메뉴 건너뛰기




Volumn 9, Issue , 2009, Pages

Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIAL ENZYME; BURKHOLDERIA CEPACIA LIPASE; TOLUENE; UNCLASSIFIED DRUG; SOLVENT; TRIACYLGLYCEROL LIPASE; WATER;

EID: 67649548462     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-9-38     Document Type: Article
Times cited : (57)

References (76)
  • 4
    • 0036669425 scopus 로고    scopus 로고
    • Lipases for biotechnology
    • DOI 10.1016/S0958-1669(02)00341-5
    • Lipases for biotechnology. KE Jaeger T Eggert, Curr. Opin. Biotechnol 2002 13 390 397 12323363 (Pubitemid 35254099)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 390-397
    • Jaeger, K.-E.1    Eggert, T.2
  • 5
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and alpha/beta hydrolase fold
    • Lipases and alpha/beta hydrolase fold. JD Schrag M Cygler, Lipases, Part A 1997 284 85 107
    • (1997) Lipases, Part A , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 7
    • 0024538543 scopus 로고
    • How do serine proteases really work?
    • DOI 10.1021/bi00435a001
    • How Do Serine Proteases Really Work. A Warshel G Narayszabo F Sussman JK Hwang, Biochemistry 1989 28 3629 3637 2665806 (Pubitemid 19125405)
    • (1989) Biochemistry , vol.28 , Issue.9 , pp. 3629-3637
    • Warshel, A.1    Naray-Szabo, G.2    Sussman, F.3    Hwang, J.-K.4
  • 8
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: Facts and artifacts
    • DOI 10.1016/S0167-7799(96)10064-0, PII S0167779996100640
    • "Interfacial activation" of lipases: facts and artefacts. R Verger, Trends Biotechnol 1997 15 32 38 (Pubitemid 27067151)
    • (1997) Trends in Biotechnology , vol.15 , Issue.1 , pp. 32-38
    • Verger, R.1
  • 10
    • 0001406913 scopus 로고
    • Action de la Lipase Pancreatique sur les Esters en Emulsion
    • 13618257
    • Action De La Lipase Pancreatique Sur Les Esters En Emulsion. L Sarda P Desnuelle, Biochim Biophys Acta 1958 30 513 521 13618257
    • (1958) Biochim Biophys Acta , vol.30 , pp. 513-521
    • Sarda, L.1    Desnuelle, P.2
  • 11
    • 0018890516 scopus 로고
    • Enzyme kinetics of lipolysis
    • 7374455
    • Enzyme kinetics of lipolysis. R Verger, Methods Enzymol 1980 64 340 392 7374455
    • (1980) Methods Enzymol , vol.64 , pp. 340-392
    • Verger, R.1
  • 12
    • 0027200087 scopus 로고
    • Interfacial Activation of the Lipase Procolipase Complex by Mixed Micelles Revealed by X-Ray Crystallography
    • 8479519
    • Interfacial Activation of the Lipase Procolipase Complex by Mixed Micelles Revealed by X-Ray Crystallography. H Vantilbeurgh MP Egloff C Martinez N Rugani R Verger C Cambillau, Nature 1993 362 814 820 8479519
    • (1993) Nature , vol.362 , pp. 814-820
    • Vantilbeurgh, H.1    Egloff, M.P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 13
  • 17
    • 0030596528 scopus 로고    scopus 로고
    • Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 resolution
    • DOI 10.1006/jmbi.1996.0352
    • Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstrom resolution. D Lang B Hofmann L Haalck HJ Hecht F Spener RD Schmid D Schomburg, J Mol Biol 1996 259 704 717 8683577 (Pubitemid 26226011)
    • (1996) Journal of Molecular Biology , vol.259 , Issue.4 , pp. 704-717
    • Lang, D.1    Hofmann, B.2    Haalck, L.3    Hecht, H.-J.4    Spener, F.5    Schmid, R.D.6    Schomburg, D.7
  • 18
    • 0024299305 scopus 로고
    • A Model for the Molecular Mechanism of Interfacial Activation of Phospholipase-A2 Supporting the Substrate Theory
    • 3345843
    • A Model for the Molecular Mechanism of Interfacial Activation of Phospholipase-A2 Supporting the Substrate Theory. T Thuren, FEBS Lett 1988 229 95 99 3345843
    • (1988) FEBS Lett , vol.229 , pp. 95-99
    • Thuren, T.1
  • 19
    • 0015884950 scopus 로고
    • Catalysis by Adsorbed Enzymes - Hydrolysis of Tripropionin by Pancreatic Lipase Adsorbed to Siliconized Glass Beads
    • 4736887
    • Catalysis by Adsorbed Enzymes - Hydrolysis of Tripropionin by Pancreatic Lipase Adsorbed to Siliconized Glass Beads. HL Brockman JH Law FJ Kezdy, J Biol Chem 1973 248 4965 4970 4736887
    • (1973) J Biol Chem , vol.248 , pp. 4965-4970
    • Brockman, H.L.1    Law, J.H.2    Kezdy, F.J.3
  • 20
    • 0028103723 scopus 로고
    • Conformational States of Candida-Rugosa Lipase
    • 8142901
    • Conformational States of Candida-Rugosa Lipase. P Grochulski Y Li JD Schrag M Cygler, Protein Sci 1994 3 82 91 8142901
    • (1994) Protein Sci , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 22
    • 0034613390 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases
    • Crystal structure of Pseudomonas aeruginosa lipase in the open conformation - The prototype for family I.1 of bacterial lipases. M Nardini DA Lang K Liebeton KE Jaeger BM Dijkstra, J Biol Chem 2000 275 31219 31225 10893416 (Pubitemid 30757785)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.40 , pp. 31219-31225
    • Nardini, M.1    Lang, D.A.2    Liebeton, K.3    Jaeger, K.-E.4    Dijkstra, B.W.5
  • 23
    • 0034828837 scopus 로고    scopus 로고
    • Complex of burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: Biocatalytic, structural and modelling study
    • DOI 10.1046/j.1432-1327.2001.02303.x
    • Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane - Biocatalytic, structural and modelling study. M Luic S Tomic I Lescic E Ljubovic D Sepac V Sunjic L Vitale W Saenger B Kojic-Prodic, Eur J Biochem 2001 268 3964 3973 11453990 (Pubitemid 32868609)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.14 , pp. 3964-3973
    • Luic, M.1    Tomic, S.2    Lescic, I.3    Ljubovic, E.4    Sepac, D.5    Sunjic, V.6    Vitale, L.7    Saenger, W.8    Kojic-Prodic, B.9
  • 24
    • 17844410348 scopus 로고    scopus 로고
    • Mirror-image packing in enantiomer discrimination: Molecular basis for the enantioselectivity of B. cepacia lipase toward 2-methyl-3-phenyl-1-propanol
    • DOI 10.1016/j.chembiol.2005.01.016
    • Mirror-image packing in enantiomer discrimination: Molecular basis for the enantioselectivity of B-cepacia lipase toward 2-methyl-3-phenyl-1-propanol. A Mezzetti JD Schrag CS Cheong RJ Kazlauskas, Chem Biol 2005 12 427 437 15850979 (Pubitemid 40588917)
    • (2005) Chemistry and Biology , vol.12 , Issue.4 , pp. 427-437
    • Mezzetti, A.1    Schrag, J.D.2    Cheong, C.S.3    Kazlauskas, R.J.4
  • 26
    • 0028146056 scopus 로고
    • Molecular dynamics simulations of an enzyme surrounded by vacuum, water, or a hydrophobic solvent
    • Molecular dynamics simulations of an enzyme surrounded by vacuum, water, or a hydrophobic solvent. M Norin F Haeffner K Hult O Edholm, Biophys J 1994 67 548 559 7948673 (Pubitemid 24235384)
    • (1994) Biophysical Journal , vol.67 , Issue.2 , pp. 548-559
    • Norin, M.1    Haeffner, F.2    Hult, K.3    Edholm, O.4
  • 27
    • 0032848986 scopus 로고    scopus 로고
    • Computational analysis of chain flexibility and fluctuations in Rhizomucor miehei lipase
    • Computational analysis of chain flexibility and fluctuations in Rhizomucor miehei lipase. GH Peters RP Bywater, Protein Eng 1999 12 747 754 10506284 (Pubitemid 29472081)
    • (1999) Protein Engineering , vol.12 , Issue.9 , pp. 747-754
    • Peters, G.H.1    Bywater, R.P.2
  • 28
    • 0033739140 scopus 로고    scopus 로고
    • Computational studies of essential dynamics of Pseudomonas cepacia lipase
    • Computational studies of essential dynamics of Pseudomonas cepacia lipase. J Lee SW Suh S Shin, J Biomol Struct Dyn 2000 18 297 309 11089650 (Pubitemid 30840161)
    • (2000) Journal of Biomolecular Structure and Dynamics , vol.18 , Issue.2 , pp. 297-309
    • Lee, J.1    Se Won Suh2    Shin, S.3
  • 29
    • 33645543400 scopus 로고    scopus 로고
    • Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase: Insights from Molecular Dynamics Simulations
    • 16110344
    • Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase: Insights from Molecular Dynamics Simulations. SL Cherukuvada ASN Seshasayee K Raghunathan S Anishetty G Pennathur, PLoS Comput Biol 2005 1 e28 16110344
    • (2005) PLoS Comput Biol , vol.1 , pp. 28
    • Cherukuvada, S.L.1    Seshasayee, A.S.N.2    Raghunathan, K.3    Anishetty, S.4    Pennathur, G.5
  • 30
    • 0036286862 scopus 로고    scopus 로고
    • Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations
    • Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations. MO Jensen TR Jensen K Kjaer T Bjornholm OG Mouritsen GH Peters, Biophys J 2002 83 98 111 12080103 (Pubitemid 34694723)
    • (2002) Biophysical Journal , vol.83 , Issue.1 , pp. 98-111
    • Jensen, M.O.1    Jensen, T.R.2    Kjaer, K.3    Bjornholm, T.4    Mouritsen, O.G.5    Peters, G.H.6
  • 32
    • 0031042532 scopus 로고    scopus 로고
    • Computational studies of the activation of lipases and the effect of a hydrophobic environment
    • Computational studies of the activation of lipases and the effect of a hydrophobic environment. GH Peters S Toxvaerd OH Olsen A Svendsen, Protein Eng 1997 10 137 147 9089813 (Pubitemid 27113276)
    • (1997) Protein Engineering , vol.10 , Issue.2 , pp. 137-147
    • Peters, G.H.1    Toxvaerd, S.2    Olsen, O.H.3    Svendsen, A.4
  • 33
    • 0039554797 scopus 로고    scopus 로고
    • Conformational change in the activation of lipase: An analysis in terms of low-frequency normal modes
    • Conformational change in the activation of lipase: An analysis in terms of low-frequency normal modes. S Jaaskelainen CS Verma RE Hubbard P Linko LSD Caves, Protein Sci 1998 7 1359 1367 9655340 (Pubitemid 28272904)
    • (1998) Protein Science , vol.7 , Issue.6 , pp. 1359-1367
    • Jaaskelainen, S.1    Verma, C.S.2    Hubbard, R.E.3    Linko, P.4    Caves, L.S.D.5
  • 34
    • 0029933809 scopus 로고    scopus 로고
    • Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase
    • Theoretical investigation of the dynamics of the active site lid in Rhizomucor miehei lipase. GH Peters OH Olsen A Svendsen RC Wade, Biophys J 1996 71 119 129 8804595 (Pubitemid 26227298)
    • (1996) Biophysical Journal , vol.71 , Issue.1 , pp. 119-129
    • Peters, G.H.1    Olsen, O.H.2    Svendsen, A.3    Wade, R.C.4
  • 36
    • 2542506051 scopus 로고    scopus 로고
    • The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
    • The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor. KK Kim HK Song DH Shin KY Hwang SW Suh, Structure 1997 5 173 185 9032073 (Pubitemid 27158725)
    • (1997) Structure , vol.5 , Issue.2 , pp. 173-185
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Sun, S.W.5
  • 37
    • 0030768420 scopus 로고    scopus 로고
    • Structure as basis for understanding interfacial properties of lipases
    • DOI 10.1016/S0076-6879(97)84003-7
    • Structure as basis for understanding interfacial properties of lipases. M Cygler JD Schrag, Lipases, Part A 1997 284 3 27 (Pubitemid 27381566)
    • (1997) Methods in Enzymology , vol.284 , pp. 3-27
    • Cycler, M.1    Schrag, J.D.2
  • 39
    • 0042386531 scopus 로고    scopus 로고
    • Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: Crystal structure of the lipase 2 isoenzyme at 1.97 A resolution
    • DOI 10.1016/j.jmb.2003.08.005
    • Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: Crystal structure of the lipase 2 isoenzyme at 1.97 angstrom resolution. JM Mancheno MA Pernas MJ Martinez B Ochoa ML Rua JA Hermoso, J Mol Biol 2003 332 1059 1069 14499609 (Pubitemid 37108799)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.5 , pp. 1059-1069
    • Mancheno, J.M.1    Pernas, M.A.2    Martinez, M.J.3    Ochoa, B.4    Rua, M.L.5    Hermoso, J.A.6
  • 40
    • 35348909085 scopus 로고    scopus 로고
    • Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation
    • DOI 10.1016/j.febslet.2007.09.048, PII S0014579307010307
    • Crystal structure of a family I.3 lipase from Pseudomonas sp MIS38 in a closed conformation. C Angkawidjaja DJ You H Matsumura K Kuwahara Y Koga K Takano S Kanaya, FEBS Lett 2007 581 5060 5064 17923123 (Pubitemid 47576086)
    • (2007) FEBS Letters , vol.581 , Issue.26 , pp. 5060-5064
    • Angkawidjaja, C.1    You, D.-j.2    Matsumura, H.3    Kuwahara, K.4    Koga, Y.5    Takano, K.6    Kanaya, S.7
  • 41
    • 0034681120 scopus 로고    scopus 로고
    • Interfacial control of lid opening in Thermomyces lanuginosa lipase
    • DOI 10.1021/bi991927i
    • Interfacial control of lid opening in Thermomyces lanuginosa lipase. Y Cajal A Svendsen V Girona SA Patkar MA Alsina, Biochemistry 2000 39 413 423 10631003 (Pubitemid 30056477)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 413-423
    • Cajal, Y.1    Svendsen, A.2    Girona, V.3    Patkar, S.A.4    Alsina, M.A.5
  • 42
    • 0028295251 scopus 로고
    • Conformational lability of lipases observed in the absence of an oil- water interface: Crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar
    • Conformational Lability of Lipases Observed in the Absence of an Oil-Water Interface - Crystallographic Studies of Enzymes from the Fungi Humicola-Lanuginosa and Rhizopus-Delemar. U Derewenda L Swenson YY Wei R Green PM Kobos R Joerger MJ Haas ZS Derewenda, J Lipid Res 1994 35 524 534 8014587 (Pubitemid 24081866)
    • (1994) Journal of Lipid Research , vol.35 , Issue.3 , pp. 524-534
    • Derewenda, U.1    Swenson, L.2    Wei, Y.3    Green, R.4    Kobos, P.M.5    Joerger, R.6    Haas, M.J.7    Derewenda, Z.S.8
  • 43
    • 0035193287 scopus 로고    scopus 로고
    • Influence of a lipid interface on protein dynamics in a fungal lipase
    • Influence of a lipid interface on protein dynamics in a fungal lipase. GH Peters RP Bywater, Biophys J 2001 81 3052 3065 11720974 (Pubitemid 33111458)
    • (2001) Biophysical Journal , vol.81 , Issue.6 , pp. 3052-3065
    • Peters, G.H.1    Bywater, R.P.2
  • 44
    • 0026645602 scopus 로고
    • Variability of Conformations at Crystal Contacts in Bpti Represent True Low-Energy Structures - Correspondence among Lattice Packing and Molecular-Dynamics Structures
    • 1384033
    • Variability of Conformations at Crystal Contacts in Bpti Represent True Low-Energy Structures - Correspondence among Lattice Packing and Molecular-Dynamics Structures. AA Kossiakoff M Randal J Guenot C Eigenbrot, Proteins 1992 14 65 74 1384033
    • (1992) Proteins , vol.14 , pp. 65-74
    • Kossiakoff, A.A.1    Randal, M.2    Guenot, J.3    Eigenbrot, C.4
  • 45
    • 0035960203 scopus 로고    scopus 로고
    • Conformational averaging in pK calculations: Improvement and limitations in prediction of ionization properties of proteins
    • DOI 10.1021/jp010949n
    • Conformational averaging in pK calculations: Improvement and limitations in prediction of ionization properties of proteins. A Koumanov A Karshikoff EP Friis TV Borchert, J Phys Chem B 2001 105 9339 9344 (Pubitemid 35338731)
    • (2001) Journal of Physical Chemistry B , vol.105 , Issue.38 , pp. 9339-9344
    • Koumanov, A.1    Karshikoff, A.2    Friis, E.P.3    Borchert, T.V.4
  • 46
    • 0029560442 scopus 로고
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility
    • DOI 10.1021/ja00156a001
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility. J Broos AJWG Visser JFJ Engbersen W Verboom A vanHoek DN Reinhoudt, J Am Chem Soc 1995 117 12657 12663 (Pubitemid 26037411)
    • (1995) Journal of the American Chemical Society , vol.117 , Issue.51 , pp. 12657-12663
    • Broos, J.1    Visser, A.J.W.G.2    Engbersen, J.F.J.3    Verboom, W.4    Van Hoek, A.5    Reinhoudt, D.N.6
  • 48
    • 0034374492 scopus 로고    scopus 로고
    • Modelling of enzyme properties in organic solvents
    • Modelling of enzyme properties in organic solvents. G Colombo G Ottolina G Carrea, Monatsh Chem 2000 131 527 547
    • (2000) Monatsh Chem , vol.131 , pp. 527-547
    • Colombo, G.1    Ottolina, G.2    Carrea, G.3
  • 49
    • 0037342275 scopus 로고    scopus 로고
    • Protein structure and dynamics in nonaqueous solvents: Insights from molecular dynamics simulation studies
    • Protein structure and dynamics in nonaqueous solvents: insights from molecular dynamics simulation studies. CM Soares VH Teixeira AM Baptista, Biophys J 2003 84 1628 1641 12609866 (Pubitemid 36322927)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1628-1641
    • Soares, C.M.1    Teixeira, V.H.2    Baptista, A.M.3
  • 50
    • 34247363159 scopus 로고    scopus 로고
    • Modeling hydration mechanisms of enzymes in nonpolar and polar organic solvents
    • DOI 10.1111/j.1742-4658.2007.05781.x
    • Modeling hydration mechanisms of enzymes in nonpolar and polar organic solvents. NM Micaelo CM Soares, FEBS J 2007 274 2424 2436 17419728 (Pubitemid 46633469)
    • (2007) FEBS Journal , vol.274 , Issue.9 , pp. 2424-2436
    • Micaelo, N.M.1    Soares, C.M.2
  • 51
    • 40449100818 scopus 로고    scopus 로고
    • Modeling structure and flexibility of Candida antarctica lipase B in organic solvents
    • 18254946
    • Modeling structure and flexibility of Candida antarctica lipase B in organic solvents. P Trodler J Pleiss, BMC Struct Biol 2008 8 9 18254946
    • (2008) BMC Struct Biol , vol.8 , pp. 9
    • Trodler, P.1    Pleiss, J.2
  • 52
    • 0026550733 scopus 로고
    • Catalysis at the Interface - the Anatomy of a Conformational Change in a Triglyceride Lipase
    • 1737010
    • Catalysis at the Interface - the Anatomy of a Conformational Change in a Triglyceride Lipase. U Derewenda AM Brzozowski DM Lawson ZS Derewenda, Biochemistry 1992 31 1532 1541 1737010
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 54
    • 0029926518 scopus 로고    scopus 로고
    • Dynamics of proteins in different solvent systems: Analysis of essential motion in lipases
    • Dynamics of proteins in different solvent systems: Analysis of essential motion in lipases. GH Peters DMF vanAalten O Edholm S Toxvaerd R Bywater, Biophys J 1996 71 2245 2255 8913568 (Pubitemid 26367693)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2245-2255
    • Peters, G.H.1    Van Aalten, D.M.F.2    Edholm, O.3    Toxvaerd, S.4    Bywater, R.5
  • 55
    • 34548429987 scopus 로고    scopus 로고
    • Activation of Candida rugosa lipase at alkane-aqueous interfaces: A molecular dynamics study
    • DOI 10.1016/j.febslet.2007.08.002, PII S0014579307008678
    • Activation of Candida rugosa lipase at alkane-aqueous interfaces: A molecular dynamics study. JJ James BS Lakshmi AS Seshasayee P Gautam, FEBS Lett 2007 581 4377 4383 17765226 (Pubitemid 47368194)
    • (2007) FEBS Letters , vol.581 , Issue.23 , pp. 4377-4383
    • James, J.J.1    Lakshmi, B.S.2    Seshasayee, A.S.N.3    Gautam, P.4
  • 56
    • 0043237705 scopus 로고    scopus 로고
    • Triggering loops and enzyme function: Identification of loops that trigger and modulate movements
    • DOI 10.1016/S0022-2836(03)00893-3
    • Triggering loops and enzyme function: Identification of loops that trigger and modulate movements. K Gunasekaran BY Ma R Nussinov, J Mol Biol 2003 332 143 159 12946353 (Pubitemid 36999737)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.1 , pp. 143-159
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 58
    • 0035808171 scopus 로고    scopus 로고
    • Analysis of conformational states of Candida rugosa lipase in solution: Implications for mechanism of interfacial activation and separation of open and closed forms
    • Analysis of conformational states of Candida rugosa lipase in solution: implications for mechanism of interfacial activation and separation of open and closed forms. NA Turner EC Needs JA Khan EN Vulfson, Biotechnol Bioeng 2001 72 108 118 11084600 (Pubitemid 32085899)
    • (2001) Biotechnology and Bioengineering , vol.72 , Issue.1 , pp. 108-118
    • Turner, N.A.1    Needs, E.C.2    Khan, J.A.3    Vulfson, E.N.4
  • 59
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. K Arnold L Bordoli J Kopp T Schwede, Bioinformatics 2006 22 195 201 16301204 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 63
    • 0031553664 scopus 로고    scopus 로고
    • On the pH memory of lyophilized compounds containing protein functional groups
    • DOI 10.1002/(SICI)1097-0290(19970205)53:3<345::AID-BIT14>3.0.CO;2-J
    • On the pH memory of lyophilized compounds containing protein functional groups. HR Costantino K Griebenow R Langer AM Klibanov, Biotechnol Bioeng 1997 53 345 348 18633990 (Pubitemid 27076430)
    • (1997) Biotechnology and Bioengineering , vol.53 , Issue.3 , pp. 345-348
    • Costantino, H.R.1    Griebenow, K.2    Langer, R.3    Klibanov, A.M.4
  • 64
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • 7761829
    • Classical electrostatics in biology and chemistry. B Honig A Nicholls, Science 1995 268 1144 1149 7761829
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 65
    • 32844457567 scopus 로고
    • Accurate Calculation of Hydration Free-Energies Using Macroscopic Solvent Models
    • Accurate Calculation of Hydration Free-Energies Using Macroscopic Solvent Models. D Sitkoff KA Sharp B Honig, J Phys Chem 1994 98 1978 1988
    • (1994) J Phys Chem , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 69
    • 33646940952 scopus 로고
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints - Molecular-Dynamics of N-Alkanes
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints - Molecular-Dynamics of N-Alkanes. JP Ryckaert G Ciccotti HJC Berendsen, J Comput Phys 1977 23 327 341
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 71
    • 0025398721 scopus 로고
    • What if - a Molecular Modeling and Drug Design Program
    • What If - a Molecular Modeling and Drug Design Program. G Vriend, J Mol Graphics 1990 8 52
    • (1990) J Mol Graphics , vol.8 , pp. 52
    • Vriend, G.1
  • 72
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure - Pattern-Recognition of Hydrogen-Bonded and Geometrical Features
    • 6667333
    • Dictionary of Protein Secondary Structure - Pattern-Recognition of Hydrogen-Bonded and Geometrical Features. W Kabsch C Sander, Biopolymers 1983 22 2577 2637 6667333
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 75
    • 0021691817 scopus 로고
    • Amino acid scale: Normalized consensus hydrophobicity scale
    • 6502707
    • Amino acid scale: Normalized consensus hydrophobicity scale. D Eisenberg E Schwarz M Komarony R Wall, J Mol Biol 1984 179 125 142 6502707
    • (1984) J Mol Biol , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komarony, M.3    Wall, R.4
  • 76
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 17517781
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. M Wiederstein MJ Sippl, Nucleic Acids Res 2007 35 W407 W410 17517781
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein, M.1    Sippl, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.