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Volumn 49, Issue 11, 2010, Pages 2464-2474

Circular Permutation of Bacillus circulam Xylanase: A Kinetic and Structural Study

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC RESIDUE; CIRCULAR PERMUTATION; CONGO RED; DELETERIOUS EFFECTS; ENDOXYLANASE; EXCELLENT SET; GLOBAL STABILITY; LOCAL MOBILITY; LOOP REGIONS; NMR SPECTROSCOPY; PCR METHOD; SALT BRIDGES; START POINT; STRUCTURAL STUDIES; THERMAL DENATURATIONS; XYLANASE ACTIVITY; XYLANASES;

EID: 77949506674     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100036f     Document Type: Article
Times cited : (40)

References (65)
  • 2
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins, T., Gerday, C., and Feller, G. (2005) Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29, 3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 4
    • 0028244925 scopus 로고
    • Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry
    • Miao, S., Ziser, L., Aebersold, R., and Withers, S. G. (1994) Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry. Biochemistry 33. 7027-7032.
    • (1994) Biochemistry , vol.33 , pp. 7027-7032
    • Miao, S.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 5
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active site residues of the Bacillus circulons xylanase
    • Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Mutational and crystallographic analyses of the active site residues of the Bacillus circulons xylanase. Protein Sci. 3, 467-475.
    • (1994) Protein Sci. , vol.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 6
    • 34250212548 scopus 로고    scopus 로고
    • Recruitment of both uniform and differential binding energy in enzymatic catalysis: Xylanases from families 10 and 11
    • Wicki, J., Schloegl, J., Tarling, C. A., and Withers, S. G. (2007) Recruitment of both uniform and differential binding energy in enzymatic catalysis: xylanases from families 10 and 11. Biochemistry 46, 6996-7005.
    • (2007) Biochemistry , vol.46 , pp. 6996-7005
    • Wicki, J.1    Schloegl, J.2    Tarling, C.A.3    Withers, S.G.4
  • 8
    • 0033609135 scopus 로고    scopus 로고
    • Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase
    • Sidhu, G., Withers, S. G., Nguyen, N. T., Mcintosh, L. P., Ziser, L., and Brayer, G. D. (1999) Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase. Biochemistry 38, 5346-5354.
    • (1999) Biochemistry , vol.38 , pp. 5346-5354
    • Sidhu, G.1    Withers, S.G.2    Nguyen, N.T.3    Mcintosh, L.P.4    Ziser, L.5    Brayer, G.D.6
  • 9
    • 0034021175 scopus 로고    scopus 로고
    • Analysis of the dynamic properties of Bacillus circulons xylanase upon formation of a covalent glycosyl-enzyme intermediate
    • Connelly, G. P., Withers, S. G., and Mcintosh, L. P. (2000) Analysis of the dynamic properties of Bacillus circulons xylanase upon formation of a covalent glycosyl-enzyme intermediate. Protein Sci. 9, 512-524.
    • (2000) Protein Sci. , vol.9 , pp. 512-524
    • Connelly, G.P.1    Withers, S.G.2    Mcintosh, L.P.3
  • 10
    • 0034716940 scopus 로고    scopus 로고
    • Hydrogen bonding and catalysis: A novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
    • Joshi, M. D., Sidhu, G., Pot, I., Brayer, G. D., Withers, S. G., and Mcintosh, L. P. (2000) Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase. J. Mol. Biol. 299, 255-279.
    • (2000) J. Mol. Biol. , vol.299 , pp. 255-279
    • Joshi, M.D.1    Sidhu, G.2    Pot, I.3    Brayer, G.D.4    Withers, S.G.5    Mcintosh, L.P.6
  • 11
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • Joshi, M. D., Sidhu, G., Nielsen, J. E., Brayer, G. D., Withers, S. G., and Mcintosh, L. P. (2001) Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry 40, 10115-10139.
    • (2001) Biochemistry , vol.40 , pp. 10115-10139
    • Joshi, M.D.1    Sidhu, G.2    Nielsen, J.E.3    Brayer, G.D.4    Withers, S.G.5    Mcintosh, L.P.6
  • 12
    • 34548853710 scopus 로고    scopus 로고
    • A secondary xylan-binding site enhances the catalytic activity of a single-domain family 11 glycoside hydrolase
    • Ludwiczek, M. L., Heller, M., Kantner, T., and McIntosh, L. P. (2007) A secondary xylan-binding site enhances the catalytic activity of a single-domain family 11 glycoside hydrolase. J. Mol. Biol. 373, 337-354.
    • (2007) J. Mol. Biol. , vol.373 , pp. 337-354
    • Ludwiczek, M.L.1    Heller, M.2    Kantner, T.3    McIntosh, L.P.4
  • 13
    • 0030052194 scopus 로고    scopus 로고
    • Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase
    • White, A., Tull, D., Johns, K., Withers, S. G., and Rose, D. R. (1996) Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. Nat. Struct. Biol. 3, 149-154.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 149-154
    • White, A.1    Tull, D.2    Johns, K.3    Withers, S.G.4    Rose, D.R.5
  • 14
    • 33847058858 scopus 로고    scopus 로고
    • NMR spectroscopic characterization of a beta-(1,4)-glycosidase along its reaction pathway: Stabilization upon, formation, of the glycosyl-enzyme intermediate
    • Poon, D. K., Ludwiczek, M. L., Schubert, M., Kwan, E. M., Withers, S. G., and Mcintosh, L. P. (2007) NMR spectroscopic characterization of a beta-(1,4)-glycosidase along its reaction pathway: stabilization upon, formation, of the glycosyl-enzyme intermediate. Biochemistry 46, 1759-1770.
    • (2007) Biochemistry , vol.46 , pp. 1759-1770
    • Poon, D.K.1    Ludwiczek, M.L.2    Schubert, M.3    Kwan, E.M.4    Withers, S.G.5    Mcintosh, L.P.6
  • 15
    • 56149088769 scopus 로고    scopus 로고
    • A circularly permuted beta-lactamase as a novel reporter for evaluation of protein cyclization efficiency
    • Kwon, J. S., Bal, J., Hwang, H. M., and Kim, J. Y. (2008) A circularly permuted beta-lactamase as a novel reporter for evaluation of protein cyclization efficiency. J. Microbiol. 46, 456-461.
    • (2008) J. Microbiol. , vol.46 , pp. 456-461
    • Kwon, J.S.1    Bal, J.2    Hwang, H.M.3    Kim, J.Y.4
  • 16
    • 0029422261 scopus 로고
    • Circular permutation of polypeptide chains: Implications for protein folding and stability
    • Heinemann, U., and Hahn, M. (1995) Circular permutation of polypeptide chains: implications for protein folding and stability. Prog. Biophys. MoI, Biol, 64, 121-143.
    • (1995) Prog. Biophys. MoI, Biol , vol.64 , pp. 121-143
    • Heinemann, U.1    Hahn, M.2
  • 17
    • 0033525640 scopus 로고    scopus 로고
    • Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
    • Hennecke, J., Sebbel, P., and Glockshuber, R. (1999) Random circular permutation of DsbA reveals segments that are essential for protein folding and stability. J. Mol. Biol. 286, 1197-1215.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1197-1215
    • Hennecke, J.1    Sebbel, P.2    Glockshuber, R.3
  • 18
    • 0033923044 scopus 로고    scopus 로고
    • Systematic circular permutation of an entire protein reveals essential folding elements
    • Iwakura, M., Nakamura, T., Yamane, C., and Maki, K. (2000) Systematic circular permutation of an entire protein reveals essential folding elements. Nat. Struct. Biol. 7, 580-585.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 580-585
    • Iwakura, M.1    Nakamura, T.2    Yamane, C.3    Maki, K.4
  • 20
    • 55549098922 scopus 로고    scopus 로고
    • Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity
    • Haglund, E., Lindberg, M. O., and Oliveberg, M. (2008) Changes of protein folding pathways by circular permutation. Overlapping nuclei promote global cooperativity. J. Biol. Chem. 283, 27904-27915.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27904-27915
    • Haglund, E.1    Lindberg, M.O.2    Oliveberg, M.3
  • 21
    • 0037027311 scopus 로고    scopus 로고
    • A circularly permuted myoglobin possesses a folded structure and ligand binding similar to those of the wild-type protein but with a reduced thermodynamic stability
    • Fishburn, A. L., Keeffe, J. R., Lissounov, A. V., Peyton, D. H., and Anthony-Cahill, S. J. (2002) A circularly permuted myoglobin possesses a folded structure and ligand binding similar to those of the wild-type protein but with a reduced thermodynamic stability. BioChemistry 41, 13318-13327.
    • (2002) BioChemistry , vol.41 , pp. 13318-13327
    • Fishburn, A.L.1    Keeffe, J.R.2    Lissounov, A.V.3    Peyton, D.H.4    Anthony-Cahill, S.J.5
  • 22
    • 0030840018 scopus 로고    scopus 로고
    • Circularly permuted, beta-lactamase from Staphylococcus aureus PC1
    • Pieper, U., Hayakawa, K., Li, Z., and Herzberg, O. (1997) Circularly permuted, beta-lactamase from Staphylococcus aureus PC1. Biochemistry 36, 8767-8774.
    • (1997) Biochemistry , vol.36 , pp. 8767-8774
    • Pieper, U.1    Hayakawa, K.2    Li, Z.3    Herzberg, O.4
  • 23
    • 0347359185 scopus 로고    scopus 로고
    • Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor
    • Piervincenzi, R. T., and Chilkoti, A. (2004) Effect of genetic circular permutation near the active site on the activity and stability of an enzyme inhibitor. Biomol. Em. 21, 33-42.
    • (2004) Biomol. Em. , vol.21 , pp. 33-42
    • Piervincenzi, R.T.1    Chilkoti, A.2
  • 24
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • Qian, Z., and Lutz, S. (2005) Improving the catalytic activity of Candida antarctica lipase B by circular permutation. J. Am. Chem. Soc. 127, 13466-13467.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 26
    • 70349255505 scopus 로고    scopus 로고
    • Structural redesign of Lipase B from Candida antarctica by circular permutation and incremental truncation. J
    • Qian, Z., Horton, J. R., Cheng, X., and Lutz, S. (2009) Structural redesign of Lipase B from Candida antarctica by circular permutation and incremental truncation. J. Mol. Biol. 393, 191-201.
    • (2009) Mol. Biol. , vol.393 , pp. 191-201
    • Qian, Z.1    Horton, J.R.2    Cheng, X.3    Lutz, S.4
  • 27
    • 73949098126 scopus 로고    scopus 로고
    • Improved triglyceride transesterification by circular permuted Candida antarctica lipase B
    • Yu, Y., and Lutz, S. (2010) Improved triglyceride transesterification by circular permuted Candida antarctica lipase B. Biotechnol. Bioeng. 105, 44-50.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 44-50
    • Yu, Y.1    Lutz, S.2
  • 28
    • 58149195099 scopus 로고    scopus 로고
    • CPDB: A database of circular permutation in proteins
    • Lo, W. C., Lee, C. C., Lee, C. Y., and Lyu, P. C. (2009) CPDB: a database of circular permutation in proteins. Nucleic Acids Res. 37, D328-332.
    • (2009) Nucleic Acids Res. , vol.37
    • Lo, W.C.1    Lee, C.C.2    Lee, C.Y.3    Lyu, P.C.4
  • 29
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg, D. P., and Creighton, T. E. (1983) Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 165, 401-413.
    • (1983) J. Mol. Biol. , vol.165 , pp. 401-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 30
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
    • Luger, K., Hommel, U., Herold, M., Hofsteenge, J., and Kirschner, K. (1989) Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. Science 243, 206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 31
    • 0028099766 scopus 로고
    • Native-like in vivo folding of a circularly permuted jellyroll protein, shown by crystal structure analysis
    • Hahn, M., Piotukh, K., Borriss, R., and Heinemann, U. (1994) Native-like in vivo folding of a circularly permuted jellyroll protein, shown by crystal structure analysis. Proc., Natf, Acad. Sci. U.S.A. 91, 10417-10421.
    • (1994) Proc., Natf, Acad. Sci. U.S.A. , vol.91 , pp. 10417-10421
    • Hahn, M.1    Piotukh, K.2    Borriss, R.3    Heinemann, U.4
  • 33
    • 0029982529 scopus 로고    scopus 로고
    • In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: Implications for protein folding and assembly
    • Zhang, P., and Schachman, H. K. (1996) In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly. Protein Sci. 5, 1290-1300.
    • (1996) Protein Sci. , vol.5 , pp. 1290-1300
    • Zhang, P.1    Schachman, H.K.2
  • 34
    • 0029859408 scopus 로고    scopus 로고
    • Random, circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
    • Graf, R., and Schachman, H. K. (1996) Random, circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U.S.A. 93, 11591-11596.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11591-11596
    • Graf, R.1    Schachman, H.K.2
  • 36
    • 37549058473 scopus 로고    scopus 로고
    • Investigating the structural and functional consequences of circular permutation on lipase B from
    • Qian, Z., Fields, C. J., and Lutz, S. (2007) Investigating the structural and functional consequences of circular permutation on lipase B from Candida antarctica. ChemBioChem 8, 1989-1996.
    • (2007) Candida Antarctica. ChemBioChem , vol.8 , pp. 1989-1996
    • Qian, Z.1    Fields, C.J.2    Lutz, S.3
  • 38
    • 0020032328 scopus 로고
    • Use of Congo Red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen
    • Teather, R. M., and Wood, P. J. (1982) Use of Congo Red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen. Appl. Environ. Microbiol. 43, 777-780.
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 777-780
    • Teather, R.M.1    Wood, P.J.2
  • 39
    • 0027617799 scopus 로고
    • Overexpression of the Bacillus subtilis and circulons xylanases in Escherichia coli
    • Sung, W. L., Luk, C. K., Zahab, D. M., and Wakarchuk, W. (1993) Overexpression of the Bacillus subtilis and circulons xylanases in Escherichia coli. Protein Expression Purif, 200-206.
    • (1993) Protein Expression Purif , pp. 200-206
    • Sung, W.L.1    Luk, C.K.2    Zahab, D.M.3    Wakarchuk, W.4
  • 40
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification, and analysis tools on the ExPASy Server
    • (Walker, J. M., Ed.) pp Humana Press, Totowa, NJ.
    • Gasteiger, E., Hoogland, C., A., G., S., D., R., W., M., D., A., R., and A., B. (2005) Protein identification, and analysis tools on the ExPASy Server, in The Proteomics Protocols Handbook (Walker, J. M., Ed.) pp 571-607, Humana Press, Totowa, NJ.
    • (2005) The Proteomics Protocols Handbook , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2
  • 41
    • 0023940907 scopus 로고
    • 2-Deoxy-2-fluoroD-glycosyl fluorides-a new class of specific mechanism-based, glycosidase inhibitors
    • Withers, S. G., Rupitz, K., and Street, I. P. (1988) 2-Deoxy-2-fluoroD- glycosyl fluorides-a new class of specific mechanism-based, glycosidase inhibitors. J. Biol. Chem. 263, 7929-7932.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7929-7932
    • Withers, S.G.1    Rupitz, K.2    Street, I.P.3
  • 42
    • 0031056260 scopus 로고    scopus 로고
    • Positioning the acid/base catalyst in a glycosidase: Studies with Bacillus circulons xylanase
    • Lawson, S. L., Wakarchuk, W. W., and Withers, S. G. (1997) Positioning the acid/base catalyst in a glycosidase: studies with Bacillus circulons xylanase. Biochemistry 36, 2257-2265.
    • (1997) Biochemistry , vol.36 , pp. 2257-2265
    • Lawson, S.L.1    Wakarchuk, W.W.2    Withers, S.G.3
  • 43
    • 0028761771 scopus 로고
    • A short synthesis of [beta]xylobiosides
    • Ziser, L., and Withers, S. G. (1994) A short synthesis of [beta]xylobiosides. Carbohydr. Res. 265, 9-17.
    • (1994) Carbohydr. Res. , vol.265 , pp. 9-17
    • Ziser, L.1    Withers, S.G.2
  • 44
    • 0029119140 scopus 로고
    • Syntheses and testing of substrates and mechanism-based inactivators for xylanases
    • Ziser, L., Setyawati, I., and Withers, S. G. (1995) Syntheses and testing of substrates and mechanism-based inactivators for xylanases. Carbohydr. Res. 274, 137-153.
    • (1995) Carbohydr. Res. , vol.274 , pp. 137-153
    • Ziser, L.1    Setyawati, I.2    Withers, S.G.3
  • 45
    • 0011756062 scopus 로고    scopus 로고
    • Version 5, 5.0 ed., Erithacus Software Limited, Horley, U.K.
    • Leatherbarrow, R. J. (2001) GraFit Version 5, 5.0 ed., Erithacus Software Limited, Horley, U.K.
    • (2001) GraFit
    • Leatherbarrow, R.J.1
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., and Carter, Charles W., Jr. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter Charles Jr., W.3
  • 48
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. Sect. D 57 1373-1382.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 1373-1382
    • Read, R.1
  • 51
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) COOT: model-building tools for molecular graphics. Acta Crystallogr., Sect. D 60, 2126-2132.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 52
    • 0012293235 scopus 로고    scopus 로고
    • Release 0.99, DeLano Scientific LLC, Palo Alto, CA.
    • DeLano, W. (2002) PyMOL Release 0.99, DeLano Scientific LLC, Palo Alto, CA.
    • (2002) PyMOL
    • Delano, W.1
  • 53
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 54
    • 0004040543 scopus 로고    scopus 로고
    • 3rd ed., University of California, San. Francisco, CA.
    • Goddard, T. D., and Kneeler, D. G. (1999) Sparky 3, 3rd ed., University of California, San. Francisco, CA.
    • (1999) Sparky 3
    • Goddard, T.D.1    Kneeler, D.G.2
  • 55
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution, employing pulsed field gradients
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution, employing pulsed field gradients. Prog. Nucl. Magn. Res. Spectrosc. 34, 93-158.
    • (1999) Prog. Nucl. Magn. Res. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 56
    • 0029955152 scopus 로고    scopus 로고
    • Secondary structure and NMR assignments of Bacillus circulons xylanase. Protein
    • Plesniak, L. A., Wakarchuk, W. W., and Mcintosh, L. P. (1996) Secondary structure and NMR assignments of Bacillus circulons xylanase. Protein Sci. 5, 1118-1135.
    • (1996) Sci. , vol.5 , pp. 1118-1135
    • Plesniak, L.A.1    Wakarchuk, W.W.2    Mcintosh, L.P.3
  • 58
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 59
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset, P., Hus, J.-C., Blackledge, M., and Marion, D. (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR 16, 23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.-C.2    Blackledge, M.3    Marion, D.4
  • 61
    • 70349443443 scopus 로고    scopus 로고
    • Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases. Proteins: Struct
    • Pollet, A., Vandermarliere, E., Lammertyn, J., Strelkov, S. V., Delcour, J. A., and Courtin, C. M. (2009) Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases. Proteins: Struct., Funct., Genet. 77, 395-403.
    • (2009) Funct., Genet. , vol.77 , pp. 395-403
    • Pollet, A.1    Vandermarliere, E.2    Lammertyn, J.3    Strelkov, S.V.4    Delcour, J.A.5    Courtin, C.M.6
  • 62
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- And gamma-synuclein: Implications for fibrillation
    • Marsh, J. A., Singh, V. K., Jia, Z. C., and Forman-Kay, J. D. (2006) Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation. Protein Sci. 15, 2795-2804.
    • (2006) Protein Sci. , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.C.3    Forman-Kay, J.D.4
  • 65
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-a program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G., and Thornton, J. M. (1996) PROMOTIF-a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.