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Volumn 100, Issue 9, 2011, Pages 2217-2225

Electronic structure of neighboring extein residue modulates intein C-terminal cleavage activity

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79959758646     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.02.037     Document Type: Article
Times cited : (17)

References (66)
  • 1
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. 2000. Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69:447-496.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 2
    • 0033963173 scopus 로고    scopus 로고
    • InBase, the intein database
    • Perler, F. B. 2000. InBase, the intein database. Nucleic Acids Res. 28:344-345. (Pubitemid 30047802)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 344-345
    • Perler, F.B.1
  • 3
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • DOI 10.1038/nsb0198-31
    • Klabunde, T., S. Sharma,..., J. C. Sacchettini. 1998. Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nat. Struct. Biol. 5:31-36. (Pubitemid 28048974)
    • (1998) Nature Structural Biology , vol.5 , Issue.1 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 4
    • 0030611387 scopus 로고    scopus 로고
    • Crystal structure of Pl-SceI, a homing endonuclease with protein splicing activity
    • Duan, X. Q., F. S. Gimble, and F. A. Quiocho. 1997. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell. 89:555-564. (Pubitemid 27511766)
    • (1997) Cell , vol.89 , Issue.4 , pp. 555-564
    • Duan, X.1    Gimble, F.S.2    Quiocho, F.A.3
  • 5
    • 0141755113 scopus 로고    scopus 로고
    • Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing
    • DOI 10.1074/jbc.M306197200
    • Ding, Y., M. Q. Xu,..., Z. Rao. 2003. Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. J. Biol. Chem. 278:39133-39142. (Pubitemid 37221816)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39133-39142
    • Ding, Y.1    Xu, M.-Q.2    Ghosh, I.3    Chen, X.4    Ferrandon, S.5    Lesage, G.6    Rao, Z.7
  • 7
    • 0032534048 scopus 로고    scopus 로고
    • Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step
    • Chong, S., G. E. Montello,..., J. Benner. 1998. Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 26:5109-5115. (Pubitemid 28517566)
    • (1998) Nucleic Acids Research , vol.26 , Issue.22 , pp. 5109-5115
    • Chong, S.1    Montello, G.E.2    Zhang, A.3    Cantor, E.J.4    Liao, W.5    Xu, M.-Q.6    Benner, J.7
  • 8
    • 0032562685 scopus 로고    scopus 로고
    • Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein
    • DOI 10.1074/jbc.273.17.10567
    • Chong, S., K. S. Williams,..., M. Q. Xu. 1998. Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein. J. Biol. Chem. 273:10567-10577. (Pubitemid 28227668)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10567-10577
    • Chong, S.1    Williams, K.S.2    Wotkowicz, C.3    Xu, M.-Q.4
  • 9
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein
    • 116, 118-120
    • Southworth, M. W., K. Amaya,..., F. B. Perler. 1999. Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques. 27:110-114, 116, 118-120.
    • (1999) Biotechniques. , vol.27 , pp. 110-114
    • Southworth, M.W.1    Amaya, K.2    Perler, F.B.3
  • 10
    • 33644912308 scopus 로고    scopus 로고
    • Highly efficient protein transsplicing by a naturally split DnaE intein from Nostoc punctiforme
    • Iwai, H., S. Züger,..., P. H. Tam. 2006. Highly efficient protein transsplicing by a naturally split DnaE intein from Nostoc punctiforme. FEBS Lett. 580:1853-1858.
    • (2006) FEBS Lett. , vol.580 , pp. 1853-1858
    • Iwai, H.1    Züger, S.2    Tam, P.H.3
  • 11
    • 67650492166 scopus 로고    scopus 로고
    • Modulation of intein activity by its neighboring extein substrates
    • Amitai, G., B. P. Callahan,..., M. Belfort. 2009. Modulation of intein activity by its neighboring extein substrates. Proc. Natl. Acad. Sci. USA. 106:11005-11010.
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 11005-11010
    • Amitai, G.1    Callahan, B.P.2    Belfort, M.3
  • 12
    • 0032882220 scopus 로고    scopus 로고
    • Fine-tuning an engineered intein
    • DOI 10.1038/12839
    • Amitai, G., and S. Pietrokovski. 1999. Fine-tuning an engineered intein. Nat. Biotechnol. 17:854-855. (Pubitemid 29416654)
    • (1999) Nature Biotechnology , vol.17 , Issue.9 , pp. 854-855
    • Amitai, G.1    Pietrokovski, S.2
  • 14
    • 0037112699 scopus 로고    scopus 로고
    • Intein-mediated purification of cytotoxic endonuclease I-Tevl by insertional inactivation and pH-controllable splicing
    • Wu, W., D. W. Wood,..., M. Belfort. 2002. Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing. Nucleic Acids Res. 30:4864-4871. (Pubitemid 35414646)
    • (2002) Nucleic Acids Research , vol.30 , Issue.22 , pp. 4864-4871
    • Wu, W.1    Wood, D.W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 16
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags
    • DOI 10.1038/nmeth787
    • Banki, M. R., L. A. Feng, and D. W. Wood. 2005. Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat. Methods. 2:659-661. (Pubitemid 41223091)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 17
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • DOI 10.1110/ps.041296305
    • Banki, M. R., T. U. Gerngross, and D. W. Wood. 2005. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci. 14:1387-1395. (Pubitemid 41007905)
    • (2005) Protein Science , vol.14 , Issue.6 , pp. 1387-1395
    • Banki, M.R.1    Gerngross, T.U.2    Wood, D.W.3
  • 18
    • 33745991799 scopus 로고    scopus 로고
    • Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli
    • DOI 10.1016/j.jbiotec.2006.01.018, PII S0168165606000903
    • Sharma, S. S., S. Chong, and S. W. Harcum. 2006. Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli. J. Biotechnol. 125:48-56. (Pubitemid 44066600)
    • (2006) Journal of Biotechnology , vol.125 , Issue.1 , pp. 48-56
    • Sharma, S.S.1    Chong, S.2    Harcum, S.W.3
  • 19
    • 75649127236 scopus 로고    scopus 로고
    • Expression of intein-tagged fusion protein and its applications in downstream processing
    • Wang, L., J. H. Kang,..., E. K. Lee. 2010. Expression of intein-tagged fusion protein and its applications in downstream processing. J. Chem. Technol. Biotechnol. 85:11-18.
    • (2010) J. Chem. Technol. Biotechnol. , vol.85 , pp. 11-18
    • Wang, L.1    Kang, J.H.2    Lee, E.K.3
  • 20
    • 77951976127 scopus 로고    scopus 로고
    • The potential role of self-cleaving purification tags in commercial-scale processes
    • Fong, B. A., W. Y. Wu, and D. W. Wood. 2010. The potential role of self-cleaving purification tags in commercial-scale processes. Trends Biotechnol. 28:272-279.
    • (2010) Trends Biotechnol. , vol.28 , pp. 272-279
    • Fong, B.A.1    Wu, W.Y.2    Wood, D.W.3
  • 21
    • 3042840324 scopus 로고    scopus 로고
    • Inteins as targets for potential antimycobacterial drugs
    • S992-1436
    • Paulus, H. 2003. Inteins as targets for potential antimycobacterial drugs. Front. Biosci. 8:s1157-s1165. (Pubitemid 38925376)
    • (2003) Frontiers in Bioscience , vol.8 , Issue.SUPPL.
    • Paulus, H.1
  • 22
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: A versatile tool for drug discovery
    • Cheriyan, M., and F. B. Perler. 2009. Protein splicing: a versatile tool for drug discovery. Adv. Drug Deliv. Rev. 61:899-907.
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 23
    • 0037036791 scopus 로고    scopus 로고
    • Protein splicing triggered by a small molecule
    • DOI 10.1021/ja026769o
    • Mootz, H. D., and T. W. Muir. 2002. Protein splicing triggered by a small molecule. J. Am. Chem. Soc. 124:9044-9045. (Pubitemid 34847653)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.31 , pp. 9044-9045
    • Mootz, H.D.1    Muir, T.W.2
  • 24
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • DOI 10.1038/nmeth886, PII N886
    • Muralidharan, V., and T. W. Muir. 2006. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat. Methods. 3:429-438. (Pubitemid 43811554)
    • (2006) Nature Methods , vol.3 , Issue.6 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 27
    • 27844584367 scopus 로고    scopus 로고
    • Industrial relevance of thermophilic Archaea
    • DOI 10.1016/j.mib.2005.10.015, PII S1369527405001712, Growth Development
    • Egorova, K., and G. Antranikian. 2005. Industrial relevance of thermophilic Archaea. Curr. Opin. Microbiol. 8:649-655. (Pubitemid 41643962)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 649-655
    • Egorova, K.1    Antranikian, G.2
  • 28
    • 78149491924 scopus 로고    scopus 로고
    • Fructose 1, 6-bisphosphatase from a hyper-thermophilic bacterium Thermotoga maritima: Characterization, metabolite stability, and its implications
    • Myung, S., Y. Wang, and Y. H. P. Zhang. 2010. Fructose 1, 6-bisphosphatase from a hyper-thermophilic bacterium Thermotoga maritima: characterization, metabolite stability, and its implications. Process Biochem. 45:1882-1887.
    • (2010) Process Biochem. , vol.45 , pp. 1882-1887
    • Myung, S.1    Wang, Y.2    Zhang, Y.H.P.3
  • 29
    • 85031222248 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 30
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • DOI 10.1038/12879
    • Wood, D. W., W. Wu,..., M. Belfort. 1999. A genetic system yields self-cleaving inteins for bioseparations. Nat. Biotechnol. 17:889-892. (Pubitemid 29416663)
    • (1999) Nature Biotechnology , vol.17 , Issue.9 , pp. 889-892
    • Wood, D.W.1    Wu, W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 31
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor
    • DOI 10.1021/bp0000858
    • Wood, D. W., V. Derbyshire,..., G. Belfort. 2000. Optimized singlestep affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor. Biotechnol. Prog. 16:1055-1063. (Pubitemid 32044859)
    • (2000) Biotechnology Progress , vol.16 , Issue.6 , pp. 1055-1063
    • Wood, D.W.1    Derbyshire, V.2    Wu, W.3    Chartrain, M.4    Belfort, M.5    Belfort, G.6
  • 33
    • 85031230190 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 35
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM methods for biomolecular systems
    • Senn, H. M., and W. Thiel. 2009. QM/MM methods for biomolecular systems. Angew. Chem. Int. Ed. Engl. 48:1198-1229.
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 36
    • 77949868796 scopus 로고    scopus 로고
    • Investigations of enzyme-catalyzed reactions with combined quantum mechanics/molecular mechanics (QM/MM) methods
    • Ranaghan, K. E., and A. J. Mulholland. 2010. Investigations of enzyme-catalyzed reactions with combined quantum mechanics/molecular mechanics (QM/MM) methods. Int. Rev. Phys. Chem. 29:65-133.
    • (2010) Int. Rev. Phys. Chem. , vol.29 , pp. 65-133
    • Ranaghan, K.E.1    Mulholland, A.J.2
  • 38
    • 70350008258 scopus 로고    scopus 로고
    • Selection and structure of hyperactive inteins: Peripheral changes relayed to the catalytic center
    • Hiraga, K., I. Soga,..., M. Belfort. 2009. Selection and structure of hyperactive inteins: peripheral changes relayed to the catalytic center. J. Mol. Biol. 393:1106-1117.
    • (2009) J. Mol. Biol. , vol.393 , pp. 1106-1117
    • Hiraga, K.1    Soga, I.2    Belfort, M.3
  • 39
    • 10644250257 scopus 로고
    • Inhomogeneous electron gas
    • Hohenberg, P., and W. Kohn. 1964. Inhomogeneous electron gas. Phys. Rev. B. 136:864-871.
    • (1964) Phys. Rev. B. , vol.136 , pp. 864-871
    • Hohenberg, P.1    Kohn, W.2
  • 40
    • 0042113153 scopus 로고
    • Self-consistent equations including exchange and correlation effects
    • Kohn, W., and L. J. Sham. 1965. Self-consistent equations including exchange and correlation effects. Phys. Rev. 140:1133-1138.
    • (1965) Phys. Rev. , vol.140 , pp. 1133-1138
    • Kohn, W.1    Sham, L.J.2
  • 41
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. 1993. Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98:5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 43
    • 84986527758 scopus 로고
    • IMOMM: A new integrated ab initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition states
    • Maseras, F., and K. Morokuma. 1995. IMOMM: a new integrated ab initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition states. J. Comput. Chem. 16:1170-1179.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 44
    • 0036025446 scopus 로고    scopus 로고
    • Quantum mechanical methods for enzyme kinetics
    • Gao, J., and D. G. Truhlar. 2002. Quantum mechanical methods for enzyme kinetics. Annu. Rev. Phys. Chem. 53:467-505.
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 467-505
    • Gao, J.1    Truhlar, D.G.2
  • 45
    • 0037076062 scopus 로고    scopus 로고
    • A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH)
    • DOI 10.1021/jp013012v
    • Cui, Q., M. Elstner, and M. Karplus. 2002. A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH). J. Phys. Chem. B. 106:2721-2740. (Pubitemid 35275952)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.10 , pp. 2721-2740
    • Cui, Q.1    Elstner, M.2    Karplus, M.3
  • 46
    • 0037116512 scopus 로고    scopus 로고
    • Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monooxygenase and ribonucleotide reductase
    • DOI 10.1021/ja016589z
    • Torrent, M., T. Vreven,..., H. B. Schlegel. 2002. Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monooxygenase and ribonucleotide reductase. J. Am. Chem. Soc. 124:192-193. (Pubitemid 34062751)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.2 , pp. 192-193
    • Torrent, M.1    Vreven, T.2    Musaev, D.G.3    Morokuma, K.4    Farkas, O.5    Schlegel, H.B.6
  • 47
    • 0037473497 scopus 로고    scopus 로고
    • Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints
    • Vreven, T., K. Morokuma,..., M. J. Frisch. 2003. Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints. J. Comput. Chem. 24:760-769.
    • (2003) J. Comput. Chem. , vol.24 , pp. 760-769
    • Vreven, T.1    Morokuma, K.2    Frisch, M.J.3
  • 48
    • 33847071304 scopus 로고    scopus 로고
    • Crystallographic and Mutational Studies of Mycobacterium tuberculosis recA Mini-inteins Suggest a Pivotal Role for a Highly Conserved Aspartate Residue
    • DOI 10.1016/j.jmb.2006.12.050, PII S0022283606017281
    • Van Roey, P., B. Pereira,..., V. Derbyshire. 2007. Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue. J. Mol. Biol. 367:162-173. (Pubitemid 46274715)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.1 , pp. 162-173
    • Van Roey, P.1    Pereira, B.2    Li, Z.3    Hiraga, K.4    Belfort, M.5    Derbyshire, V.6
  • 49
    • 0025990865 scopus 로고
    • Novel structure of the recA locus of Mycobacterium tuberculosis implies processing of the gene product
    • Davis, E. O., S. G. Sedgwick, and M. J. Colston. 1991. Novel structure of the recA locus of Mycobacterium tuberculosis implies processing of the gene product. J. Bacteriol. 173:5653-5662.
    • (1991) J. Bacteriol. , vol.173 , pp. 5653-5662
    • Davis, E.O.1    Sedgwick, S.G.2    Colston, M.J.3
  • 50
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell, W. D., P. Cieplak,..., P. A. Kollman. 1995. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117:5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Kollman, P.A.3
  • 51
    • 28444477686 scopus 로고    scopus 로고
    • Minimization and stabilization of the Mycobacterium tuberculosis recA intein
    • DOI 10.1016/j.jmb.2005.09.088, PII S0022283605011009
    • Hiraga, K., V. Derbyshire,..., M. Belfort. 2005. Minimization and stabilization of the Mycobacterium tuberculosis recA intein. J. Mol. Biol. 354:916-926. (Pubitemid 41735512)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 916-926
    • Hiraga, K.1    Derbyshire, V.2    Dansereau, J.T.3    Van Roey, P.4    Belfort, M.5
  • 53
    • 77954386029 scopus 로고    scopus 로고
    • Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins
    • Du, Z., Y. Liu,..., C. Wang. 2010. Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins. J. Mol. Biol. 400:755-767.
    • (2010) J. Mol. Biol. , vol.400 , pp. 755-767
    • Du, Z.1    Liu, Y.2    Wang, C.3
  • 54
    • 0036295886 scopus 로고    scopus 로고
    • Protein-splicing reaction via a thiazolidine intermediate: Crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides
    • DOI 10.1006/jmbi.2001.5357
    • Mizutani, R., S. Nogami,..., Y. Satow. 2002. Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides. J. Mol. Biol. 316:919-929. (Pubitemid 34722131)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.4 , pp. 919-929
    • Mizutani, R.1    Nogami, S.2    Kawasaki, M.3    Ohya, Y.4    Anraku, Y.5    Satow, Y.6
  • 55
    • 0034595699 scopus 로고    scopus 로고
    • Structural insights into the protein splicing mechanism of PI-SceI
    • DOI 10.1074/jbc.275.22.16408
    • Poland, B. W., M. Q. Xu, and F. A. Quiocho. 2000. Structural insights into the protein splicing mechanism of PI-SceI. J. Biol. Chem. 275:16408-16413. (Pubitemid 30398859)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16408-16413
    • Poland, B.W.1    Xu, M.-Q.2    Quiocho, F.A.3
  • 56
    • 0034697993 scopus 로고    scopus 로고
    • Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI
    • Ichiyanagi, K., Y Ishino,..., K. Morikawa. 2000. Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI. J. Mol. Biol. 300:889-901.
    • (2000) J. Mol. Biol. , vol.300 , pp. 889-901
    • Ichiyanagi, K.1    Ishino, Y.2    Morikawa, K.3
  • 58
    • 84961979054 scopus 로고    scopus 로고
    • Identifying the reaction mechanisms of inteins with QM/MM multiscale methods
    • Shemella, P. T., and S. K. Nayak. 2010. Identifying the reaction mechanisms of inteins with QM/MM multiscale methods. In Computational Modeling in Biomechanics. 469-489.
    • (2010) Computational Modeling in Biomechanics , pp. 469-489
    • Shemella, P.T.1    Nayak, S.K.2
  • 59
    • 67650480533 scopus 로고    scopus 로고
    • Protein autoproteolysis: Conformational strain linked to the rate of peptide cleavage by the pH dependence of the N → O acyl shift reaction
    • Johansson, D. G. A., G. Wallin,..., T. Härd. 2009. Protein autoproteolysis: conformational strain linked to the rate of peptide cleavage by the pH dependence of the N → O acyl shift reaction. J. Am. Chem. Soc. 131:9475-9477.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9475-9477
    • Johansson, D.G.A.1    Wallin, G.2    Härd, T.3
  • 60
    • 0030665811 scopus 로고    scopus 로고
    • The partial charge of the nitrogen atom in peptide bonds
    • Milner-White, E. J. 1997. The partial charge of the nitrogen atom in peptide bonds. Protein Sci. 6:2477-2482. (Pubitemid 27490762)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2477-2482
    • Milner-White, E.J.1
  • 61
    • 85031220654 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 62
    • 33947405744 scopus 로고    scopus 로고
    • Solvation free energy of amino acids and side-chain analogues
    • DOI 10.1021/jp0620163
    • Chang, J., A. M. Lenhoff, and S. I. Sandler. 2007. Solvation free energy of amino acids and side-chain analogues. J. Phys. Chem. B. 111:2098-2106. (Pubitemid 46456207)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.8 , pp. 2098-2106
    • Chang, J.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 63
    • 33846247813 scopus 로고    scopus 로고
    • Quantifying the protein core flexibility through analysis of cavity formation
    • Pereira, B., S. Jain, and S. Garde. 2006. Quantifying the protein core flexibility through analysis of cavity formation. J. Chem. Phys. 124:74704.
    • (2006) J. Chem. Phys. , vol.124 , pp. 74704
    • Pereira, B.1    Jain, S.2    Garde, S.3
  • 64
    • 85031225613 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 65
    • 0011083499 scopus 로고
    • Intermolecular interactions from a natural bond orbital, donor-acceptor viewpoint
    • Reed, A. E., L. A. Curtiss, and F Weinhold. 1988. Intermolecular interactions from a natural bond orbital, donor-acceptor viewpoint. Chem. Rev. 88:899-926.
    • (1988) Chem. Rev. , vol.88 , pp. 899-926
    • Reed, A.E.1    Curtiss, L.A.2    Weinhold, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.