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Volumn 5, Issue 2, 1997, Pages 173-185

The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor

Author keywords

lipase; Pseudomonas cepacia; X ray structure

Indexed keywords

BACTERIA (MICROORGANISMS); BURKHOLDERIA CEPACIA; BURKHOLDERIA GLUMAE; CHROMOBACTERIUM; CHROMOBACTERIUM VISCOSUM; MAMMALIA; PSEUDOMONAS;

EID: 2542506051     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00177-9     Document Type: Article
Times cited : (306)

References (61)
  • 2
    • 4243794106 scopus 로고
    • The biocatalytic approach to the preparation of enantiomerically pure chiral building blocks
    • Santaniello, E., Ferraboschi, P., Grisenti, P. & Manzocchi, A. (1992). The biocatalytic approach to the preparation of enantiomerically pure chiral building blocks. Chem. Rev. 92, 1071-1140.
    • (1992) Chem. Rev. , vol.92 , pp. 1071-1140
    • Santaniello, E.1    Ferraboschi, P.2    Grisenti, P.3    Manzocchi, A.4
  • 4
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa
    • Kazlauskas, R.J., Weissfloch, A.N.E., Rappaport, A.T. & Cuccia, L.A. (1991 ). A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa. J. Org. Chem. 56, 2656-2665.
    • (1991) J. Org. Chem. , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Cuccia, L.A.4
  • 5
    • 0028134021 scopus 로고
    • A structural basis for the chiral preference of lipases
    • Cygler, M., et al., & Gupta, A.K. (1994). A structural basis for the chiral preference of lipases. J. Am. Chem. Soc. 116, 3180-3186.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 3180-3186
    • Cygler, M.1    Gupta, A.K.2
  • 6
    • 0028327132 scopus 로고
    • Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase
    • Grochulski, P., et al., & Cygler, M. (1994). Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry 33, 3494-3500.
    • (1994) Biochemistry , vol.33 , pp. 3494-3500
    • Grochulski, P.1    Cygler, M.2
  • 7
    • 0029417196 scopus 로고
    • Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols
    • Uppenberg, J., et al., & Jones, TA (1995). Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 34, 16838-16851.
    • (1995) Biochemistry , vol.34 , pp. 16838-16851
    • Uppenberg, J.1    Jones, T.A.2
  • 8
    • 0025057072 scopus 로고
    • A serine protease triad forms the catalytic center of a triacylglycerol lipase
    • Brady, L., et al., & Menge, U. (1990). A serine protease triad forms the catalytic center of a triacylglycerol lipase. Nature 343, 767-770.
    • (1990) Nature , vol.343 , pp. 767-770
    • Brady, L.1    Menge, U.2
  • 9
    • 0027336654 scopus 로고
    • 1.8 Å refined structure of the lipase from Geotrichum candidum
    • Schrag, J.D. & Cygler, M. (1993). 1.8 Å refined structure of the lipase from Geotrichum candidum. J. Mol. Biol. 230, 575-591.
    • (1993) J. Mol. Biol. , vol.230 , pp. 575-591
    • Schrag, J.D.1    Cygler, M.2
  • 10
    • 0026432669 scopus 로고
    • Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
    • Schrag, J.D., Li, Y., Wu, S. & Cygler, M. (1991). Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351, 761-764.
    • (1991) Nature , vol.351 , pp. 761-764
    • Schrag, J.D.1    Li, Y.2    Wu, S.3    Cygler, M.4
  • 11
    • 0027160452 scopus 로고
    • Insights into interfacial activation from an open structure of Candida rugosa lipase
    • Grochulski, P., et al., & Cygler, M. (1993). Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 268, 12843-12847.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12843-12847
    • Grochulski, P.1    Cygler, M.2
  • 12
    • 0028367597 scopus 로고
    • An unusual buried polar cluster in a family of fungal lipases
    • Derewenda, U., et al., & Derewenda, Z.S. (1994). An unusual buried polar cluster in a family of fungal lipases. Nat. Struct. Biol. 1, 36-47.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 36-47
    • Derewenda, U.1    Derewenda, Z.S.2
  • 13
    • 0028773288 scopus 로고
    • Tne sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg, J., Hansen, M.T., Patkar, S. & Jones, T.A (1994). Tne sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2, 293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 14
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler, F.K., D'Arcy, A. & Hunziker, W. (1990). Structure of human pancreatic lipase. Nature 343, 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 15
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complexes by mixed micelles revealed by X-ray crystallography
    • van Tilbeurgh, H., Egloff, M.-P., Martinez, C., Rugani, N., Verger, R. & Cambillau, C. (1993). Interfacial activation of the lipase-procolipase complexes by mixed micelles revealed by X-ray crystallography. Nature 362, 814-820.
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.-P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 17
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • Noble, M.E.M., Cleasby, A., Johnson, L.N., Egmond, M.R. & Frenken, L.G.J. (1993). The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett. 331, 123-128.
    • (1993) FEBS Lett. , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.J.5
  • 18
    • 0030596528 scopus 로고    scopus 로고
    • Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 Å resolution
    • Lang, D., et al., & Schomburg, D. (1996). Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 Å resolution. J. Mol. Biol. 259, 704-717.
    • (1996) J. Mol. Biol. , vol.259 , pp. 704-717
    • Lang, D.1    Schomburg, D.2
  • 20
    • 0026540411 scopus 로고
    • The α/β hydrolase fold
    • Ollis, D.L., et al., & Goldman, A. (1992). The α/β hydrolase fold. Protein Eng. 5, 197-211.
    • (1992) Protein Eng. , vol.5 , pp. 197-211
    • Ollis, D.L.1    Goldman, A.2
  • 21
    • 0024293455 scopus 로고
    • X-ray crystallographic structure of dienelactone hydrolase at 2.8 A
    • Pathak, D., Ngai, K.-L. & Ollis, D. (1988). X-ray crystallographic structure of dienelactone hydrolase at 2.8 A. J. Mol. Biol. 204, 435-445.
    • (1988) J. Mol. Biol. , vol.204 , pp. 435-445
    • Pathak, D.1    Ngai, K.-L.2    Ollis, D.3
  • 22
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L., et al., & Silman, I. (1991). Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Silman, I.2
  • 23
    • 0025734772 scopus 로고
    • Crystal structures of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken, S.M., Rozeboom, H.J., Kalk, K.H. & Dijkstra, B.W. (1991). Crystal structures of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. EMBO J. 10, 1297-1302.
    • (1991) EMBO J. , vol.10 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 24
    • 0026787333 scopus 로고
    • Refined atomic model of wheat serine carboxypeptidase II at 2.2 Å resolution
    • Liao, D.I., Breddam, K., Sweet, R.M., Bullock, T. & Remington, S.J. (1992). Refined atomic model of wheat serine carboxypeptidase II at 2.2 Å resolution. Biochemistry 31, 9796-9812.
    • (1992) Biochemistry , vol.31 , pp. 9796-9812
    • Liao, D.I.1    Breddam, K.2    Sweet, R.M.3    Bullock, T.4    Remington, S.J.5
  • 25
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez, C., Geus, P.D., Lauwereys, M., Matthyssens, G. & Cambillau, C. (1992). Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356, 615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    Geus, P.D.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 26
    • 0028141817 scopus 로고
    • Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi
    • Lawson, D.M., et al., & Derewenda, Z.S. (1994). Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry 33, 9382-9388.
    • (1994) Biochemistry , vol.33 , pp. 9382-9388
    • Lawson, D.M.1    Derewenda, Z.S.2
  • 27
    • 0029644244 scopus 로고
    • Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase
    • Ghosh, D., et al., & Duax, W.L. (1995). Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase. Structure 3, 279-288.
    • (1995) Structure , vol.3 , pp. 279-288
    • Ghosh, D.1    Duax, W.L.2
  • 28
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipase from the structure of a fungal lipase-inhibitor complex
    • Brzozowski, A.M., et al., & Thim, L. (1991). A model for interfacial activation in lipase from the structure of a fungal lipase-inhibitor complex. Nature 351, 491-494.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Thim, L.2
  • 29
    • 0028103723 scopus 로고
    • Two conformational states of Candida rugosa lipase
    • Grochulski, P., Li, Y., Schrag, J.D. & Cygler, M. (1994). Two conformational states of Candida rugosa lipase. Protein Sci. 3, 82-91.
    • (1994) Protein Sci. , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 30
    • 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
    • Derewenda, U., et al., & Derewenda, Z.S. (1994). 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. J. Lipid Res. 35, 524-534.
    • (1994) J. Lipid Res. , vol.35 , pp. 524-534
    • Derewenda, U.1    Derewenda, Z.S.2
  • 32
    • 0026007830 scopus 로고
    • Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: Lipase production in heterologous hosts requires two Pseudomonas genes
    • Jørgensen, S., Skov, K.W. & Diderichsen, B. (1991). Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes. J. Bacteriol. 173, 559-567.
    • (1991) J. Bacteriol. , vol.173 , pp. 559-567
    • Jørgensen, S.1    Skov, K.W.2    Diderichsen, B.3
  • 33
    • 0342768967 scopus 로고
    • Properties and purification of a Pseudomonas cepacia lipase
    • Alberghina, L., Schmid, R.D., & Verger, R., eds, GBF monographs, VCH, Weinheim, Germany
    • Dunhaupt, A., Lang, S. & Wagner, F. (1991). Properties and purification of a Pseudomonas cepacia lipase. In Lipase; Structure, Mechanism, and Genetic Engineering. (Alberghina, L., Schmid, R.D., & Verger, R., eds), pp. 389-392, GBF monographs, VCH, Weinheim, Germany.
    • (1991) Lipase; Structure, Mechanism, and Genetic Engineering , pp. 389-392
    • Dunhaupt, A.1    Lang, S.2    Wagner, F.3
  • 34
    • 0025914935 scopus 로고
    • Extracellular lipase of Pseudomonas sp. strain ATCC 21808: Purification, characterization, crystallization, and preliminary X-ray diffraction data
    • Kordel, M., Hofmann, B., Schomburg, D. & Schmid, R. D. (1991). Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-ray diffraction data. J. Bacteriol. 73, 4836-4841.
    • (1991) J. Bacteriol. , vol.73 , pp. 4836-4841
    • Kordel, M.1    Hofmann, B.2    Schomburg, D.3    Schmid, R.D.4
  • 35
    • 0003948322 scopus 로고
    • Lipase from Pseudomonas sp.: Reactions, cloning and amino acid sequence analysis
    • Alberghina, L., Verger, R., Schmid, R., eds, VCH, Weinheim, Germany
    • Nishioka, T., et al., & Oda, J. (1991). Lipase from Pseudomonas sp.: reactions, cloning and amino acid sequence analysis. In Lipase; Structure, Mechanism, and Genetic Engineering. (Alberghina, L., Verger, R., Schmid, R., eds), pp. 253-262, VCH, Weinheim, Germany.
    • (1991) Lipase; Structure, Mechanism, and Genetic Engineering , pp. 253-262
    • Nishioka, T.1    Oda, J.2
  • 36
    • 0026488315 scopus 로고
    • Purification and characterization of a novel thermostable lipase from Pseudomonas cepacia
    • Sugihara, A., Ueshima, M., Shimada, Y., Tsunasawa, S. & Tominaga, Y. (1992). Purification and characterization of a novel thermostable lipase from Pseudomonas cepacia. J. Biochem. 112, 598-603.
    • (1992) J. Biochem. , vol.112 , pp. 598-603
    • Sugihara, A.1    Ueshima, M.2    Shimada, Y.3    Tsunasawa, S.4    Tominaga, Y.5
  • 37
    • 0028111533 scopus 로고
    • Lipase of Pseudomonas cepacia for biotechnological purpose: Purification, crystallization and characterization
    • Bornscheuer, U., et al., & Menge, U. (1994). Lipase of Pseudomonas cepacia for biotechnological purpose: purification, crystallization and characterization. Biochim. Biophys. Acta 1201, 55-60.
    • (1994) Biochim. Biophys. Acta , vol.1201 , pp. 55-60
    • Bornscheuer, U.1    Menge, U.2
  • 38
    • 0026462716 scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of lipase from Pseudomonas cepacia
    • Kim, K.K., et al., & Suh, S.W. (1992). Crystallization and preliminary X-ray crystallographic analysis of lipase from Pseudomonas cepacia. J. Mol. Biol. 227, 1258-1262.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1258-1262
    • Kim, K.K.1    Suh, S.W.2
  • 39
    • 0242528545 scopus 로고
    • Enantiopreference of lipase from Pseudomonas cepacia toward primary alcohols
    • Weissfloch, A. & Kazlauskas, A. (1995). Enantiopreference of lipase from Pseudomonas cepacia toward primary alcohols. J. Org. Chem. 60, 6959-6969.
    • (1995) J. Org. Chem. , vol.60 , pp. 6959-6969
    • Weissfloch, A.1    Kazlauskas, A.2
  • 41
    • 0024235347 scopus 로고
    • Cloning, sequencing and expression of the lipase gene from Pseudomonas fragi IFO-12049 in E. coli
    • Aoyama, S., Yoshida, N. & Inouye, S. (1988). Cloning, sequencing and expression of the lipase gene from Pseudomonas fragi IFO-12049 in E. coli. FEBS Lett. 242, 36-40.
    • (1988) FEBS Lett. , vol.242 , pp. 36-40
    • Aoyama, S.1    Yoshida, N.2    Inouye, S.3
  • 42
    • 0026562254 scopus 로고
    • Cloning, expression, and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52
    • Tan, Y & Miller, K.J. (1992). Cloning, expression, and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52. Appl. Environ. Microbiol. 58, 1402-1407.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1402-1407
    • Tan, Y.1    Miller, K.J.2
  • 43
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner, S. (1988). The molecular evolution of genes and proteins: a tale of two serines. Nature 334, 528-530.
    • (1988) Nature , vol.334 , pp. 528-530
    • Brenner, S.1
  • 44
    • 0028075638 scopus 로고
    • Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties
    • Kazlauskas, R.J. (1994). Elucidating structure-mechanism relationships in lipases: prospects for predicting and engineering catalytic properties. Trends Biotechnol. 12, 464-472.
    • (1994) Trends Biotechnol. , vol.12 , pp. 464-472
    • Kazlauskas, R.J.1
  • 45
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U., Brzozowski, A.M., Lawson, D.M. & Derewenda, Z.S. (1992). Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry 31, 1532-1541.
    • (1992) Biochemistry , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 46
    • 0029161231 scopus 로고
    • The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate
    • Egloff, M.-P., Marguet, F., Buono, G., Verger, R., Cambillau, C. & van Tilbeurgh, H. (1995). The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34, 2751-2762.
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.-P.1    Marguet, F.2    Buono, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 47
    • 0027957435 scopus 로고
    • Cutinase, a lipolytic enzyme with a preformed oxyanion hole
    • Martinez, C., et al., & Cambillau, C. (1994). Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33, 83-89.
    • (1994) Biochemistry , vol.33 , pp. 83-89
    • Martinez, C.1    Cambillau, C.2
  • 49
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt, A. & Pflugrath, J.W. (1987). Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Cryst. 20, 306-315.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 50
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21, 916-924.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 51
    • 0002863521 scopus 로고
    • Strategies for extracting isomorphous and anomolous signals
    • Sayre, D., ed., Oxford University Press, Oxford, UK
    • Weissman, L. (1982). Strategies for extracting isomorphous and anomolous signals. In Computational Crystallography. (Sayre, D., ed.), pp. 56-63, Oxford University Press, Oxford, UK.
    • (1982) Computational Crystallography , pp. 56-63
    • Weissman, L.1
  • 52
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 53
    • 84920325457 scopus 로고
    • AMORE: An automated package for molecular replacement
    • Navaza, J. (1994). AMORE: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 54
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 55
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 57
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 58
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 60
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 61
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-293.
    • (1991) Proteins , vol.11 , pp. 281-293
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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