메뉴 건너뛰기




Volumn 49, Issue 29, 2010, Pages 6247-6262

Widespread but small-scale changes in the structural and dynamic properties of vaccinia virus poly(A) polymerase upon association with its processivity factor in solution

Author keywords

[No Author keywords available]

Indexed keywords

ALL-ATOM SIMULATIONS; AMIDE PROTON; ATOMIC FLUCTUATIONS; C-TERMINAL DOMAINS; COOLING EFFECTS; DEGREE OF CORRELATIONS; DEGREE OF DISORDER; DEPROTECTION; DEUTERATIONS; DYNAMIC PROPERTY; HYDROGEN BONDINGS; HYDROGEN-DEUTERIUM EXCHANGE; LANGEVIN DYNAMICS; N-AND C-TERMINAL DOMAINS; NEGATIVE CORRELATION; PROCESSIVITY; RELAXATION TO EQUILIBRIUM; VACCINIA VIRUS; X RAY CRYSTAL STRUCTURES;

EID: 77954821226     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100166x     Document Type: Article
Times cited : (4)

References (63)
  • 1
    • 0025771504 scopus 로고
    • Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus
    • Gershon, P. D., Ahn, B.-Y., Garfield, M., and Moss, B. (1991) Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus Cell 66, 1269-1278
    • (1991) Cell , vol.66 , pp. 1269-1278
    • Gershon, P.D.1    Ahn, B.-Y.2    Garfield, M.3    Moss, B.4
  • 2
    • 0026781188 scopus 로고
    • Transition from rapid processive to slow non-processive polyadenylation by vaccinia virus poly(A) polymerase catalytic subunit is regulated by the net length of the poly(A) tail
    • Gershon, P. D. and Moss, B. (1992) Transition from rapid processive to slow non-processive polyadenylation by vaccinia virus poly(A) polymerase catalytic subunit is regulated by the net length of the poly(A) tail Genes Dev. 6, 1575-1586
    • (1992) Genes Dev. , vol.6 , pp. 1575-1586
    • Gershon, P.D.1    Moss, B.2
  • 3
    • 1642381309 scopus 로고    scopus 로고
    • Molecular flexibility and discontinuous translocation of a non-templated polymerase
    • Johnson, L., Liu, S., and Gershon, P. D. (2004) Molecular flexibility and discontinuous translocation of a non-templated polymerase J. Mol. Biol. 337, 843-885
    • (2004) J. Mol. Biol. , vol.337 , pp. 843-885
    • Johnson, L.1    Liu, S.2    Gershon, P.D.3
  • 4
    • 34547097537 scopus 로고    scopus 로고
    • Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition
    • Yoshizawa, J., Li, C., and Gershon, P. D. (2007) Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition J. Biol. Chem. 282, 19144-19151
    • (2007) J. Biol. Chem. , vol.282 , pp. 19144-19151
    • Yoshizawa, J.1    Li, C.2    Gershon, P.D.3
  • 5
    • 0031993338 scopus 로고    scopus 로고
    • Structural basis for sequence non-specific recognition of 5′-capped mRNA by a cap modifying enzyme
    • Hodel, A. E., Gershon, P. D., and Quiocho, F. A. (1998) Structural basis for sequence non-specific recognition of 5′-capped mRNA by a cap modifying enzyme Mol. Cell 1, 443-447
    • (1998) Mol. Cell , vol.1 , pp. 443-447
    • Hodel, A.E.1    Gershon, P.D.2    Quiocho, F.A.3
  • 6
    • 0029665054 scopus 로고    scopus 로고
    • The 1.85 structure of vaccinia protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends
    • Hodel, A. E., Gershon, P. D., Shi, X., and Quiocho, F. A. (1996) The 1.85 structure of vaccinia protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends Cell 85, 247-256
    • (1996) Cell , vol.85 , pp. 247-256
    • Hodel, A.E.1    Gershon, P.D.2    Shi, X.3    Quiocho, F.A.4
  • 7
    • 0033168555 scopus 로고    scopus 로고
    • RNA binding characteristics and overall topology of the vaccinia poly(A) polymerase-processivity factor complex
    • Johnson, L. and Gershon, P. D. (1999) RNA binding characteristics and overall topology of the vaccinia poly(A) polymerase-processivity factor complex Nucleic Acids Res. 27, 2708-2721
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2708-2721
    • Johnson, L.1    Gershon, P.D.2
  • 8
    • 33646164166 scopus 로고    scopus 로고
    • Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: Insights into ATP selectivity and processivity
    • Moure, C. M., Bowman, B. R., Gershon, P. D., and Quiocho, F. A. (2006) Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: Insights into ATP selectivity and processivity Mol. Cell 33, 339-349
    • (2006) Mol. Cell , vol.33 , pp. 339-349
    • Moure, C.M.1    Bowman, B.R.2    Gershon, P.D.3    Quiocho, F.A.4
  • 9
    • 28644431836 scopus 로고    scopus 로고
    • Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei
    • Deng, J., Ernst, N. L., Turley, S., Stuart, K. D., and Hol, W. G. (2005) Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei EMBO J. 24, 4007-4017
    • (2005) EMBO J. , vol.24 , pp. 4007-4017
    • Deng, J.1    Ernst, N.L.2    Turley, S.3    Stuart, K.D.4    Hol, W.G.5
  • 11
    • 65149098522 scopus 로고    scopus 로고
    • Polymerase translocation with respect to single-stranded nucleic acid: Looping or wrapping of primer around a poly(A) polymerase
    • Li, C.-Z., Li, H., Zhou, S.-F., Sun, E., Yoshizawa, J., Poulos, T. L., and Gershon, P. D. (2009) Polymerase translocation with respect to single-stranded nucleic acid: Looping or wrapping of primer around a poly(A) polymerase Structure 17, 1-10
    • (2009) Structure , vol.17 , pp. 1-10
    • Li, C.-Z.1    Li, H.2    Zhou, S.-F.3    Sun, E.4    Yoshizawa, J.5    Poulos, T.L.6    Gershon, P.D.7
  • 12
    • 0031137290 scopus 로고    scopus 로고
    • Specific protein recognition of an mRNA cap through its alkylated base
    • Hodel, A. E., Gershon, P. D., Shi, X., Wang, S.-M., and Quiocho, F. A. (1997) Specific protein recognition of an mRNA cap through its alkylated base Nat. Struct. Biol. 4, 350-354
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 350-354
    • Hodel, A.E.1    Gershon, P.D.2    Shi, X.3    Wang, S.-M.4    Quiocho, F.A.5
  • 13
    • 4243921927 scopus 로고
    • Lane Medical Lectures
    • In, Stanford University Press, Palo Alto, CA
    • Linderstrøm-Lang, K. (1952) Lane Medical Lectures. In Proteins and Enzymes, Stanford University Press, Palo Alto, CA.
    • (1952) Proteins and Enzymes
    • Linderstrøm-Lang, K.1
  • 14
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. and Nielsen, S. O. (1966) Hydrogen exchange in proteins Adv. Protein Chem. 21, 287-386
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 17
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T. E. and Engen, J. R. (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics Mass Spectrom. Rev. 25, 158-170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 18
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J. C., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 19
    • 53349173099 scopus 로고    scopus 로고
    • TOF2H: A precision toolbox for rapid, high density/high coverage hydrogen-deuterium exchange mass spectrometry via an LC-MALDI approach, covering the data pipeline from spectral acquisition to HDX rate analysis
    • Nikamanon, P., Pun, E., Chou, W., Koter, M., and Gershon, P. D. (2008) TOF2H: A precision toolbox for rapid, high density/high coverage hydrogen-deuterium exchange mass spectrometry via an LC-MALDI approach, covering the data pipeline from spectral acquisition to HDX rate analysis BMC Bioinf. 9, 387
    • (2008) BMC Bioinf. , vol.9 , pp. 387
    • Nikamanon, P.1    Pun, E.2    Chou, W.3    Koter, M.4    Gershon, P.D.5
  • 20
    • 1942535471 scopus 로고    scopus 로고
    • Efficient approximate all-atom solvent accessible surface area method parameterized for folded and denatured protein conformations
    • Guvench, G. and Brooks, C. L., III (2004) Efficient approximate all-atom solvent accessible surface area method parameterized for folded and denatured protein conformations J. Comput. Chem. 25, 1005-1014
    • (2004) J. Comput. Chem. , vol.25 , pp. 1005-1014
    • Guvench, G.1    Brooks III, C.L.2
  • 21
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser, A., Do, R. K., and Sali, A. (2000) Modeling of loops in protein structures Protein Sci. 9, 1753-1773
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 33646940952 scopus 로고
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of N-Alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical-Integration of Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of N-Alkanes J. Comput. Phys. 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 26
    • 34447628760 scopus 로고    scopus 로고
    • Regions of I-Bα that are critical for its inhibition of NF-B DNA interaction fold upon binding to NF-B
    • Truhlar, S. M. E., Torpey, J. W., and Komives, E. A. (2006) Regions of I-Bα that are critical for its inhibition of NF-B DNA interaction fold upon binding to NF-B Proc. Natl. Acad. Sci. U.S.A. 103, 18951-18956
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18951-18956
    • Truhlar, S.M.E.1    Torpey, J.W.2    Komives, E.A.3
  • 27
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W. and Kallenbach, N. (1984) Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16, 521-655
    • (1984) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.2
  • 28
    • 0033200247 scopus 로고    scopus 로고
    • Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function
    • Ishima, R., Freedberg, D. I., Wang, Y. X., Louis, J. M., and Torchia, D. A. (1999) Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function Structure 7, 1047-1055
    • (1999) Structure , vol.7 , pp. 1047-1055
    • Ishima, R.1    Freedberg, D.I.2    Wang, Y.X.3    Louis, J.M.4    Torchia, D.A.5
  • 29
    • 32244437816 scopus 로고    scopus 로고
    • HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations
    • Hornak, V., Okur, A., Rizzo, R. C., and Simmerling, C. (2006) HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations Proc. Natl. Acad. Sci. U.S.A. 103, 915-920
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 915-920
    • Hornak, V.1    Okur, A.2    Rizzo, R.C.3    Simmerling, C.4
  • 30
    • 33749507175 scopus 로고    scopus 로고
    • Hydrogen-deuterium exchange analyzed by matrix-assisted laser desorption-ionization mass spectrometry and the HET-s prion model
    • Nazabal, A. and Schmitter, J.-M. (2006) Hydrogen-deuterium exchange analyzed by matrix-assisted laser desorption-ionization mass spectrometry and the HET-s prion model Methods Enzymol. 413, 167-181
    • (2006) Methods Enzymol. , vol.413 , pp. 167-181
    • Nazabal, A.1    Schmitter, J.-M.2
  • 31
    • 0035936693 scopus 로고    scopus 로고
    • Hydrogen-deuterium exchange as a probe of folding and assembly in viral capsids
    • Tuma, R., Coward, L., Kirk, M., Barnes, S., and Prevelige, P. J. (2001) Hydrogen-deuterium exchange as a probe of folding and assembly in viral capsids J. Mol. Biol. 306, 389-396
    • (2001) J. Mol. Biol. , vol.306 , pp. 389-396
    • Tuma, R.1    Coward, L.2    Kirk, M.3    Barnes, S.4    Prevelige, P.J.5
  • 33
    • 47049086608 scopus 로고    scopus 로고
    • Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain
    • Betts, G. N., van der Geer, P., and Komives, E. A. (2008) Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain J. Biol. Chem. 283, 15656-15664
    • (2008) J. Biol. Chem. , vol.283 , pp. 15656-15664
    • Betts, G.N.1    Van Der Geer, P.2    Komives, E.A.3
  • 35
    • 0035815111 scopus 로고    scopus 로고
    • Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB
    • Hughes, C. A., Mandell, J. G., Anand, G. S., Stock, A. M., and Komives, E. A. (2001) Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB J. Mol. Biol. 307, 967-976
    • (2001) J. Mol. Biol. , vol.307 , pp. 967-976
    • Hughes, C.A.1    Mandell, J.G.2    Anand, G.S.3    Stock, A.M.4    Komives, E.A.5
  • 36
    • 3042628330 scopus 로고    scopus 로고
    • Biophysical characterization of the free I-Bα ankyrin repeat domain in solution
    • Hughes Croy, C., Bergqvist, S., Huxford, T., Ghosh, G., and Komives, E. A. (2004) Biophysical characterization of the free I-Bα ankyrin repeat domain in solution Protein Sci. 13, 1767-1777
    • (2004) Protein Sci. , vol.13 , pp. 1767-1777
    • Hughes Croy, C.1    Bergqvist, S.2    Huxford, T.3    Ghosh, G.4    Komives, E.A.5
  • 38
    • 33746921279 scopus 로고    scopus 로고
    • Amide H/2H exchange reveals a mechanism of thrombin activation
    • Koeppe, J. R. and Komives, E. A. (2006) Amide H/2H exchange reveals a mechanism of thrombin activation Biochemistry 45, 7724-7732
    • (2006) Biochemistry , vol.45 , pp. 7724-7732
    • Koeppe, J.R.1    Komives, E.A.2
  • 39
    • 33744962772 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in the acetylcholine-binding protein analyzed by hydrogen-deuterium exchange mass spectrometry
    • Shi, J., Koeppe, J. R., Komives, E. A., and Taylor, P. (2006) Ligand-induced conformational changes in the acetylcholine-binding protein analyzed by hydrogen-deuterium exchange mass spectrometry J. Biol. Chem. 281, 12170-12177
    • (2006) J. Biol. Chem. , vol.281 , pp. 12170-12177
    • Shi, J.1    Koeppe, J.R.2    Komives, E.A.3    Taylor, P.4
  • 41
    • 0036025308 scopus 로고    scopus 로고
    • Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the RIa subunit of protein kinase A
    • Anand, G. S., Hughes, C. A., Jones, J. M., Taylor, S. S., and Komives, E. A. (2002) Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the RIa subunit of protein kinase A J. Mol. Biol. 323, 377-386
    • (2002) J. Mol. Biol. , vol.323 , pp. 377-386
    • Anand, G.S.1    Hughes, C.A.2    Jones, J.M.3    Taylor, S.S.4    Komives, E.A.5
  • 42
    • 2442419061 scopus 로고    scopus 로고
    • Allosteric changes in solvent accessibility observed in thrombin upon active site occupation
    • Croy, C. H., Koeppe, J. R., Bergqvist, S., and Komives, E. A. (2004) Allosteric changes in solvent accessibility observed in thrombin upon active site occupation Biochemistry 43, 5246-5255
    • (2004) Biochemistry , vol.43 , pp. 5246-5255
    • Croy, C.H.1    Koeppe, J.R.2    Bergqvist, S.3    Komives, E.A.4
  • 43
    • 33750329946 scopus 로고    scopus 로고
    • Solvent accessibility of protein surfaces by amide H/2H exchange MALDI-TOF mass spectrometry
    • Truhlar, S. M., Croy, C. H., Torpey, J. W., Koeppe, J. R., and Komives, E. A. (2006) Solvent accessibility of protein surfaces by amide H/2H exchange MALDI-TOF mass spectrometry J. Am. Soc. Mass Spectrom. 17, 1490-1497
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1490-1497
    • Truhlar, S.M.1    Croy, C.H.2    Torpey, J.W.3    Koeppe, J.R.4    Komives, E.A.5
  • 44
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • Yan, X., Watson, J., Ho, P. S., and Deinzer, M. L. (2004) Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes Mol. Cell. Proteomics 3, 10-23
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 10-23
    • Yan, X.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 45
    • 0022426014 scopus 로고
    • Protein Hydrogen Exchange Studied by the Fragment Separation Method
    • Englander, J. J., Rogero, J. R., and Englander, S. W. (1985) Protein Hydrogen Exchange Studied by the Fragment Separation Method Anal. Biochem. 147, 234-244
    • (1985) Anal. Biochem. , vol.147 , pp. 234-244
    • Englander, J.J.1    Rogero, J.R.2    Englander, S.W.3
  • 47
    • 0942290634 scopus 로고    scopus 로고
    • Dynamics and Ligand-Induced Solvent Accessibility Changes in Human Retinoid X Receptor Homodimer Determined by Hydrogen Deuterium Exchange and Mass Spectrometry
    • Yan, X., Broderick, D., Leid, M. E., Schimerlik, M. I., and Deinzer, M. L. (2004) Dynamics and Ligand-Induced Solvent Accessibility Changes in Human Retinoid X Receptor Homodimer Determined by Hydrogen Deuterium Exchange and Mass Spectrometry Biochemistry 43, 909-917
    • (2004) Biochemistry , vol.43 , pp. 909-917
    • Yan, X.1    Broderick, D.2    Leid, M.E.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 48
    • 0028943576 scopus 로고
    • Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia coli thioredoxin
    • Jeng, M.-F. and Dyson, H. J. (1995) Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia coli thioredoxin Biochemistry 34, 611-619
    • (1995) Biochemistry , vol.34 , pp. 611-619
    • Jeng, M.-F.1    Dyson, H.J.2
  • 49
    • 0036707994 scopus 로고    scopus 로고
    • H/D exchange and mass spectrometric analysis of a protein containing multiple disulfide bonds: Solution structure of recombinant macrophage colony stimulating factor-β (rhM-CSF)
    • Yan, X., Zhang, H., Watson, J., Schimerlik, M. I., and Deinzer, M. L. (2002) H/D exchange and mass spectrometric analysis of a protein containing multiple disulfide bonds: Solution structure of recombinant macrophage colony stimulating factor-β (rhM-CSF) Protein Sci. 11, 2113-2124
    • (2002) Protein Sci. , vol.11 , pp. 2113-2124
    • Yan, X.1    Zhang, H.2    Watson, J.3    Schimerlik, M.I.4    Deinzer, M.L.5
  • 50
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R. and Wraun, B. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comput. Chem. 19, 319-19333
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-19333
    • Fraczkiewicz, R.1    Wraun, B.2
  • 51
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M. L. (1983) Solvent-accessible surfaces of proteins and nucleic acids Science 221, 709-713
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 53
    • 33947720248 scopus 로고    scopus 로고
    • A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation
    • Olsen, O. H., Rand, K. D., stergaard, H., and Persson, E. (2007) A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation Protein Sci. 16, 671-682
    • (2007) Protein Sci. , vol.16 , pp. 671-682
    • Olsen, O.H.1    Rand, K.D.2    Stergaard, H.3    Persson, E.4
  • 54
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita, O., Onuchic, J. N., and Wolynes, P. G. (2003) Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins Proc. Natl. Acad. Sci. U.S.A. 100, 12570-12575
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 55
    • 0141754098 scopus 로고    scopus 로고
    • Gating of MscL studied by steered molecular dynamics
    • Gullingsrud, J. and Schulten, K. (2003) Gating of MscL studied by steered molecular dynamics Biophys. J. 85, 2087-2099
    • (2003) Biophys. J. , vol.85 , pp. 2087-2099
    • Gullingsrud, J.1    Schulten, K.2
  • 57
    • 0033515615 scopus 로고    scopus 로고
    • Exploring Structures in Protein Folding Funnels with Free Energy Functional: The Transition State Ensemble
    • Shoemaker, B. A., Wang, J., and Wolynes, P. G. (1999) Exploring Structures in Protein Folding Funnels with Free Energy Functional: The Transition State Ensemble J. Mol. Biol. 287, 675-694
    • (1999) J. Mol. Biol. , vol.287 , pp. 675-694
    • Shoemaker, B.A.1    Wang, J.2    Wolynes, P.G.3
  • 58
    • 0033515614 scopus 로고    scopus 로고
    • Exploring Structures in Protein Folding Funnels with Free Energy Functionals: The Denatured Ensemble
    • Shoemaker, B. A. and Wolynes, P. G. (1999) Exploring Structures in Protein Folding Funnels with Free Energy Functionals: The Denatured Ensemble J. Mol. Biol. 287, 657-674
    • (1999) J. Mol. Biol. , vol.287 , pp. 657-674
    • Shoemaker, B.A.1    Wolynes, P.G.2
  • 59
    • 67650540778 scopus 로고    scopus 로고
    • Location of Inhibitors Bound to Group IVA Phospholipase A2 Determined by Molecular Dynamics and Deuterium Exchange Mass Spectrometry
    • Burke, J. E., Babakhani, A., Gorfe, A. A., Kokotos, G., Li, S., Woods, V. L., Jr., McCammon, J. A., and Dennis, E. A. (2009) Location of Inhibitors Bound to Group IVA Phospholipase A2 Determined by Molecular Dynamics and Deuterium Exchange Mass Spectrometry J. Am. Chem. Soc. 131, 8083-8091
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8083-8091
    • Burke, J.E.1    Babakhani, A.2    Gorfe, A.A.3    Kokotos, G.4    Li, S.5    Woods, Jr.V.L.6    McCammon, J.A.7    Dennis, E.A.8
  • 60
    • 0028609035 scopus 로고
    • Mass-spectrometric measurement of protein amide hydrogen-exchange rates of apo-myoglobin and holo-myoglobin
    • Johnson, R. and Walsh, K. (1994) Mass-spectrometric measurement of protein amide hydrogen-exchange rates of apo-myoglobin and holo-myoglobin Protein Sci. 3, 2411-2418
    • (1994) Protein Sci. , vol.3 , pp. 2411-2418
    • Johnson, R.1    Walsh, K.2
  • 61
    • 0030901492 scopus 로고    scopus 로고
    • Gas phasehydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer
    • Kaltashov, I. A., Doroshenko, V. M., and Cotter, R. J. (1997) Gas phasehydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer Proteins: Struct., Funct., Genet. 28, 53-58
    • (1997) Proteins: Struct., Funct., Genet. , vol.28 , pp. 53-58
    • Kaltashov, I.A.1    Doroshenko, V.M.2    Cotter, R.J.3
  • 62
    • 0027391646 scopus 로고
    • Stimulation of poly(A) tail elongation by the VP39 subunit of the vaccinia virus-encoded poly(A) polymerase
    • Gershon, P. D. and Moss, B. (1993) Stimulation of poly(A) tail elongation by the VP39 subunit of the vaccinia virus-encoded poly(A) polymerase J. Biol. Chem. 268, 2203-2210
    • (1993) J. Biol. Chem. , vol.268 , pp. 2203-2210
    • Gershon, P.D.1    Moss, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.