메뉴 건너뛰기




Volumn 14, Issue 6, 2018, Pages 542-547

Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein article

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CYCLOHEXADIENYL DEHYDRATASE; HYDROLYASE; SOLUTE BINDING PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; OLIGONUCLEOTIDE; PREPHENATE DEHYDRATASE; PROTEIN BINDING;

EID: 85045855955     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/s41589-018-0043-2     Document Type: Article
Times cited : (76)

References (60)
  • 1
    • 84997426755 scopus 로고    scopus 로고
    • Evolution of enzyme superfamilies: Comprehensive exploration of sequence-function relationships
    • Baier, F., Copp, J. N. & Tokuriki, N. Evolution of enzyme superfamilies: Comprehensive exploration of sequence-function relationships. Biochemistry 55, 6375-6388 (2016).
    • (2016) Biochemistry , vol.55 , pp. 6375-6388
    • Baier, F.1    Copp, J.N.2    Tokuriki, N.3
  • 2
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O. & Tawfik, D. S. Enzyme promiscuity: A mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 3
    • 84957449877 scopus 로고    scopus 로고
    • Large-scale analysis exploring evolution of catalytic machineries and mechanisms in enzyme superfamilies
    • Furnham, N., Dawson, N. L., Rahman, S. A., Thornton, J. M. & Orengo, C. A. Large-scale analysis exploring evolution of catalytic machineries and mechanisms in enzyme superfamilies. J. Mol. Biol. 428 2 Pt A, 253-267 (2016).
    • (2016) J. Mol. Biol. , vol.428 , Issue.2 PART A , pp. 253-267
    • Furnham, N.1    Dawson, N.L.2    Rahman, S.A.3    Thornton, J.M.4    Orengo, C.A.5
  • 4
    • 84880862788 scopus 로고    scopus 로고
    • Evolutionary biochemistry: Revealing the historical and physical causes of protein properties
    • Harms, M. J. & Thornton, J. W. Evolutionary biochemistry: Revealing the historical and physical causes of protein properties. Nat. Rev. Genet. 14, 559-571 (2013).
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 559-571
    • Harms, M.J.1    Thornton, J.W.2
  • 5
    • 0027264847 scopus 로고
    • A bacterial periplasmic receptor homologue with catalytic activity: Cyclohexadienyl dehydratase of Pseudomonas aeruginosa is homologous to receptors specific for polar amino acids
    • Tam, R. & Saier, M. H. Jr. A bacterial periplasmic receptor homologue with catalytic activity: Cyclohexadienyl dehydratase of Pseudomonas aeruginosa is homologous to receptors specific for polar amino acids. Res. Microbiol. 144, 165-169 (1993).
    • (1993) Res. Microbiol. , vol.144 , pp. 165-169
    • Tam, R.1    Saier, M.H.2
  • 6
    • 84861449462 scopus 로고    scopus 로고
    • Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis
    • Ngaki, M. N. et al. Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis. Nature 485, 530-533 (2012).
    • (2012) Nature , vol.485 , pp. 530-533
    • Ngaki, M.N.1
  • 7
    • 85016144548 scopus 로고    scopus 로고
    • An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme
    • Ortmayer, M. et al. An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme. Nature 539, 593-597 (2016).
    • (2016) Nature , vol.539 , pp. 593-597
    • Ortmayer, M.1
  • 8
    • 0026806046 scopus 로고
    • Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product
    • Zhao, G. S., Xia, T. H., Fischer, R. S. & Jensen, R. A. Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product. J. Biol. Chem. 267, 2487-2493 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 2487-2493
    • Zhao, G.S.1    Xia, T.H.2    Fischer, R.S.3    Jensen, R.A.4
  • 10
    • 85019699606 scopus 로고    scopus 로고
    • Reconstructing ancient proteins to understand the causes of structure and function
    • Hochberg, G. K. A. & Thornton, J. W. Reconstructing ancient proteins to understand the causes of structure and function. Annu. Rev. Biophys. 46, 247-269 (2017).
    • (2017) Annu. Rev. Biophys. , vol.46 , pp. 247-269
    • Hochberg, G.K.A.1    Thornton, J.W.2
  • 11
    • 84921865985 scopus 로고    scopus 로고
    • Experimental strategies for functional annotation and metabolism discovery: Targeted screening of solute binding proteins and unbiased panning of metabolomes
    • Vetting, M. W. et al. Experimental strategies for functional annotation and metabolism discovery: Targeted screening of solute binding proteins and unbiased panning of metabolomes. Biochemistry 54, 909-931 (2015).
    • (2015) Biochemistry , vol.54 , pp. 909-931
    • Vetting, M.W.1
  • 12
    • 84925286236 scopus 로고    scopus 로고
    • Conformational dynamics in substrate-binding domains influences transport in the ABC importer GlnPQ
    • Gouridis, G. et al. Conformational dynamics in substrate-binding domains influences transport in the ABC importer GlnPQ. Nat. Struct. Mol. Biol. 22, 57-64 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 57-64
    • Gouridis, G.1
  • 13
    • 0034863015 scopus 로고    scopus 로고
    • Manipulation of ligand binding affinity by exploitation of conformational coupling
    • Marvin, J. S. & Hellinga, H. W. Manipulation of ligand binding affinity by exploitation of conformational coupling. Nat. Struct. Mol. Biol. 8, 795-798 (2001).
    • (2001) Nat. Struct. Mol. Biol. , vol.8 , pp. 795-798
    • Marvin, J.S.1    Hellinga, H.W.2
  • 14
    • 84987641979 scopus 로고    scopus 로고
    • The role of protein dynamics in the evolution of new enzyme function
    • Campbell, E. et al. The role of protein dynamics in the evolution of new enzyme function. Nat. Chem. Biol. 12, 944-950 (2016).
    • (2016) Nat. Chem. Biol. , vol.12 , pp. 944-950
    • Campbell, E.1
  • 15
    • 84939644294 scopus 로고    scopus 로고
    • The moderately efficient enzyme: Futile encounters and enzyme floppiness
    • Bar-Even, A., Milo, R., Noor, E. & Tawfik, D. S. The moderately efficient enzyme: Futile encounters and enzyme floppiness. Biochemistry 54, 4969-4977 (2015).
    • (2015) Biochemistry , vol.54 , pp. 4969-4977
    • Bar-Even, A.1    Milo, R.2    Noor, E.3    Tawfik, D.S.4
  • 16
    • 77749286394 scopus 로고    scopus 로고
    • Ligand-free open-closed transitions of periplasmic binding proteins: The case of glutamine-binding protein
    • Bermejo, G. A., Strub, M.-P., Ho, C. & Tjandra, N. Ligand-free open-closed transitions of periplasmic binding proteins: The case of glutamine-binding protein. Biochemistry 49, 1893-1902 (2010).
    • (2010) Biochemistry , vol.49 , pp. 1893-1902
    • Bermejo, G.A.1    Strub, M.-P.2    Ho, C.3    Tjandra, N.4
  • 17
    • 79958772218 scopus 로고    scopus 로고
    • Conformational dynamics of l-lysine, l-arginine, l-ornithine binding protein reveals ligand-dependent plasticity
    • Silva, D.-A., Domínguez-Ramírez, L., Rojo-Domínguez, A. & Sosa-Peinado, A. Conformational dynamics of l-lysine, l-arginine, l-ornithine binding protein reveals ligand-dependent plasticity. Proteins 79, 2097-2108 (2011).
    • (2011) Proteins , vol.79 , pp. 2097-2108
    • Silva, D.-A.1    Domínguez-Ramírez, L.2    Rojo-Domínguez, A.3    Sosa-Peinado, A.4
  • 18
    • 84893734804 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation
    • Chu, B. C. H., Chan, D. I., DeWolf, T., Periole, X. & Vogel, H. J. Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation. Proteins 82, 386-398 (2014).
    • (2014) Proteins , vol.82 , pp. 386-398
    • Chu, B.C.H.1    Chan, D.I.2    DeWolf, T.3    Periole, X.4    Vogel, H.J.5
  • 19
    • 79953738501 scopus 로고    scopus 로고
    • Initial mutations direct alternative pathways of protein evolution
    • Salverda, M. L. M. et al. Initial mutations direct alternative pathways of protein evolution. PLoS Genet. 7, e1001321 (2011).
    • (2011) PLoS Genet. , vol.7 , pp. e1001321
    • Salverda, M.L.M.1
  • 20
    • 84943792201 scopus 로고    scopus 로고
    • Reverse evolution leads to genotypic incompatibility despite functional and active site convergence
    • Kaltenbach, M., Jackson, C. J., Campbell, E. C., Hollfelder, F. & Tokuriki, N. Reverse evolution leads to genotypic incompatibility despite functional and active site convergence. eLife 4, e06492 (2015).
    • (2015) ELife , vol.4 , pp. e06492
    • Kaltenbach, M.1    Jackson, C.J.2    Campbell, E.C.3    Hollfelder, F.4    Tokuriki, N.5
  • 21
    • 84995783980 scopus 로고    scopus 로고
    • Active site desolvation and thermostability tradeoffs in the evolution of catalytically diverse triazine hydrolases
    • Sugrue, E., Carr, P. D., Scott, C. & Jackson, C. J. Active site desolvation and thermostability tradeoffs in the evolution of catalytically diverse triazine hydrolases. Biochemistry 55, 6304-6313 (2016).
    • (2016) Biochemistry , vol.55 , pp. 6304-6313
    • Sugrue, E.1    Carr, P.D.2    Scott, C.3    Jackson, C.J.4
  • 22
    • 84948701202 scopus 로고    scopus 로고
    • New tricks for old proteins: Single mutations in a non-enzymatic protein give rise to various enzymatic activities
    • Moroz, Y. S. et al. New tricks for old proteins: Single mutations in a non-enzymatic protein give rise to various enzymatic activities. J. Am. Chem. Soc. 137, 14905-14911 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 14905-14911
    • Moroz, Y.S.1
  • 23
    • 84871755504 scopus 로고    scopus 로고
    • Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme
    • Tokuriki, N. et al. Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme. Nat. Commun. 3, 1257 (2012).
    • (2012) Nat. Commun. , vol.3 , pp. 1257
    • Tokuriki, N.1
  • 24
    • 84956891086 scopus 로고    scopus 로고
    • Evolution of an ancient protein function involved in organized multicellularity in animals
    • Anderson, D. P. et al. Evolution of an ancient protein function involved in organized multicellularity in animals. eLife 5, e10147 (2016).
    • (2016) ELife , vol.5 , pp. e10147
    • Anderson, D.P.1
  • 25
    • 84988443529 scopus 로고    scopus 로고
    • The coming of age of de novo protein design
    • Huang, P.-S., Boyken, S. E. & Baker, D. The coming of age of de novo protein design. Nature 537, 320-327 (2016).
    • (2016) Nature , vol.537 , pp. 320-327
    • Huang, P.-S.1    Boyken, S.E.2    Baker, D.3
  • 26
    • 84983605294 scopus 로고    scopus 로고
    • Installing hydrolytic activity into a completely de novo protein framework
    • Burton, A. J., Thomson, A. R., Dawson, W. M., Brady, R. L. & Woolfson, D. N. Installing hydrolytic activity into a completely de novo protein framework. Nat. Chem. 8, 837-844 (2016).
    • (2016) Nat. Chem. , vol.8 , pp. 837-844
    • Burton, A.J.1    Thomson, A.R.2    Dawson, W.M.3    Brady, R.L.4    Woolfson, D.N.5
  • 27
    • 43449098518 scopus 로고    scopus 로고
    • Kemp elimination catalysts by computational enzyme design
    • Röthlisberger, D. et al. Kemp elimination catalysts by computational enzyme design. Nature 453, 190-195 (2008).
    • (2008) Nature , vol.453 , pp. 190-195
    • Röthlisberger, D.1
  • 28
    • 84903827354 scopus 로고    scopus 로고
    • Computational enzyme design: Transitioning from catalytic proteins to enzymes
    • Mak, W. S. & Siegel, J. B. Computational enzyme design: Transitioning from catalytic proteins to enzymes. Curr. Opin. Struct. Biol. 27, 87-94 (2014).
    • (2014) Curr. Opin. Struct. Biol. , vol.27 , pp. 87-94
    • Mak, W.S.1    Siegel, J.B.2
  • 29
    • 84904466057 scopus 로고    scopus 로고
    • Catalytic efficiency of designed catalytic proteins
    • Korendovych, I. V. & DeGrado, W. F. Catalytic efficiency of designed catalytic proteins. Curr. Opin. Struct. Biol. 27, 113-121 (2014).
    • (2014) Curr. Opin. Struct. Biol. , vol.27 , pp. 113-121
    • Korendovych, I.V.1    DeGrado, W.F.2
  • 30
    • 84888034901 scopus 로고    scopus 로고
    • Precision is essential for efficient catalysis in an evolved Kemp eliminase
    • Blomberg, R. et al. Precision is essential for efficient catalysis in an evolved Kemp eliminase. Nature 503, 418-421 (2013).
    • (2013) Nature , vol.503 , pp. 418-421
    • Blomberg, R.1
  • 31
    • 84863000087 scopus 로고    scopus 로고
    • Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59
    • Khersonsky, O. et al. Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59. Proc. Natl. Acad. Sci. USA 109, 10358-10363 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10358-10363
    • Khersonsky, O.1
  • 32
    • 56649114274 scopus 로고    scopus 로고
    • A one pot, one step, precision cloning method with high throughput capability
    • Engler, C., Kandzia, R. & Marillonnet, S. A one pot, one step, precision cloning method with high throughput capability. PLoS One 3, e3647 (2008).
    • (2008) PLoS One , vol.3 , pp. e3647
    • Engler, C.1    Kandzia, R.2    Marillonnet, S.3
  • 33
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 34
    • 84965006405 scopus 로고    scopus 로고
    • Ancestral protein reconstruction yields insights into adaptive evolution of binding specificity in solute-binding proteins
    • Clifton, B. E. & Jackson, C. J. Ancestral protein reconstruction yields insights into adaptive evolution of binding specificity in solute-binding proteins. Cell Chem. Biol. 23, 236-245 (2016).
    • (2016) Cell Chem. Biol. , vol.23 , pp. 236-245
    • Clifton, B.E.1    Jackson, C.J.2
  • 35
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximumlikelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon, S. et al. New algorithms and methods to estimate maximumlikelihood phylogenies: Assessing the performance of PhyML 3.0. Syst. Biol. 59, 307-321 (2010).
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1
  • 36
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • Abascal, F., Zardoya, R. & Posada, D. ProtTest: Selection of best-fit models of protein evolution. Bioinformatics 21, 2104-2105 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 37
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: Phylogenetic analysis by maximum likelihood
    • Yang, Z. PAML 4: Phylogenetic analysis by maximum likelihood. Mol. Biol. Evol. 24, 1586-1591 (2007).
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 38
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson, D. G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343-345 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1
  • 39
    • 84929275058 scopus 로고    scopus 로고
    • A high-throughput screen for ligand binding reveals the specificities of three amino acid chemoreceptors from Pseudomonas syringae pv. Actinidiae
    • McKellar, J. L., Minnell, J. J. & Gerth, M. L. A high-throughput screen for ligand binding reveals the specificities of three amino acid chemoreceptors from Pseudomonas syringae pv. actinidiae. Mol. Microbiol. 96, 694-707 (2015).
    • (2015) Mol. Microbiol. , vol.96 , pp. 694-707
    • McKellar, J.L.1    Minnell, J.J.2    Gerth, M.L.3
  • 40
    • 0000316121 scopus 로고
    • Chorismic acid: Purification and some chemical and physical studies
    • Gibson, F. Chorismic acid: Purification and some chemical and physical studies. Biochem. J. 90, 256-261 (1964).
    • (1964) Biochem. J. , vol.90 , pp. 256-261
    • Gibson, F.1
  • 41
    • 0001762419 scopus 로고
    • Preliminary studies on the isolation and metabolism of an intermediate in aromatic biosynthesis: Chorismic acid
    • Gibson, M. I. & Gibson, F. Preliminary studies on the isolation and metabolism of an intermediate in aromatic biosynthesis: Chorismic acid. Biochem. J. 90, 248-256 (1964).
    • (1964) Biochem. J. , vol.90 , pp. 248-256
    • Gibson, M.I.1    Gibson, F.2
  • 42
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T. M. et al. Blu-Ice and the Distributed Control System: Software for data acquisition and instrument control at macromolecular crystallography beamlines. J. Synchrotron Radiat. 9, 401-406 (2002).
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 401-406
    • McPhillips, T.M.1
  • 45
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 46
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 49
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 50
    • 34248632787 scopus 로고    scopus 로고
    • In vitro 'sexual' evolution through the PCR-based staggered extension process (StEP)
    • Zhao, H. & Zha, W. In vitro 'sexual' evolution through the PCR-based staggered extension process (StEP). Nat. Protoc. 1, 1865-1871 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 1865-1871
    • Zhao, H.1    Zha, W.2
  • 51
    • 34548014497 scopus 로고    scopus 로고
    • Incorporating Synthetic Oligonucleotides via Gene Reassembly (ISOR): A versatile tool for generating targeted libraries
    • Herman, A. & Tawfik, D. S. Incorporating Synthetic Oligonucleotides via Gene Reassembly (ISOR): A versatile tool for generating targeted libraries. Protein Eng. Des. Sel. 20, 219-226 (2007).
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 219-226
    • Herman, A.1    Tawfik, D.S.2
  • 53
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 54
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk, S. et al. GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845-854 (2013).
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1
  • 55
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C., Villa, A., Mark, A. E. & van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6. J. Comput. Chem. 25, 1656-1676 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 56
    • 34548283148 scopus 로고    scopus 로고
    • Scalable algorithms for molecular dynamics simulations on commodity clusters
    • (ACM, Tampa, Florida)
    • Bowers, K. et al. Scalable algorithms for molecular dynamics simulations on commodity clusters. Proc. ACM/IEEE SC Conf. Supercomput. (SC06) (ACM, Tampa, Florida, 2006).
    • (2006) Proc. ACM/IEEE SC Conf. Supercomput. (SC06)
    • Bowers, K.1
  • 57
    • 84954459896 scopus 로고    scopus 로고
    • OPLS3: A force field providing broad coverage of drug-like small molecules and proteins
    • Harder, E. et al. OPLS3: A force field providing broad coverage of drug-like small molecules and proteins. J. Chem. Theory Comput. 12, 281-296 (2016).
    • (2016) J. Chem. Theory Comput. , vol.12 , pp. 281-296
    • Harder, E.1
  • 59
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S. & Berendsen, H. J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30, 144-154 (1998).
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 60
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pKa calculations
    • Olsson, M. H. M., Søndergaard, C. R., Rostkowski, M. & Jensen, J. H. PROPKA3: Consistent treatment of internal and surface residues in empirical pKa calculations. J. Chem. Theory Comput. 7, 525-537 (2011).
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.