casadio R. Predicting protein thermostability changes from sequence upon multiple mutations. Bioinformatics (Oxford, England) 2008, 24:I190-I195. 10.1093/bioinformatics/btn166, 2718644, 18586713.
    • (2008) Bioinformatics (Oxford, England) , vol.24
    • Montanucci, L.1    Fariselli, P.2    Martelli, P.L.3    Casadio, R.4
  • 21
    • 39749148317 scopus 로고    scopus 로고
    • Discrimination of mesophilic and thermophilic proteins using machine learning algorithms
    • Gromiha MM, Suresh MX. Discrimination of mesophilic and thermophilic proteins using machine learning algorithms. Proteins-Structure Function and Bioinformatics 2008, 70:1274-1279.
    • (2008) Proteins-Structure Function and Bioinformatics , vol.70 , pp. 1274-1279
    • Gromiha, M.M.1    Suresh, M.X.2
  • 22
    • 33749022803 scopus 로고    scopus 로고
    • Analysis of Nanoarchaeum equitans genome and proteome composition: indications for hyperthermophilic and parasitic adaptation
    • 10.1186/1471-2164-7-186, 1574309, 16869956
    • Das S, Paul S, Bag SK, Dutta C. Analysis of Nanoarchaeum equitans genome and proteome composition: indications for hyperthermophilic and parasitic adaptation. Bmc Genomics 2006, 7:186. 10.1186/1471-2164-7-186, 1574309, 16869956.
    • (2006) Bmc Genomics , vol.7 , pp. 186
    • Das, S.1    Paul, S.2    Bag, S.K.3    Dutta, C.4
  • 23
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • Haney PJ, Badger JH, Buldak GL, Reich CI, Woese CR, Olsen GJ. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. P Natl Acad Sci USA 1999, 96:3578-3583.
    • (1999) P Natl Acad Sci USA , vol.96 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 24
    • 32044454841 scopus 로고    scopus 로고
    • Effective factors in thermostability of thermophilic proteins
    • 10.1016/j.bpc.2005.09.018, 16253416
    • Sadeghi M, Naderi-Manesh H, Zarrabi M, Ranjbar B. Effective factors in thermostability of thermophilic proteins. Biophysical Chemistry 2006, 119:256-270. 10.1016/j.bpc.2005.09.018, 16253416.
    • (2006) Biophysical Chemistry , vol.119 , pp. 256-270
    • Sadeghi, M.1    Naderi-Manesh, H.2    Zarrabi, M.3    Ranjbar, B.4
  • 25
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • 10.1074/jbc.C000497200, 10940293
    • Cambillau C, Claverie JM. Structural and genomic correlates of hyperthermostability. J Biol Chem 2000, 275:32383-32386. 10.1074/jbc.C000497200, 10940293.
    • (2000) J Biol Chem , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 26
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • 10.1006/jmbi.1999.2810, 10373377
    • Xiao L, Honig B. Electrostatic contributions to the stability of hyperthermophilic proteins. Journal of Molecular Biology 1999, 289:1435-1444. 10.1006/jmbi.1999.2810, 10373377.
    • (1999) Journal of Molecular Biology , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 27
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: their classification and role in protein folding
    • 10.1093/protein/15.11.871, 12538906
    • George RA, Heringa J. An analysis of protein domain linkers: their classification and role in protein folding. Protein Eng 2002, 15:871-879. 10.1093/protein/15.11.871, 12538906.
    • (2002) Protein Eng , vol.15 , pp. 871-879
    • George, R.A.1    Heringa, J.2
  • 28
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • 10.1006/jmbi.1997.1042, 9217266
    • Vogt G, Woell S, Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol 1997, 269:631-643. 10.1006/jmbi.1997.1042, 9217266.
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 29
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • 10.1006/jmbi.1999.2889, 10390356
    • Thompson MJ, Eisenberg D. Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability. J Mol Biol 1999, 290:595-604. 10.1006/jmbi.1999.2889, 10390356.
    • (1999) J Mol Biol , vol.290 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 30
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey
    • 10.1016/S0969-2126(00)00133-7, 10801491
    • Szilagyi A, Zavodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 2000, 8:493-504. 10.1016/S0969-2126(00)00133-7, 10801491.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 31
    • 60549110049 scopus 로고    scopus 로고
    • Structural adaptation of the subunit interface of oligomeric thermophilic and hyperthermophilic enzymes
    • 10.1016/j.compbiolchem.2008.08.003, 18845483
    • Maugini E, Tronelli D, Bossa F, Pascarella S. Structural adaptation of the subunit interface of oligomeric thermophilic and hyperthermophilic enzymes. Computational biology and chemistry 2009, 33:137-148. 10.1016/j.compbiolchem.2008.08.003, 18845483.
    • (2009) Computational biology and chemistry , vol.33 , pp. 137-148
    • Maugini, E.1    Tronelli, D.2    Bossa, F.3    Pascarella, S.4
  • 32
    • 24644472817 scopus 로고    scopus 로고
    • Physics and evolution of thermophilic adaptation
    • 10.1073/pnas.0503890102, 1189736,1189736, 16120678
    • Berezovsky IN, Shakhnovich EI. Physics and evolution of thermophilic adaptation. Proc Natl Acad Sci USA 2005, 102:12742-12747. 10.1073/pnas.0503890102, 1189736,1189736, 16120678.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12742-12747
    • Berezovsky, I.N.1    Shakhnovich, E.I.2
  • 33
    • 43049097575 scopus 로고    scopus 로고
    • Experimental and theoretical studies of sodium cation complexes of the deamidation and dehydration products of asparagine, glutamine, aspartic acid, and glutamic acid
    • Heaton AL, Ye SJ, Armentrout PB. Experimental and theoretical studies of sodium cation complexes of the deamidation and dehydration products of asparagine, glutamine, aspartic acid, and glutamic acid. The journal of physical chemistry 2008, 112:3328-3338.
    • (2008) The journal of physical chemistry , vol.112 , pp. 3328-3338
    • Heaton, A.L.1    Ye, S.J.2    Armentrout, P.B.3
  • 35
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 37
    • 34548730241 scopus 로고    scopus 로고
    • Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms
    • 10.1093/bioinformatics/btm345, 17599925
    • Glyakina AV, Garbuzynskiy SO, Lobanov MY, Galzitskaya OV. Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms. Bioinformatics 2007, 23:2231-2238. 10.1093/bioinformatics/btm345, 17599925.
    • (2007) Bioinformatics , vol.23 , pp. 2231-2238
    • Glyakina, A.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3    Galzitskaya, O.V.4
  • 38
    • 0033214040 scopus 로고    scopus 로고
    • Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus
    • 10.1074/jbc.274.40.28453, 10497207
    • Haney PJ, Stees M, Konisky J. Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus. J Biol Chem 1999, 274:28453-28458. 10.1074/jbc.274.40.28453, 10497207.
    • (1999) J Biol Chem , vol.274 , pp. 28453-28458
    • Haney, P.J.1    Stees, M.2    Konisky, J.3
  • 39
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • 10.1006/jmbi.1999.3091, 10493868
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. Journal of molecular biology 1999, 292:195-202. 10.1006/jmbi.1999.3091, 10493868.
    • (1999) Journal of molecular biology , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 40
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: a protein structure and structural feature prediction server
    • 10.1093/nar/gki396, 1160157, 15980571
    • Cheng J, Randall AZ, Sweredoski MJ, Baldi P. SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res 2005, 33:W72-76. 10.1093/nar/gki396, 1160157, 15980571.
    • (2005) Nucleic Acids Res , vol.33
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 41
  • 42
    • 67349229243 scopus 로고    scopus 로고
    • Supervised machine learning algorithms for protein structure classification
    • 10.1016/j.compbiolchem.2009.04.004, 19473879
    • Jain P, Garibaldi JM, Hirst JD. Supervised machine learning algorithms for protein structure classification. Comput Biol Chem 2009, 33:216-223. 10.1016/j.compbiolchem.2009.04.004, 19473879.
    • (2009) Comput Biol Chem , vol.33 , pp. 216-223
    • Jain, P.1    Garibaldi, J.M.2    Hirst, J.D.3
  • 43
    • 60949104277 scopus 로고    scopus 로고
    • Predicting disordered regions in proteins using the profiles of amino acid indices
    • 10.1186/1471-2105-10-S1-S42, 2648739, 19208144
    • Han P, Zhang X, Feng ZP. Predicting disordered regions in proteins using the profiles of amino acid indices. Bmc Bioinformatics 2009, 10(Suppl 1):S42. 10.1186/1471-2105-10-S1-S42, 2648739, 19208144.
    • (2009) Bmc Bioinformatics , vol.10 , Issue.SUPPL 1
    • Han, P.1    Zhang, X.2    Feng, Z.P.3
  • 44
    • 0003802343 scopus 로고
    • Classification and Regression Trees
    • Norwell: Kluwer Academic Publishers
    • Breiman L, Friedman J, Olshen R, Stone C. Classification and Regression Trees. 1984, Norwell: Kluwer Academic Publishers.
    • (1984)
    • Breiman, L.1    Friedman, J.2    Olshen, R.3    Stone, C.4
  • 45
    • 32244442728 scopus 로고    scopus 로고
    • Discrimination of thermophilic and mesophilic proteins via pattern recognition methods
    • Zhang GY, Fang BS. Discrimination of thermophilic and mesophilic proteins via pattern recognition methods. Process Biochemistry 2006, 41:552-556.
    • (2006) Process Biochemistry , vol.41 , pp. 552-556
    • Zhang, G.Y.1    Fang, B.S.2
  • 46
    • 0002386913 scopus 로고
    • On the interpretation of χ2 from contingency tables, and the calculation of P
    • Fisher RA. On the interpretation of χ2 from contingency tables, and the calculation of P. Journal of the Royal Statistical Society 1922, 85:87-94.
    • (1922) Journal of the Royal Statistical Society , vol.85 , pp. 87-94
    • Fisher, R.A.1
  • 47
    • 0027270159 scopus 로고
    • Prediction of Protein Folding Class from Amino-Acid-Composition
    • 10.1002/prot.340160109, 8497486
    • Dubchak I, Holbrook SR, Kim SH. Prediction of Protein Folding Class from Amino-Acid-Composition. Proteins 1993, 16:79-91. 10.1002/prot.340160109, 8497486.
    • (1993) Proteins , vol.16 , pp. 79-91
    • Dubchak, I.1    Holbrook, S.R.2    Kim, S.H.3
  • 49
    • 33845679397 scopus 로고    scopus 로고
    • A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase
    • 10.1002/prot.21170, 17063493
    • Goihberg E, Dym O, Tel-Or S, Levin I, Peretz M, Burstein Y. A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase. Proteins 2007, 66:196-204. 10.1002/prot.21170, 17063493.
    • (2007) Proteins , vol.66 , pp. 196-204
    • Goihberg, E.1    Dym, O.2    Tel-Or, S.3    Levin, I.4    Peretz, M.5    Burstein, Y.6
  • 50
    • 84913591509 scopus 로고
    • Improved strategy in analytic surface calculation for molecular systems: Handling of singularities and computational efficiency
    • Frank Eisenhaber PA. Improved strategy in analytic surface calculation for molecular systems: Handling of singularities and computational efficiency. Journal of Computational Chemistry 1993, 14:1272-1280.
    • (1993) Journal of Computational Chemistry , vol.14 , pp. 1272-1280
    • Frank Eisenhaber, P.A.1
  • 52
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • 10.1093/bioinformatics/16.4.404, 10869041
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000, 16:404-405. 10.1093/bioinformatics/16.4.404, 10869041.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 53
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: implications for structural proteomics
    • 10.1016/j.str.2003.10.002, 14604535
    • Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, Russell RB. Protein disorder prediction: implications for structural proteomics. Structure 2003, 11:1453-1459. 10.1016/j.str.2003.10.002, 14604535.
    • (2003) Structure , vol.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5    Russell, R.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.