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Volumn 98, Issue 12, 2010, Pages 2974-2983

Molecular dynamics free energy calculations to assess the possibility of water existence in protein nonpolar cavities

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EID: 77953574626     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.01.029     Document Type: Article
Times cited : (9)

References (62)
  • 1
    • 0023051843 scopus 로고
    • Internal cavities and buried waters in globular proteins
    • Rashin, A. A., M. Iofin, and B. Honig. 1986. Internal cavities and buried waters in globular proteins. Biochemistry. 25:3619-3625.
    • (1986) Biochemistry , vol.25 , pp. 3619-3625
    • Rashin, A.A.1    Iofin, M.2    Honig, B.3
  • 2
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams, M. A., J. M. Goodfellow, and J. M. Thornton. 1994. Buried waters and internal cavities in monomeric proteins. Protein Sci. 3: 1224-1235.
    • (1994) Protein Sci. , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 3
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S. J., K. H. Gross, and P. Argos. 1994. Intramolecular cavities in globular proteins. Protein Eng. 7:613-626.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.H.2    Argos, P.3
  • 5
    • 34748906798 scopus 로고    scopus 로고
    • Long distance electrontransfer mechanism in peptidylglycine α-hydroxylating monooxygenase: A perfect fitting for a water bridge
    • de Ia Lande, A., S. Martí, V. Moliner. 2007. Long distance electrontransfer mechanism in peptidylglycine α-hydroxylating monooxygenase: a perfect fitting for a water bridge. J. Am. Chem. Soc. 129: 11700-11707.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11700-11707
    • De Ia Lande, A.1    Martí, S.2    Moliner, V.3
  • 6
    • 0030828226 scopus 로고    scopus 로고
    • The reorganization energy of cytochrome c revisited
    • Muegge, I., P. X. Qi, A. Warshel, 1997. The reorganization energy of cytochrome c revisited. J. Phys. Chem. B. 101:825-836.
    • (1997) J Phys. Chem. B. , vol.101 , pp. 825-836
    • Muegge, I.1    Qi, P.X.2    Warshel, A.3
  • 7
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: Assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base
    • DOI 10.1016/S0022-2836(03)00576-X
    • Schobert, B., L. S. Brown, and J. K. Lanyi. 2003. Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between. Asp-96 and the retinal Schiff base. J. Mol. Biol. 330:553-570. (Pubitemid 36814053)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 9
    • 0034088779 scopus 로고    scopus 로고
    • The catalytic pathway of cytochrome p450cam at atomic resolution
    • Schlichting, I., J. Berendzen, S. G. Sugar. 2000. The catalytic pathway of cytochrome p450cam at atomic resolution. Science. 287:1615-1622.
    • (2000) Science. , vol.287 , pp. 1615-1622
    • Schlichting, I.1    Berendzen, J.2    Sugar, S.G.3
  • 10
    • 0024278562 scopus 로고
    • Evaluation of catalytic free energies in genetically modified proteins
    • Warshel, A., F. Sussman, and J. K. Hwang. 1988. Evaluation of catalytic free energies in genetically modified proteins. J. Mol. Biol. 201:139-159.
    • (1988) J Mol. Biol. , vol.201 , pp. 139-159
    • Warshel, A.1    Sussman, F.2    Hwang, J.K.3
  • 11
    • 0037246110 scopus 로고    scopus 로고
    • Buried water molecules contribute to the conformational stability of a protein
    • Takano, K., Y. Yamagata, and K. Yutani, 2003. Buried water molecules contribute to the conformational stability of a protein. Protein Eng. 16:5-9.
    • (2003) Protein Eng. , vol.16 , pp. 5-9
    • Takano, K.1    Yamagata, Y.2    Yutani, K.3
  • 12
    • 28044463816 scopus 로고    scopus 로고
    • Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation
    • Collins, M. D., G. Hummer, S. M. Gruner. 2005. Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation. Proc. Natl. Acad. Sci,.USA. 102: 16668-16671.
    • (2005) Proc. Natl. Acad. Sci,.USA. , vol.102 , pp. 16668-16671
    • Collins, M.D.1    Hummer, G.2    Gruner, S.M.3
  • 13
    • 54349114270 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation
    • Ando, N., B. Barstow, S. M. Gruner. 2008. Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation. Biochemistry. 47: 11097-11109.
    • (2008) Biochemistry. , vol.47 , pp. 11097-11109
    • Ando, N.1    Barstow, B.2    Gruner, S.M.3
  • 14
    • 34548397683 scopus 로고    scopus 로고
    • Crystallographic evidence for water-assisted photo-induced peptide cleavage in the stony coral fluorescent protein Kaede
    • Hayashi, I., H. Mizuno, M. Ikura. 2007. Crystallographic evidence for water-assisted photo-induced peptide cleavage in the stony coral fluorescent protein Kaede. J. Mol. Biol. 372:918-926.
    • (2007) J. Mol. Biol. , vol.372 , pp. 918-926
    • Hayashi, I.1    Mizuno, H.2    Ikura, M.3
  • 15
    • 0029757992 scopus 로고    scopus 로고
    • Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: A molecular dynamics free energy perturbation study
    • Roux, B., M. Nina, J. C. Smith. 1996. Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: a molecular dynamics free energy perturbation study. Biophys. J. 71:670-681.
    • (1996) Biophys. J. , vol.71 , pp. 670-681
    • Roux, B.1    Nina, M.2    Smith, J.C.3
  • 16
    • 34250845103 scopus 로고    scopus 로고
    • Metastable water clusters in the nonpolar cavities of the thermostable protein tetrabrachion
    • Yin, H., G. Hummer, and J. C. Rasaiah. 2007. Metastable water clusters in the nonpolar cavities of the thermostable protein tetrabrachion. J. Am. Chem. Soc. 129:7369-7377.
    • (2007) J Am. Chem. Soc. , vol.129 , pp. 7369-7377
    • Yin, H.1    Hummer, G.2    Rasaiah, J.C.3
  • 17
    • 33847655150 scopus 로고    scopus 로고
    • Classification of water molecules in protein binding sites
    • Barillari, C., J. Taylor, J. W. Essex. 2007. Classification of water molecules in protein binding sites. J. Am. Chem. Soc. 129:2577-2587.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2577-2587
    • Barillari, C.1    Taylor, J.2    Essex, J.W.3
  • 18
    • 0033578333 scopus 로고    scopus 로고
    • Binding of buried structural water increases the flexibility of proteins
    • Fischer, S., and C. S. Verma. 1999. Binding of buried structural water increases the flexibility of proteins. Proc. Natl. Acad. Sci. USA. 96:9613-9615.
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 9613-9615
    • Fischer, S.1    Verma, C.S.2
  • 19
    • 0035940247 scopus 로고    scopus 로고
    • Dissecting the vibrational entropy change on protein/ligand binding: Burial of a watermolecule in bovine pancreatic trypsin inhibitor
    • Fischer, S., J. C. Smith and C. S. Verma. 2001. Dissecting the vibrational entropy change on protein/ligand binding: burial of a watermolecule in bovine pancreatic trypsin inhibitor. J. Phys. Chem. B. 105:8050-8055.
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 8050-8055
    • Fischer, S.1    Smith, J.C.2    Verma, C.S.3
  • 20
    • 14744270583 scopus 로고    scopus 로고
    • Protein stability and ligand binding: New paradigms from in-silico experiments
    • Verma, C. S., and S. Fischer. 2005. Protein stability and ligand binding: new paradigms from in-silico experiments. Biophys. Chem. 115:295-302.
    • (2005) Biophys Chem. , vol.115 , pp. 295-302
    • Verma, C.S.1    Fischer, S.2
  • 21
    • 0032529586 scopus 로고    scopus 로고
    • Hydration energy landscape of the active site cavity in cytochrome P450cam
    • Helms, V., and R. C. Wade. 1998. Hydration energy landscape of the active site cavity in cytochrome P450cam. Proteins. 32:381-396.
    • (1998) Proteins. , vol.32 , pp. 381-396
    • Helms, V.1    Wade, R.C.2
  • 22
    • 3042592839 scopus 로고    scopus 로고
    • Hydration free energies and entropies for water in protein interiors
    • Olano, L. R., and S. W. Rick. 2004. Hydration free energies and entropies for water in protein interiors. J. Am. Chem. Soc. 126:7991-8000.
    • (2004) J Am. Chem. Soc. , vol.126 , pp. 7991-8000
    • Olano, L.R.1    Rick, S.W.2
  • 23
    • 21244469736 scopus 로고    scopus 로고
    • Molecular dynamics study of water penetration in staphylococcal nuclease
    • Damjanović, A., B. García-Moreno, A. E. Garcia. 2005. Molecular dynamics study of water penetration in staphylococcal nuclease. Proteins. 60:433-449.
    • (2005) Proteins. , vol.60 , pp. 433-449
    • Damjanović, A.1    García-Moreno, B.2    Garcia, A.E.3
  • 24
    • 23044435317 scopus 로고    scopus 로고
    • Statistical and molecular dynamics studies of buried waters in globular proteins
    • Park, S., and J. G. Saven. 2005. Statistical and molecular dynamics studies of buried waters in globular proteins. Proteins. 60:450-463.
    • (2005) Proteins. , vol.60 , pp. 450-463
    • Park, S.1    Saven, J.G.2
  • 25
    • 0033524454 scopus 로고    scopus 로고
    • Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography
    • Yu, B., M. Blaber, D. L. Caspar. 1999. Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography. Proc. Natl. Acad. Sci. USA. 96:103-108.
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 103-108
    • Yu, B.1    Blaber, M.2    Caspar, D.L.3
  • 26
    • 0028921999 scopus 로고
    • Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR
    • Ernst, J. A., R. T. Clubb, G. M. Clore. 1995. Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science. 267:1813-1817.
    • (1995) Science. , vol.267 , pp. 1813-1817
    • Ernst, J.A.1    Clubb, R.T.2    Clore, G.M.3
  • 27
    • 33845957884 scopus 로고    scopus 로고
    • Determination of solvent content in cavities in IL-1β using experimentally phased electron density
    • Quillin, M. L., P. T. Wingfield, and B. W. Matthews. 2006. Determination of solvent content in cavities in IL-1β using experimentally phased electron density. Proc. Natl. Acad. Sci. USA. 103:19749-19753.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 19749-19753
    • Quillin, M.L.1    Wingfield, P.T.2    Matthews, B.W.3
  • 28
    • 0024368527 scopus 로고
    • Crystal structure of recombinant human interleukin-1 β at 2.0 Å resolution
    • Finzel, B. C., L. L. Clancy, H. M. Einspahr. 1989. Crystal structure of recombinant human interleukin-1 β at 2.0 Å resolution. J. Mol. Biol. 209:779-791.
    • (1989) J. Mol. Biol. , vol.209 , pp. 779-791
    • Finzel, B.C.1    Clancy, L.L.2    Einspahr, H.M.3
  • 29
    • 0026910956 scopus 로고
    • Combining experimental information from crystal and solution studies: Joint x-ray and NMR refinement
    • Shaanan, B., A. M. Gronenborn, G. M. Clore. 1992. Combining experimental information from crystal and solution studies: joint x-ray and NMR refinement. Science. 257:961-964.
    • (1992) Science. , vol.257 , pp. 961-964
    • Shaanan, B.1    Gronenborn, A.M.2    Clore, G.M.3
  • 30
    • 0024804106 scopus 로고
    • Crystallographic refinement of interleukin. 1 β at 2.0 Å resolution
    • Priestle, J. P., H. P. Schär, and M. G. Grütter. 1989. Crystallographic refinement of interleukin. 1 β at 2.0 Å resolution, Proc Natl. Acad. Sci. USA. 86:9667-9671.
    • (1989) Proc Natl. Acad. Sci. USA. , vol.86 , pp. 9667-9671
    • Priestle, J.P.1    Schär, H.P.2    Grütter, M.G.3
  • 31
    • 0026551727 scopus 로고
    • Functional implications of interleukin-1 β based on the three-dimensional structure
    • Veerapandian, B., G. L. Gilliland, T. L. Poulos. 1992. Functional implications of interleukin-1 β based on the three-dimensional structure. Proteins. 12:10-23.
    • (1992) Proteins. , vol.12 , pp. 10-23
    • Veerapandian, B.1    Gilliland, G.L.2    Poulos, T.L.3
  • 32
    • 0025772135 scopus 로고
    • Highresolution three-dimensional structure of interleukin 1 β in solution by three- And four-dimensional nuclear magnetic resonance spectroscopy
    • Clore, G. M., P. T. Wingfield, and A. M. Gronenbom. 1991. Highresolution three-dimensional structure of interleukin 1 β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry. 30:2315-2323.
    • (1991) Biochemistry. , vol.30 , pp. 2315-2323
    • Clore, G.M.1    Wingfield, P.T.2    Gronenbom, A.M.3
  • 33
    • 34248572405 scopus 로고    scopus 로고
    • Hydration of a hydrophobic cavity and its functional role: A simulation study of human interleukin-1
    • DOI 10.1002/prot.21320
    • Somani, S., C. P. Chng, and C. S. Verma. 2007. Hydration of a hydrophobic cavity and its functional role: a simulation study of human interleukin-1β. Proteins. 67:868-885. (Pubitemid 46753935)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.4 , pp. 868-885
    • Somani, S.1    Chng, C.-P.2    Verma, C.S.3
  • 34
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang, L., and J. Hermans. 1996. Hydrophilicity of cavities in proteins. Proteins. 24:433-438.
    • (1996) Proteins. , vol.24 , pp. 433-438
    • Zhang, L.1    Hermans, J.2
  • 36
    • 0033613812 scopus 로고    scopus 로고
    • Visualizing and quantifying molecular goodness-of-fit: Small-probe contact dots with explicit hydrogen atoms
    • Word, J. M., S. C. Lovell, D. C. Richardson. 1999. Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms. J. Mol. Biol. 285:1711-1733.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1711-1733
    • Word, J.M.1    Lovell, S.C.2    Richardson, D.C.3
  • 37
    • 23144438711 scopus 로고    scopus 로고
    • PISCES: Recent improvements to a PDB sequence culling server
    • Wang, G., and R. L. Dunbrack, Jr. 2005. PISCES: recent improvements to a PDB sequence culling server. Nucleic Acids Res. 33:W94-W98.
    • (2005) Nucleic Acids Res. , vol.33
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 38
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M. L. 1993. The molecular surface package. J. Mol. Graph. 11:139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 39
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M. L. 1983. Analytical molecular surface calculation. J. Appl. Cryst. 16:548-558.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 40
    • 0347719364 scopus 로고    scopus 로고
    • Z. Xu
    • Zhu, M., F. Shao, Z. Xu. 2004. The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc. Natl. Acad. Sci. USA. 101:302-307.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 302-307
    • Zhu, M.1    Shao, F.2
  • 41
    • 0023900891 scopus 로고
    • Flexibility of the DNA-binding domains of Trp repressor
    • Lawson, C. L., R. G. Zhang, P. B. Sigler. 1988. Flexibility of the DNA-binding domains of Trp repressor. Proteins. 3:18-31.
    • (1988) Proteins. , vol.3 , pp. 18-31
    • Lawson, C.L.1    Zhang, R.G.2    Sigler, P.B.3
  • 42
    • 0035933311 scopus 로고    scopus 로고
    • Very high-resolution structure of a trematode hemoglobin displaying a TyrB 10-TyrE7 heme distal residue pair and high oxygen affinity
    • Pesce, A., S. Dewilde, M. Bolognesi. 2001, Very high-resolution structure of a trematode hemoglobin displaying a TyrB 10-TyrE7 heme distal residue pair and high oxygen affinity. J. Mol. Biol. 309:1153-1164.
    • (2001) J Mol. Biol. , vol.309 , pp. 1153-1164
    • Pesce, A.1    Dewilde, S.2    Bolognesi, M.3
  • 43
    • 33748252631 scopus 로고    scopus 로고
    • On the use of orientational restraints and symmetry corrections in alchemical free energy calculations
    • Mobley, D. L., J. D. Chodera, and K. A. Dill. 2006. On the use of orientational restraints and symmetry corrections in alchemical free energy calculations. J. Chem. Phys. 125:084902-084916.
    • (2006) J Chem. Phys. , vol.125 , pp. 84902-84916
    • Mobley, D.L.1    Chodera, J.D.2    Dill, K.A.3
  • 44
    • 0000249851 scopus 로고
    • Avoiding singularities and numerical instabilities in free energy calculations based on molecular simulations
    • Beutler, T. C., A. E. Mark, W. F. van Gunsteren. 1994. Avoiding singularities and numerical instabilities in free energy calculations based on molecular simulations. Chem. Phys. Lett. 222:529-539.
    • (1994) Chem. Phys. Lett. , vol.222 , pp. 529-539
    • Beutler, T.C.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 45
  • 46
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L., D. S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 47
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparameterization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G. A., R. A. Friesner, W. L. Jorgensen. 2001. Evaluation and reparameterization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487.
    • (2001) J Phys. Chem. B. , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Jorgensen, W.L.3
  • 48
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W. L., J. Chandrasekhar, M. L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 49
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N·log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 50
    • 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., A. Villa, W. F. van Gunsteren. 2004. 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) J Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Van Gunsteren, W.F.3
  • 52
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 54
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma, J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81: 3684-3690.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 55
    • 0028948786 scopus 로고
    • Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion
    • Denisov, V. P., and B. Halle. 1995. Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245:682-697.
    • (1995) J. Mol. Biol. , vol.245 , pp. 682-697
    • Denisov, V.P.1    Halle, B.2
  • 56
    • 0029081424 scopus 로고
    • Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant
    • Denisov, V. P., B. Halle, H. D. Hörlein. 1995. Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant. Biochemistry. 34:9046-9051.
    • (1995) Biochemistry. , vol.34 , pp. 9046-9051
    • Denisov, V.P.1    Halle, B.2    Hörlein, H.D.3
  • 57
    • 0029561720 scopus 로고
    • Use of NMR to detect water within nonpolar protein cavities
    • Matthews, B. W., A. G. Morton, and F. W. Dahlquist. 1995. Use of NMR to detect water within nonpolar protein cavities. Science. 270:1847-1849.
    • (1995) Science. , vol.270 , pp. 1847-1849
    • Matthews, B.W.1    Morton, A.G.2    Dahlquist, F.W.3
  • 58
    • 4644298947 scopus 로고    scopus 로고
    • Accelerated exchange of a buried water molecule in selectively disulfide-reduced bovine pancreatic trypsin inhibitor
    • Denisov, V. P., J. Peters, B. Halle. 2004. Accelerated exchange of a buried water molecule in selectively disulfide-reduced bovine pancreatic trypsin inhibitor. Biochemistry. 43:12020-12027.
    • (2004) Biochemistry. , vol.43 , pp. 12020-12027
    • Denisov, V.P.1    Peters, J.2    Halle, B.3
  • 59
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • Denisov, V. P., J. Peters, B. Halle. 1996. Using buried water molecules to explore the energy landscape of proteins. Nat. Struct. Biol. 3:505-509.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 505-509
    • Denisov, V.P.1    Peters, J.2    Halle, B.3
  • 60
    • 0034651984 scopus 로고    scopus 로고
    • Water penetration and escape in proteins
    • García, A. E., and G. Hummer. 2000. Water penetration and escape in proteins. Proteins. 38:261-272.
    • (2000) Proteins. , vol.38 , pp. 261-272
    • García, A.E.1    Hummer, G.2
  • 61
    • 33745685012 scopus 로고    scopus 로고
    • Using a charging coordinate in studies of ionization induced partial unfolding
    • Kato, M., and A. Warshel, 2006. Using a charging coordinate in studies of ionization induced partial unfolding. J. Phys. Chem. B. 110: 11566-11570.
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 11566-11570
    • Kato, M.1    Warshel, A.2
  • 62
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., A. Dalke, and K. Schulten. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14:33-38, 27-28.
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.