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Volumn 280, Issue 1, 2013, Pages 56-69

Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase i from Trichoderma harzianum: Deciphering the structural features of cellobiohydrolase catalytic activity

Author keywords

biomass; cellobiohydrolase; enzymatic hydrolysis; molecular dynamics; X ray structure

Indexed keywords

ALANINE; CELLOBIOHYDROLASE 1; FUNGAL ENZYME; GLUCOSIDE; TYROSINE; UNCLASSIFIED DRUG; VALINE;

EID: 84872039730     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12049     Document Type: Article
Times cited : (44)

References (68)
  • 1
    • 77953094162 scopus 로고    scopus 로고
    • Importance of carbon dioxide physiological forcing to future climate change
    • Cao L, Bala G, Caldeira K, Nemani R, &, Ban-Weiss G, (2010) Importance of carbon dioxide physiological forcing to future climate change. Proc Natl Acad Sci USA 107, 9513-9518.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9513-9518
    • Cao, L.1    Bala, G.2    Caldeira, K.3    Nemani, R.4    Ban-Weiss, G.5
  • 5
    • 45449111746 scopus 로고    scopus 로고
    • Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation of corn stover
    • Gao JM, Weng HB, Zhu DH, Yuan MX, Guan FX, &, Xi Y, (2008) Production and characterization of cellulolytic enzymes from the thermoacidophilic fungal Aspergillus terreus M11 under solid-state cultivation of corn stover. Bioresour Technol 99, 7623-7629.
    • (2008) Bioresour Technol , vol.99 , pp. 7623-7629
    • Gao, J.M.1    Weng, H.B.2    Zhu, D.H.3    Yuan, M.X.4    Guan, F.X.5    Xi, Y.6
  • 6
    • 44449092955 scopus 로고    scopus 로고
    • Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14
    • Zhou J, Wang YH, Chu J, Zhuang YP, Zhang SL, &, Yin P, (2008) Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14. Bioresour Technol 99, 6826-6833.
    • (2008) Bioresour Technol , vol.99 , pp. 6826-6833
    • Zhou, J.1    Wang, Y.H.2    Chu, J.3    Zhuang, Y.P.4    Zhang, S.L.5    Yin, P.6
  • 7
    • 44649133953 scopus 로고    scopus 로고
    • Culture-based strategies to enhance cellulase enzyme production from Trichoderma reesei RUT-C30 in bioreactor culture conditions
    • Ahamed A, &, Vermette P, (2008) Culture-based strategies to enhance cellulase enzyme production from Trichoderma reesei RUT-C30 in bioreactor culture conditions. Biochem Eng J 40, 399-407.
    • (2008) Biochem Eng J , vol.40 , pp. 399-407
    • Ahamed, A.1    Vermette, P.2
  • 8
    • 0031587296 scopus 로고    scopus 로고
    • The crystal structure of the catalytic core domain of endoglucanase i from Trichoderma reesei at 3.6 angstrom resolution, and a comparison with related enzymes
    • Kleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, &, Jones TA, (1997) The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 angstrom resolution, and a comparison with related enzymes. J Mol Biol 272, 383-397.
    • (1997) J Mol Biol , vol.272 , pp. 383-397
    • Kleywegt, G.J.1    Zou, J.Y.2    Divne, C.3    Davies, G.J.4    Sinning, I.5    Stahlberg, J.6    Reinikainen, T.7    Srisodsuk, M.8    Teeri, T.T.9    Jones, T.A.10
  • 9
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • (Gilbert H.J. Davies G.J. Henrissat B. & Svensson B. eds), The Royal Society of Chemistry, Cambridge, UK
    • Coutinho PM, &, Henrissat B, (1999) Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering (, Gilbert HJ, Davies GJ, Henrissat B, &, Svensson B, eds), pp. 3-12. The Royal Society of Chemistry, Cambridge, UK.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 10
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies GJ, Wilson KS, &, Henrissat B, (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321, 557-559.
    • (1997) Biochem J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 11
    • 0036897682 scopus 로고    scopus 로고
    • Microbial cellulose utilization: Fundamentals and biotechnology
    • (vol 66, pg 506, 2002)
    • Lynd LR, Weimer PJ, van Zyl WH, &, Pretorius IS, (2002) Microbial cellulose utilization: fundamentals and biotechnology (vol 66, pg 506, 2002). Microbiol Mol Biol Rev 66, 739-739.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 739-739
    • Lynd, L.R.1    Weimer, P.J.2    Van Zyl, W.H.3    Pretorius, I.S.4
  • 12
    • 84954875039 scopus 로고
    • The 1.4-beta-glucan cellobiohydrolases of Trichoderma reesei Qm-9414 - A new type of cellulolytic synergism
    • Fagerstam LG, &, Pettersson LG, (1980) The 1.4-beta-glucan cellobiohydrolases of Trichoderma reesei Qm-9414-a new type of cellulolytic synergism. FEBS Lett 119, 97-100.
    • (1980) FEBS Lett , vol.119 , pp. 97-100
    • Fagerstam, L.G.1    Pettersson, L.G.2
  • 14
    • 1942486976 scopus 로고    scopus 로고
    • Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O- and N-glycosylation pattern of Cel7A
    • Stals I, Sandra K, Geysens S, Contreras R, Van Beeumen J, &, Claeyssens M, (2004) Factors influencing glycosylation of Trichoderma reesei cellulases. I: postsecretorial changes of the O- and N-glycosylation pattern of Cel7A. Glycobiology 14, 713-724.
    • (2004) Glycobiology , vol.14 , pp. 713-724
    • Stals, I.1    Sandra, K.2    Geysens, S.3    Contreras, R.4    Van Beeumen, J.5    Claeyssens, M.6
  • 15
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis
    • Tomme P, Vantilbeurgh H, Pettersson G, Vandamme J, Vandekerckhove J, Knowles J, Teeri T, &, Claeyssens M, (1988) Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur J Biochem 170, 575-581.
    • (1988) Eur J Biochem , vol.170 , pp. 575-581
    • Tomme, P.1    Vantilbeurgh, H.2    Pettersson, G.3    Vandamme, J.4    Vandekerckhove, J.5    Knowles, J.6    Teeri, T.7    Claeyssens, M.8
  • 17
    • 0032577330 scopus 로고    scopus 로고
    • Ion-exchange chromatographic purification and quantitative analysis of Trichoderma reesei cellulases cellobiohydrolase I. II and endoglucanase II by fast protein liquid chromatography
    • Medve J, Lee D, &, Tjerneld F, (1998) Ion-exchange chromatographic purification and quantitative analysis of Trichoderma reesei cellulases cellobiohydrolase I. II and endoglucanase II by fast protein liquid chromatography. J Chromatogr A 808, 153-165.
    • (1998) J Chromatogr A , vol.808 , pp. 153-165
    • Medve, J.1    Lee, D.2    Tjerneld, F.3
  • 18
    • 0023132478 scopus 로고
    • Homologous domains in Trichoderma reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase i
    • Teeri TT, Lehtovaara P, Kauppinen S, Salovuori I, &, Knowles J, (1987) Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase I. Gene 51, 43-52.
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovuori, I.4    Knowles, J.5
  • 20
    • 0035861979 scopus 로고    scopus 로고
    • Family 7 cellobiohydrolases from Phanerochaete chrysosporium: Crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes
    • Munoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, &, Stahlberg J, (2001) Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes. J Mol Biol 314, 1097-1111.
    • (2001) J Mol Biol , vol.314 , pp. 1097-1111
    • Munoz, I.G.1    Ubhayasekera, W.2    Henriksson, H.3    Szabo, I.4    Pettersson, G.5    Johansson, G.6    Mowbray, S.L.7    Stahlberg, J.8
  • 21
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii
    • Grassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, &, Tuohy MG, (2004) Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Eur J Biochem 271, 4495-450622.
    • (2004) Eur J Biochem , vol.271 , pp. 4495-450622
    • Grassick, A.1    Murray, P.G.2    Thompson, R.3    Collins, C.M.4    Byrnes, L.5    Birrane, G.6    Higgins, T.M.7    Tuohy, M.G.8
  • 22
    • 48249145161 scopus 로고    scopus 로고
    • Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding
    • Parkkinen T, Koivula A, &, Rouvinen J, (2008) Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding. Protein Sci 17, 1383-1394.
    • (2008) Protein Sci , vol.17 , pp. 1383-1394
    • Parkkinen, T.1    Koivula, A.2    Rouvinen, J.3
  • 23
    • 0024962351 scopus 로고
    • Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei - A study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing
    • Kraulis PJ, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, &, Gronenborn AM, (1989) Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei-a study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing. Biochemistry 28, 7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 24
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase i from Trichoderma reesei
    • Divne C, Stahlberg J, Teeri TT, &, Jones TA, (1998) High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 275, 309-325.
    • (1998) J Mol Biol , vol.275 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 25
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr BK, Hsieh YL, Ganem B, &, Wilson DB, (1996) Identification of two functionally different classes of exocellulases. Biochemistry 35, 586-592.
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.L.2    Ganem, B.3    Wilson, D.B.4
  • 26
    • 0030606294 scopus 로고    scopus 로고
    • Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase i from Trichoderma reesei
    • Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, &, Jones TA, (1996) Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 264, 337-349.
    • (1996) J Mol Biol , vol.264 , pp. 337-349
    • Stahlberg, J.1    Divne, C.2    Koivula, A.3    Piens, K.4    Claeyssens, M.5    Teeri, T.T.6    Jones, T.A.7
  • 27
    • 77958103555 scopus 로고    scopus 로고
    • Trichoderma harzianum IOC-4038: A promising strain for the production of a cellulolytic complex with significant beta-glucosidase activity from sugarcane bagasse cellulignin
    • Castro AM, Pedro KC, Cruz JC, Ferreira MC, Leite SG, &, Pereira N Jr, (2010) Trichoderma harzianum IOC-4038: a promising strain for the production of a cellulolytic complex with significant beta-glucosidase activity from sugarcane bagasse cellulignin. Appl Biochem Biotechnol 162, 2111-2122.
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 2111-2122
    • Castro, A.M.1    Pedro, K.C.2    Cruz, J.C.3    Ferreira, M.C.4    Leite, S.G.5    Pereira Jr., N.6
  • 28
    • 0024402815 scopus 로고
    • Fungal cellulase systems. Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei
    • Claeyssens M, Van Tilbeurgh H, Tomme P, Wood TM, &, McRae SI, (1989) Fungal cellulase systems. Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei. Biochem J 261, 819-825.
    • (1989) Biochem J , vol.261 , pp. 819-825
    • Claeyssens, M.1    Van Tilbeurgh, H.2    Tomme, P.3    Wood, T.M.4    McRae, S.I.5
  • 30
    • 0021426650 scopus 로고
    • An assay for selective determination of exo-1,4,-β-glucanases in a mixture of cellulolytic enzymes
    • Deshpande MV, Eriksson K-E, &, Gran Pettersson L, (1984) An assay for selective determination of exo-1,4,-β-glucanases in a mixture of cellulolytic enzymes. Anal Biochem 138, 481-487.
    • (1984) Anal Biochem , vol.138 , pp. 481-487
    • Deshpande, M.V.1    Eriksson, K.-E.2    Gran Pettersson, L.3
  • 31
    • 0032777863 scopus 로고    scopus 로고
    • Inhibition of cellobiohydrolases from Trichoderma reesei. Synthesis and evaluation of some glucose-, cellobiose-, and cellotriose-derived hydroximolactams and imidazoles
    • Vonhoff S, Piens K, Pipelier M, Braet C, Claeyssens M, &, Vasella A, (1999) Inhibition of cellobiohydrolases from Trichoderma reesei. Synthesis and evaluation of some glucose-, cellobiose-, and cellotriose-derived hydroximolactams and imidazoles. Helv Chim Acta 82, 963-980.
    • (1999) Helv Chim Acta , vol.82 , pp. 963-980
    • Vonhoff, S.1    Piens, K.2    Pipelier, M.3    Braet, C.4    Claeyssens, M.5    Vasella, A.6
  • 32
    • 77955645816 scopus 로고    scopus 로고
    • Practical screening of purified cellobiohydrolases and endoglucanases with alpha-cellulose and specification of hydrodynamics
    • Jager G, Wu Z, Garschhammer K, Engel P, Klement T, Rinaldi R, Spiess AC, &, Buchs J, (2010) Practical screening of purified cellobiohydrolases and endoglucanases with alpha-cellulose and specification of hydrodynamics. Biotechnol Biofuels 3, 3-18.
    • (2010) Biotechnol Biofuels , vol.3 , pp. 3-18
    • Jager, G.1    Wu, Z.2    Garschhammer, K.3    Engel, P.4    Klement, T.5    Rinaldi, R.6    Spiess, A.C.7    Buchs, J.8
  • 33
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • Zhang YHP, Himmel ME, &, Mielenz JR, (2006) Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv 24, 452-481.
    • (2006) Biotechnol Adv , vol.24 , pp. 452-481
    • Zhang, Y.H.P.1    Himmel, M.E.2    Mielenz, J.R.3
  • 35
    • 0035543353 scopus 로고    scopus 로고
    • Do enzymatic hydrolyzability and simons' stain reflect the changes in the accessibility of lignocellulosic substrates to cellulase enzymes?
    • Esteghlalian AR, Bilodeau M, Mansfield SD, &, Saddler JN, (2001) Do enzymatic hydrolyzability and simons' stain reflect the changes in the accessibility of lignocellulosic substrates to cellulase enzymes? Biotechnol Prog 17, 1049-1054.
    • (2001) Biotechnol Prog , vol.17 , pp. 1049-1054
    • Esteghlalian, A.R.1    Bilodeau, M.2    Mansfield, S.D.3    Saddler, J.N.4
  • 36
    • 77950356429 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis
    • Arantes V, &, Saddler JN, (2010) Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis. Biotechnol Biofuels 3, 4.
    • (2010) Biotechnol Biofuels , vol.3 , pp. 4
    • Arantes, V.1    Saddler, J.N.2
  • 37
    • 79751535329 scopus 로고    scopus 로고
    • Cellulose accessibility limits the effectiveness of minimum cellulase loading on the efficient hydrolysis of pretreated lignocellulosic substrates
    • Arantes V, &, Saddler JN, (2011) Cellulose accessibility limits the effectiveness of minimum cellulase loading on the efficient hydrolysis of pretreated lignocellulosic substrates. Biotechnol Biofuels 4, 3.
    • (2011) Biotechnol Biofuels , vol.4 , pp. 3
    • Arantes, V.1    Saddler, J.N.2
  • 38
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
    • Jalak J, &, Vaeljamaee P, (2010) Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis. Biotechnol Bioeng 106, 871-883.
    • (2010) Biotechnol Bioeng , vol.106 , pp. 871-883
    • Jalak, J.1    Vaeljamaee, P.2
  • 39
    • 84865224370 scopus 로고    scopus 로고
    • Endo-exo synergism in cellulose hydrolysis revisited
    • Jalak J, Kurašin M, Teugjas H, &, Väljamäe P, (2012) Endo-exo synergism in cellulose hydrolysis revisited. J Biol Chem 287, 28802-28815.
    • (2012) J Biol Chem , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurašin, M.2    Teugjas, H.3    Väljamäe, P.4
  • 40
    • 36048972648 scopus 로고
    • Native cellulose: A composite of two distinct crystalline forms
    • Atalla RH, &, VanderHart DL, (1984) Native cellulose: a composite of two distinct crystalline forms. Science 223, 283-285.
    • (1984) Science , vol.223 , pp. 283-285
    • Atalla, R.H.1    Vanderhart, D.L.2
  • 41
    • 0000986657 scopus 로고
    • Band assignments in the Raman spectra of celluloses
    • Wiley JH, &, Atalla RH, (1987) Band assignments in the Raman spectra of celluloses. Carbohydr Res 160, 113-129.
    • (1987) Carbohydr Res , vol.160 , pp. 113-129
    • Wiley, J.H.1    Atalla, R.H.2
  • 42
    • 20244371467 scopus 로고    scopus 로고
    • The enzymatic susceptibility of cellulose microfibrils of the algal-bacterial type and the cotton-ramie type
    • Hayashi N, Sugiyama J, Okano T, &, Ishihara M, (1998) The enzymatic susceptibility of cellulose microfibrils of the algal-bacterial type and the cotton-ramie type. Carbohydr Res 305, 261-269.
    • (1998) Carbohydr Res , vol.305 , pp. 261-269
    • Hayashi, N.1    Sugiyama, J.2    Okano, T.3    Ishihara, M.4
  • 43
    • 77956177381 scopus 로고    scopus 로고
    • Xylooligomers are strong inhibitors of cellulose hydrolysis by enzymes
    • Qing Q, Yang B, &, Wyman CE, (2010) Xylooligomers are strong inhibitors of cellulose hydrolysis by enzymes. Bioresour Technol 101, 9624-9630.
    • (2010) Bioresour Technol , vol.101 , pp. 9624-9630
    • Qing, Q.1    Yang, B.2    Wyman, C.E.3
  • 45
    • 74149088159 scopus 로고    scopus 로고
    • Restriction of the enzymatic hydrolysis of steam-pretreated spruce by lignin and hemicellulose
    • Varnai A, Siika-aho M, &, Viikari L, (2010) Restriction of the enzymatic hydrolysis of steam-pretreated spruce by lignin and hemicellulose. Enzyme Microb Technol 46, 185-193.
    • (2010) Enzyme Microb Technol , vol.46 , pp. 185-193
    • Varnai, A.1    Siika-Aho, M.2    Viikari, L.3
  • 46
    • 0027651651 scopus 로고
    • Activity studies of 8 purified cellulases - Specificity, synergism, and binding domain effects
    • Irwin DC, Spezio M, Walker LP, &, Wilson DB, (1993) Activity studies of 8 purified cellulases-specificity, synergism, and binding domain effects. Biotechnol Bioeng 42, 1002-1013.
    • (1993) Biotechnol Bioeng , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 48
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of cellobiohydrolases is limited by the substrate
    • Kurasin M, &, Valjamae P, (2011) Processivity of cellobiohydrolases is limited by the substrate. J Biol Chem 286, 169-177.
    • (2011) J Biol Chem , vol.286 , pp. 169-177
    • Kurasin, M.1    Valjamae, P.2
  • 50
    • 0033485705 scopus 로고    scopus 로고
    • Acid hydrolosis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase i and endoglucanase i
    • Valjamae P, Sild V, Nutt A, Pettersson G, &, Johansson G, (1999) Acid hydrolosis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I. Eur J Biochem 266, 327-334.
    • (1999) Eur J Biochem , vol.266 , pp. 327-334
    • Valjamae, P.1    Sild, V.2    Nutt, A.3    Pettersson, G.4    Johansson, G.5
  • 51
    • 68149183734 scopus 로고    scopus 로고
    • Measuring the crystallinity index of cellulose by solid state C-13 nuclear magnetic resonance
    • Park S, Johnson DK, Ishizawa CI, Parilla PA, &, Davis MF, (2009) Measuring the crystallinity index of cellulose by solid state C-13 nuclear magnetic resonance. Cellulose 16, 641-647.
    • (2009) Cellulose , vol.16 , pp. 641-647
    • Park, S.1    Johnson, D.K.2    Ishizawa, C.I.3    Parilla, P.A.4    Davis, M.F.5
  • 53
    • 77956539734 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum
    • Colussi F, Textor LC, Serpa V, Maeda RN, Pereira N, &, Polikarpov I, (2010) Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum. Acta Crystallogr Sect F Struct Biol Cryst Commun 66, 1041-1044.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 1041-1044
    • Colussi, F.1    Textor, L.C.2    Serpa, V.3    Maeda, R.N.4    Pereira, N.5    Polikarpov, I.6
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr Pt A 276, 307-326.
    • (1997) Macromol Crystallogr Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, &, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 57
    • 13844301139 scopus 로고    scopus 로고
    • Direct incorporation of experimental phase information in model refinement
    • Skubak P, Murshudov GN, &, Pannu NS, (2004) Direct incorporation of experimental phase information in model refinement. Acta Crystallogr D Biol Crystallogr 60, 2196-2201.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2196-2201
    • Skubak, P.1    Murshudov, G.N.2    Pannu, N.S.3
  • 62
    • 33646794930 scopus 로고    scopus 로고
    • A simple clustering algorithm can be accurate enough for use in calculations of pKs in macromolecules
    • Myers J, Grothaus G, Narayanan S, &, Onufriev A, (2006) A simple clustering algorithm can be accurate enough for use in calculations of pKs in macromolecules. Proteins 63, 928-938.
    • (2006) Proteins , vol.63 , pp. 928-938
    • Myers, J.1    Grothaus, G.2    Narayanan, S.3    Onufriev, A.4
  • 63
    • 69949118458 scopus 로고    scopus 로고
    • PACKMOL: A package for building initial configurations for molecular dynamics simulations
    • Martinez L, Andrade R, Birgin EG, &, Martinez JM, (2009) PACKMOL: a package for building initial configurations for molecular dynamics simulations. J Comput Chem 30, 2157-2164.
    • (2009) J Comput Chem , vol.30 , pp. 2157-2164
    • Martinez, L.1    Andrade, R.2    Birgin, E.G.3    Martinez, J.M.4
  • 66
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N. log(N) method for Ewald sums in large systems
    • Darden T, York D, &, Pedersen L, (1993) Particle mesh Ewald: an N. log(N) method for Ewald sums in large systems. J Chem Phys 98, 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 67
    • 33646940952 scopus 로고    scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, &, Berendsen HJC, (1997) Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Chem 23, 327-341.
    • (1997) J Comput Chem , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.