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Volumn 67, Issue 4, 2007, Pages 868-885

Hydration of a hydrophobic cavity and its functional role: A simulation study of human interleukin-1β

Author keywords

Correlated motions; Exchange pathway; Hydrophobic cavity; Interleukin 1 ; Molecular dynamics; Water clusters

Indexed keywords

INTERLEUKIN 1BETA; WATER;

EID: 34248572405     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21320     Document Type: Article
Times cited : (21)

References (70)
  • 1
    • 23044435317 scopus 로고    scopus 로고
    • Statistical and molecular dynamics studies of buried waters in globular proteins
    • Park S, Saven JG. Statistical and molecular dynamics studies of buried waters in globular proteins. Proteins 2005;60:450-46.
    • (2005) Proteins , vol.60 , pp. 450-446
    • Park, S.1    Saven, J.G.2
  • 2
    • 13244260957 scopus 로고    scopus 로고
    • Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase
    • Tashiro M, Stuchebrukhov AA. Thermodynamic properties of internal water molecules in the hydrophobic cavity around the catalytic center of cytochrome c oxidase. J Phys Chem B 2005;109:1015-1022.
    • (2005) J Phys Chem B , vol.109 , pp. 1015-1022
    • Tashiro, M.1    Stuchebrukhov, A.A.2
  • 3
    • 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
    • Schobert B, Brown LS, Lanyi JK. 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 2003;330:553-570.
    • (2003) J Mol Biol , vol.330 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 4
    • 0033578333 scopus 로고    scopus 로고
    • Binding of buried structural water increases the flexibility of proteins
    • Fischer S, Verma CS. Binding of buried structural water increases the flexibility of proteins. Proc Natl Acad Sci USA 1999;96:9613-9615.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9613-9615
    • Fischer, S.1    Verma, C.S.2
  • 5
    • 0035940247 scopus 로고    scopus 로고
    • Dissecting the vibrational entropy change on protein/ligand binding: Burial of a water
    • Fischer S, Smith JC, Verma CS. Dissecting the vibrational entropy change on protein/ligand binding: burial of a water. J Phys Chem B 2001;105:8050-8055.
    • (2001) J Phys Chem B , vol.105 , pp. 8050-8055
    • Fischer, S.1    Smith, J.C.2    Verma, C.S.3
  • 6
    • 3042592839 scopus 로고    scopus 로고
    • Hydration free energies and entropies for water in protein interiors
    • Olano LR, Rick SW. Hydration free energies and entropies for water in protein interiors. J Am Chem Soc 2004;126:7991-8000.
    • (2004) J Am Chem Soc , vol.126 , pp. 7991-8000
    • Olano, L.R.1    Rick, S.W.2
  • 7
    • 1842534583 scopus 로고    scopus 로고
    • MHC-peptide binding is assisted by bound water molecules
    • Petrone PM, Garcia AE. MHC-peptide binding is assisted by bound water molecules. J Mol Biol 2004;338:419-435.
    • (2004) J Mol Biol , vol.338 , pp. 419-435
    • Petrone, P.M.1    Garcia, A.E.2
  • 8
    • 0027918556 scopus 로고
    • Water: Now you see it, now you don't
    • Levitt M, Park BH. Water: now you see it, now you don't. Structure 1993;1:223-226.
    • (1993) Structure , vol.1 , pp. 223-226
    • Levitt, M.1    Park, B.H.2
  • 9
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle AM, Cramer P, Fersht AR. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry 1996;35:4298-4305.
    • (1996) Biochemistry , vol.35 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 10
    • 0033524454 scopus 로고    scopus 로고
    • Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography
    • Yu B, Blaber M, Gronenborn AM, Clore GM, Caspar DLD. Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography. Proc Natl Acad Sci USA 1999;96:103-108.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 103-108
    • Yu, B.1    Blaber, M.2    Gronenborn, A.M.3    Clore, G.M.4    Caspar, D.L.D.5
  • 11
    • 0037974485 scopus 로고    scopus 로고
    • Posttransition state desolvation of the hydrophobic core of the src-SH3 protein domain
    • Guo W, Lampoudi S, Shea JE. Posttransition state desolvation of the hydrophobic core of the src-SH3 protein domain. Biophys J 2003;85:61-69.
    • (2003) Biophys J , vol.85 , pp. 61-69
    • Guo, W.1    Lampoudi, S.2    Shea, J.E.3
  • 12
    • 0028093141 scopus 로고
    • On the probability of finding a water molecule in a nonpolar cavity
    • Wolfenden R, Radzicka. On the probability of finding a water molecule in a nonpolar cavity. Science 1994;265:936-937.
    • (1994) Science , vol.265 , pp. 936-937
    • Wolfenden, R.1    Radzicka2
  • 13
    • 0029937870 scopus 로고    scopus 로고
    • Hydrophilicity of cavities in proteins
    • Zhang L, Hermans J. Hydrophilicity of cavities in proteins. Proteins 1996;24:433-438.
    • (1996) Proteins , vol.24 , pp. 433-438
    • Zhang, L.1    Hermans, J.2
  • 14
    • 0026189146 scopus 로고
    • A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins
    • Wade R, Mazor M, McCammon J, Quiocho F. A molecular dynamics study of thermodynamic and structural aspects of the hydration of cavities in proteins. Biopolymers 1991;31:919-931.
    • (1991) Biopolymers , vol.31 , pp. 919-931
    • Wade, R.1    Mazor, M.2    McCammon, J.3    Quiocho, F.4
  • 16
    • 0026549038 scopus 로고
    • Analysis of solvent structure in proteins using neutron D2O-H2O solvent maps: Pattern of primary and secondary hydration of trypsin
    • Kossiakoff AA, Sintchak MD, Shpungin J, Presta LG. Analysis of solvent structure in proteins using neutron D2O-H2O solvent maps: pattern of primary and secondary hydration of trypsin. Proteins 1992;12:223-236.
    • (1992) Proteins , vol.12 , pp. 223-236
    • Kossiakoff, A.A.1    Sintchak, M.D.2    Shpungin, J.3    Presta, L.G.4
  • 17
    • 0028921999 scopus 로고
    • Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR
    • Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM. Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR. Science 1995;267:1813-1817.
    • (1995) Science , vol.267 , pp. 1813-1817
    • Ernst, J.A.1    Clubb, R.T.2    Zhou, H.X.3    Gronenborn, A.M.4    Clore, G.M.5
  • 18
    • 0030892956 scopus 로고    scopus 로고
    • NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules
    • Otting G, Liepinsh E, Halle B, Frey U. NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules. Nature 1997;85:396-404.
    • (1997) Nature , vol.85 , pp. 396-404
    • Otting, G.1    Liepinsh, E.2    Halle, B.3    Frey, U.4
  • 19
    • 0141456396 scopus 로고    scopus 로고
    • Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments
    • Cai S, Stevens SY, Budor AP, Zuiderweg ER. Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments. Biochemistry 2003;42:11100-11108.
    • (2003) Biochemistry , vol.42 , pp. 11100-11108
    • Cai, S.1    Stevens, S.Y.2    Budor, A.P.3    Zuiderweg, E.R.4
  • 20
    • 0029561720 scopus 로고
    • Use of NMR to detect water within nonpolar protein cavities
    • Matthews BW, Morton AG, Dahlquist FW. Use of NMR to detect water within nonpolar protein cavities. Science 1995;270:1847-1848.
    • (1995) Science , vol.270 , pp. 1847-1848
    • Matthews, B.W.1    Morton, A.G.2    Dahlquist, F.W.3
  • 22
    • 21244469736 scopus 로고    scopus 로고
    • Molecular dynamics study of water penetration in staphylococcal nuclease
    • Damjanovic A, Garcia-Moreno B, Lattman EE, Garcia AE. Molecular dynamics study of water penetration in staphylococcal nuclease. Proteins 2005;60:433-449.
    • (2005) Proteins , vol.60 , pp. 433-449
    • Damjanovic, A.1    Garcia-Moreno, B.2    Lattman, E.E.3    Garcia, A.E.4
  • 23
    • 28044463816 scopus 로고    scopus 로고
    • Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation
    • Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM. Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation. Proc Natl Acad Sci USA 2005;102:16668-16671.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16668-16671
    • Collins, M.D.1    Hummer, G.2    Quillin, M.L.3    Matthews, B.W.4    Gruner, S.M.5
  • 24
    • 0037726809 scopus 로고    scopus 로고
    • Water-gated mechanism of proton translocation by cytochrome c oxidase
    • Wikstrom M, Verkhovsky MI, Hummer G. Water-gated mechanism of proton translocation by cytochrome c oxidase. Biochim Biophys Acta 2003;1604:61-65.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 61-65
    • Wikstrom, M.1    Verkhovsky, M.I.2    Hummer, G.3
  • 25
    • 14744270583 scopus 로고    scopus 로고
    • Protein stability and ligand binding: New paradigms from in-silico experiments
    • Verma CS, Fischer S. Protein stability and ligand binding: new paradigms from in-silico experiments. Biophys Chem 2005;115(2/3):295-302.
    • (2005) Biophys Chem , vol.115 , Issue.2-3 , pp. 295-302
    • Verma, C.S.1    Fischer, S.2
  • 26
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • Denisov VP, Peters J, Horlein HD, Halle B. Using buried water molecules to explore the energy landscape of proteins. Nat Struct Biol 1996;3:505-509.
    • (1996) Nat Struct Biol , vol.3 , pp. 505-509
    • Denisov, V.P.1    Peters, J.2    Horlein, H.D.3    Halle, B.4
  • 27
    • 0037198650 scopus 로고    scopus 로고
    • Hydrophobicity: Two faces of water
    • Chandler D. Hydrophobicity: two faces of water. Nature 2002;417:491.
    • (2002) Nature , vol.417 , pp. 491
    • Chandler, D.1
  • 28
    • 0034651984 scopus 로고    scopus 로고
    • Water penetration and escape in proteins
    • Garcia AE, Hummer G. Water penetration and escape in proteins. Proteins 2000;38:261-272.
    • (2000) Proteins , vol.38 , pp. 261-272
    • Garcia, A.E.1    Hummer, G.2
  • 29
    • 0036606442 scopus 로고    scopus 로고
    • Water in protein cavities: A procedure to identify internal water and exchange pathways and application to fatty acid-binding protein
    • Bakowies D, van Gunsteren WF. Water in protein cavities: a procedure to identify internal water and exchange pathways and application to fatty acid-binding protein. Proteins 2002;47: 534-545.
    • (2002) Proteins , vol.47 , pp. 534-545
    • Bakowies, D.1    van Gunsteren, W.F.2
  • 30
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • Hummer G, Rasaiah JC, Noworyta JP. Water conduction through the hydrophobic channel of a carbon nanotube. Nature 2001;414:188-190.
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 31
    • 7244251461 scopus 로고    scopus 로고
    • Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands
    • Noskov SY, Berneche S, Roux B. Control of ion selectivity in potassium channels by electrostatic and dynamic properties of carbonyl ligands. Nature 2004;431:830-834.
    • (2004) Nature , vol.431 , pp. 830-834
    • Noskov, S.Y.1    Berneche, S.2    Roux, B.3
  • 32
    • 4444255998 scopus 로고    scopus 로고
    • Detailed hydration maps of benzene and cyclohexane reveal distinct water structures
    • Raschke TM, Levitt M. Detailed hydration maps of benzene and cyclohexane reveal distinct water structures. J Phys Chem B 2004;108:13492-13500.
    • (2004) J Phys Chem B , vol.108 , pp. 13492-13500
    • Raschke, T.M.1    Levitt, M.2
  • 33
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Mod 2001;7:306-317.
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 34
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin
    • Jorgensen WL, Tirado-Rives J. The OPLS potential functions for proteins. Energy minimization for crystals of cyclic peptides and crambin. J Am Chem Soc 1988;110:1657-1666.
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 37
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto S, Kollman PA. SETTLE: an analytical version of the SHAKE and RATTLE algorithms for rigid water models. J Comp Chem 1992;13:952-962.
    • (1992) J Comp Chem , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 39
    • 0026684043 scopus 로고
    • A 500ps molecular dynamics simulation study of interleukin-1β in water: Correlation with nuclear magnetic resonance spectroscopy and crystallography
    • Chandrasekhar I, Clore GM, Szabo A, Gronenborn AM, Brooks BR. A 500ps molecular dynamics simulation study of interleukin-1β in water: correlation with nuclear magnetic resonance spectroscopy and crystallography. J Mol Biol 1992;226:239-250.
    • (1992) J Mol Biol , vol.226 , pp. 239-250
    • Chandrasekhar, I.1    Clore, G.M.2    Szabo, A.3    Gronenborn, A.M.4    Brooks, B.R.5
  • 40
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules, Part 1. Theory and range of validity
    • Lipari G, Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules, Part 1. Theory and range of validity. J Am Chem Soc 1980;104:4546-4559.
    • (1980) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 41
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M. Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 1991;11:205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 42
    • 8344280383 scopus 로고    scopus 로고
    • Electric field and temperature effects on water in carbon nanotubes
    • Vaitheeswaran S, Rasaiah JC, Hummer G. Electric field and temperature effects on water in carbon nanotubes. J Chem Phys 2004;121:7955.
    • (2004) J Chem Phys , vol.121 , pp. 7955
    • Vaitheeswaran, S.1    Rasaiah, J.C.2    Hummer, G.3
  • 43
    • 0242364982 scopus 로고    scopus 로고
    • Calculation of free-energy differences from computer simulations of initial and final states
    • Hummer G, Szabo A. Calculation of free-energy differences from computer simulations of initial and final states. J Chem Phys 1996;105:2004-2010.
    • (1996) J Chem Phys , vol.105 , pp. 2004-2010
    • Hummer, G.1    Szabo, A.2
  • 45
    • 0028986918 scopus 로고
    • Internal mobility of the basic pancreatic trypsin inhibitor in solution: A comparison of NMR spin relaxation measurements and molecular dynamics simulations
    • Smith PE, van Schaik RC, Szyperski T, Wuthrich K, van Gunsteren WF. Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations. J Mol Biol 1995;246:356-365.
    • (1995) J Mol Biol , vol.246 , pp. 356-365
    • Smith, P.E.1    van Schaik, R.C.2    Szyperski, T.3    Wuthrich, K.4    van Gunsteren, W.F.5
  • 47
    • 0029757992 scopus 로고    scopus 로고
    • Thermodynamics stability of water molecules in the bacteriorhodopsin proton channel: A molecular dynamics free energy perturbation study
    • Roux B, Nina M, Pomes R, Smith JC. Thermodynamics stability of water molecules in the bacteriorhodopsin proton channel: a molecular dynamics free energy perturbation study. Biophys J 1996;72:670-681.
    • (1996) Biophys J , vol.72 , pp. 670-681
    • Roux, B.1    Nina, M.2    Pomes, R.3    Smith, J.C.4
  • 49
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • Beckstein O, Sansom MS. Liquid-vapor oscillations of water in hydrophobic nanopores. Proc Natl Acad Sci USA 2003;100:7063-7068.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.2
  • 50
    • 0344196965 scopus 로고    scopus 로고
    • The interleukin 1 receptor: Ligand interactions and signal transduction
    • Auron PE. The interleukin 1 receptor: ligand interactions and signal transduction. Cytokine Growth Factor Rev 1998;9(3/4):221-237.
    • (1998) Cytokine Growth Factor Rev , vol.9 , Issue.3-4 , pp. 221-237
    • Auron, P.E.1
  • 51
    • 0036307741 scopus 로고    scopus 로고
    • The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus
    • Tama F, Brooks CL. The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus. J Mol Biol 2002;318:733-747.
    • (2002) J Mol Biol , vol.318 , pp. 733-747
    • Tama, F.1    Brooks, C.L.2
  • 52
    • 0034711314 scopus 로고    scopus 로고
    • X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1
    • Vigers GP, Dripps DJ, Edwards CK, III, Brandhuber BJ. X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1. J Biol Chem 2000;275:36927-36933.
    • (2000) J Biol Chem , vol.275 , pp. 36927-36933
    • Vigers, G.P.1    Dripps, D.J.2    Edwards III, C.K.3    Brandhuber, B.J.4
  • 53
    • 7444230904 scopus 로고    scopus 로고
    • Unveiling functional protein motions with picosecond X-ray crystallography and molecular dynamics simulations
    • Hummer G, Schotte F, Anfinrud PA. Unveiling functional protein motions with picosecond X-ray crystallography and molecular dynamics simulations. Proc Natl Acad Sci USA 2004;101:15330-15334.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15330-15334
    • Hummer, G.1    Schotte, F.2    Anfinrud, P.A.3
  • 54
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1 β
    • Gosavi S, Chavez LL, Jennings PA, Onuchic JN. Topological frustration and the folding of interleukin-1 β. J Mol Biol 2006;357:986-996.
    • (2006) J Mol Biol , vol.357 , pp. 986-996
    • Gosavi, S.1    Chavez, L.L.2    Jennings, P.A.3    Onuchic, J.N.4
  • 55
    • 0029905014 scopus 로고    scopus 로고
    • The change in hydrogen bond strength accompanying charge rearrangement: Implications for enzymatic catalysis
    • Shan S, Herschlag D. The change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis. Proc Natl Acad Sci USA 1996;93:14474-14479.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14474-14479
    • Shan, S.1    Herschlag, D.2
  • 56
    • 0035895356 scopus 로고    scopus 로고
    • Polar group burial contributes more to protein stability than nonpolar group burial
    • Pace CN. Polar group burial contributes more to protein stability than nonpolar group burial. Biochemistry 2001;40:310-313.
    • (2001) Biochemistry , vol.40 , pp. 310-313
    • Pace, C.N.1
  • 57
    • 7444257387 scopus 로고    scopus 로고
    • Efficient evaluation of binding free energy using continuum electrostatics solvation
    • Huang D, Caflisch A. Efficient evaluation of binding free energy using continuum electrostatics solvation. J Med Chem 2004;47:5791-5797.
    • (2004) J Med Chem , vol.47 , pp. 5791-5797
    • Huang, D.1    Caflisch, A.2
  • 60
    • 12344321689 scopus 로고    scopus 로고
    • Structural and energetic consequences of mutations in a solvated hydrophobic cavity
    • Adamek DH, Guerrero L, Blaber M, Caspar DLD. Structural and energetic consequences of mutations in a solvated hydrophobic cavity. J Mol Biol 2005;346:307-318.
    • (2005) J Mol Biol , vol.346 , pp. 307-318
    • Adamek, D.H.1    Guerrero, L.2    Blaber, M.3    Caspar, D.L.D.4
  • 61
    • 0042845836 scopus 로고    scopus 로고
    • The role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin
    • Friedman R, Nachliel E, Gutman M. The role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin. Biophys J 2003;85:886-896.
    • (2003) Biophys J , vol.85 , pp. 886-896
    • Friedman, R.1    Nachliel, E.2    Gutman, M.3
  • 62
    • 23244457434 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sperm whale myoglobin: Effects of mutations and trapped CO on the structure and dynamics of cavities
    • Bossa C, Amadei A, Daidone I, Anselmi M, Vallone B, Brunori M, Di Nola A. Molecular dynamics simulation of sperm whale myoglobin: effects of mutations and trapped CO on the structure and dynamics of cavities. Biophys J 2005;89:465-474.
    • (2005) Biophys J , vol.89 , pp. 465-474
    • Bossa, C.1    Amadei, A.2    Daidone, I.3    Anselmi, M.4    Vallone, B.5    Brunori, M.6    Di Nola, A.7
  • 63
    • 0028409107 scopus 로고
    • Discovery of new ligand binding pathways in myoglobin by random mutagenesis
    • Huang X, Boxer SG. Discovery of new ligand binding pathways in myoglobin by random mutagenesis. Nat Struct Biol 1994;1:226-229.
    • (1994) Nat Struct Biol , vol.1 , pp. 226-229
    • Huang, X.1    Boxer, S.G.2
  • 64
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • Anishkin A, Sukharev S. Water dynamics and dewetting transitions in the small mechanosensitive channel MscS. Biophys J 2004;86:2883-2895.
    • (2004) Biophys J , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 66
    • 4143085329 scopus 로고    scopus 로고
    • Modulating functional loop movements: The role of highly conserved residues in the correlated loop motions
    • Gunasekaran K, Nussinov R. Modulating functional loop movements: the role of highly conserved residues in the correlated loop motions. Chembiochem 2004;5:224-230.
    • (2004) Chembiochem , vol.5 , pp. 224-230
    • Gunasekaran, K.1    Nussinov, R.2
  • 67
    • 27144438673 scopus 로고    scopus 로고
    • Long-range coupling between separate docking sites in interleukin-1β
    • Heidary DK, Roy M, Daumy GO, Cong Y, Jennings PA. Long-range coupling between separate docking sites in interleukin-1β. J Mol Biol 2005;353:1187-1198.
    • (2005) J Mol Biol , vol.353 , pp. 1187-1198
    • Heidary, D.K.1    Roy, M.2    Daumy, G.O.3    Cong, Y.4    Jennings, P.A.5
  • 70
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA. PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 2004;32:665-667.
    • (2004) Nucleic Acids Res , vol.32 , pp. 665-667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.