메뉴 건너뛰기




Volumn 156, Issue 1, 2011, Pages 31-42

Structural characteristics of hydration sites in lysozyme

Author keywords

Clustered hydration site; Crystal water; H bond recombination; Hydration matrix; Hydration site; Hydration water

Indexed keywords

LYSOZYME; WATER;

EID: 79955968072     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.02.006     Document Type: Article
Times cited : (12)

References (66)
  • 4
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • D. Chandler, Interfaces and the driving force of hydrophobic assembly, Nature 437 (2005) 640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 5
    • 2942655388 scopus 로고    scopus 로고
    • Heat capacity effects associated with the hydrophobic hydration and interaction of simple solutes: A detailed structural and energetical analysis based on molecular dynamics simulations
    • D. Paschek, Heat capacity effects associated with the hydrophobic hydration and interaction of simple solutes: a detailed structural and energetical analysis based on molecular dynamics simulations, J. Chem. Phys. 120 (2004) 10605-10617.
    • (2004) J. Chem. Phys. , vol.120 , pp. 10605-10617
    • Paschek, D.1
  • 7
    • 0030736114 scopus 로고    scopus 로고
    • Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution
    • N. Ben-Tal, D. Sitkoff, I.A. Topol, A.S. Yang, S.K. Burt, B. Honig, Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution, J. Phys. Chem. B 101 (1997) 450-457. (Pubitemid 127617329)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.3 , pp. 450-457
    • Ben-Tal, N.1    Sitkoff, D.2    Topol, I.A.3    Yang, A.-S.4    Burt, S.K.5    Honig, B.6
  • 8
    • 0037019460 scopus 로고    scopus 로고
    • Molecular dynamics of water at protein-solvent interface
    • A.R. Bizzarri, S. Cannistraro, Molecular dynamics of water at protein-solvent interface, J. Phys. Chem. B 106 (2002) 6617-6633.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6617-6633
    • Bizzarri, A.R.1    Cannistraro, S.2
  • 9
    • 0016721016 scopus 로고
    • Solvation of crystalline proteins: Theory and its application to available data
    • W.J. Scanlon, D. Eisenberg, Solvation of crystalline proteins: theory and its application to available data, J. Mol. Biol. 98 (1975) 485-502.
    • (1975) J. Mol. Biol. , vol.98 , pp. 485-502
    • Scanlon, W.J.1    Eisenberg, D.2
  • 10
    • 0001238181 scopus 로고
    • Solvation of crystalline proteins: Solvent bound in sperm whale metmyoglobin type A crystals at 6.1 and 23.5°C
    • W.J. Scanlon, D. Eisenberg, Solvation of crystalline proteins: solvent bound in sperm whale metmyoglobin type A crystals at 6.1 and 23.5°C, J. Phys. Chem. 85 (1981) 3251-3256.
    • (1981) J. Phys. Chem. , vol.85 , pp. 3251-3256
    • Scanlon, W.J.1    Eisenberg, D.2
  • 12
    • 0037110473 scopus 로고    scopus 로고
    • Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic x-ray crystal structure analyses: On the correlation between crystal water sites, solvent density, and solvent dipole
    • DOI 10.1002/jcc.10100
    • J. Higo, M. Nakasako, Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipole, J. Comput. Chem. 23 (2002) 1323-1336. (Pubitemid 35186234)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.14 , pp. 1323-1336
    • Higo, J.1    Nakasako, M.2
  • 13
    • 11144314962 scopus 로고    scopus 로고
    • Hydrogen-bond patterns in the hydration structure of a protein
    • DOI 10.1016/j.cplett.2004.11.071, PII S0009261404018159
    • T. Yokomizo, M. Nakasako, T. Yamazaki, H. Shindo, J. Higo, Hydrogen-bond patterns in the hydration structure of a protein, Chem. Phys. Lett. 401 (2005) 332-336. (Pubitemid 40038266)
    • (2005) Chemical Physics Letters , vol.401 , Issue.4-6 , pp. 332-336
    • Yokomizo, T.1    Nakasako, M.2    Yamazaki, T.3    Shindo, H.4    Higo, J.5
  • 14
    • 0029046396 scopus 로고
    • Molecular dynamics simulation of hydration in myoglobin
    • W. Gu, B.P. Schoenborn, Molecular dynamics simulation of hydration in myoglobin, Proteins 22 (1995) 20-26.
    • (1995) Proteins , vol.22 , pp. 20-26
    • Gu, W.1    Schoenborn, B.P.2
  • 15
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • F. Merzel, J.C. Smith, Is the first hydration shell of lysozyme of higher density than bulk water? Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 5378-5383.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 16
    • 0028144626 scopus 로고
    • A connected-cluster of hydration around myoglobin: Correlation between molecular dynamics simulations and experiment
    • V. Lounnas, B.M. Pettitt, A connected-cluster of hydration around myoglobin: correlation between molecular dynamics simulations and experiment, Proteins 18 (1994) 133-147. (Pubitemid 24055076)
    • (1994) Proteins: Structure, Function and Genetics , vol.18 , Issue.2 , pp. 133-147
    • Lounnas, V.1    Pettitt, B.M.2
  • 17
    • 0028955215 scopus 로고
    • Hydration of nucleic acid fragments: Comparison of theory and experiment for high-resolution crystal structures of RNA, DNA, and DNA-drug complexes
    • G. Hummer, A.E. García, D.M. Soumpasis, Hydration of nucleic acid fragments: comparison of theory and experiment for high-resolution crystal structures of RNA, DNA, and DNA-drug complexes, Biophys. J. 68 (1995) 1639-1652.
    • (1995) Biophys. J. , vol.68 , pp. 1639-1652
    • Hummer, G.1    García, A.E.2    Soumpasis, D.M.3
  • 18
    • 0033636839 scopus 로고    scopus 로고
    • Residence times of water molecules in the hydration sites of myoglobin
    • V.A. Makarov, B.K. Andrews, P.E. Smith, B.M. Pettitt, Residence times of water molecules in the hydration sites of myoglobin, Biophys. J. 79 (2000) 2966-2974.
    • (2000) Biophys. J. , vol.79 , pp. 2966-2974
    • Makarov, V.A.1    Andrews, B.K.2    Smith, P.E.3    Pettitt, B.M.4
  • 19
    • 51649131252 scopus 로고    scopus 로고
    • Distinguishing thermodynamic and kinetic views of the preferential hydration of protein surface
    • M.H. Priya, J.K. Shah, D. Asthagiri, M. Paulaitis, Distinguishing thermodynamic and kinetic views of the preferential hydration of protein surface, Biophys. J. 95 (2008) 2219-2225.
    • (2008) Biophys. J. , vol.95 , pp. 2219-2225
    • Priya, M.H.1    Shah, J.K.2    Asthagiri, D.3    Paulaitis, M.4
  • 20
    • 0037098857 scopus 로고    scopus 로고
    • Extracting hydration sites around proteins from explicit water simulations
    • R.H. Henchman, J.A. McCammon, Extracting hydration sites around proteins from explicit water simulations, J. Comput. Chem. 23 (2002) 861-869.
    • (2002) J. Comput. Chem. , vol.23 , pp. 861-869
    • Henchman, R.H.1    McCammon, J.A.2
  • 21
    • 0034845734 scopus 로고    scopus 로고
    • Deducing hydration sites of a protein from molecular dynamics simulations
    • M.S. Madhusudhan, S. Vishveshwara, Deducing hydration sites of a protein from molecular dynamics simulations, J. Biomol. Struct. Dyn. 19 (2001) 1-10.
    • (2001) J. Biomol. Struct. Dyn. , vol.19 , pp. 1-10
    • Madhusudhan, M.S.1    Vishveshwara, S.2
  • 22
    • 2542633488 scopus 로고    scopus 로고
    • Protein-water interactions in ribonuclease A and angiogenin: A molecular dynamics study
    • DOI 10.1002/prot.20114
    • B.S. Sanjeev, S. Vishveshwara, Protein-water interactions in ribonuclease A and angiogenin: a molecular dynamics study, Proteins 55 (2004) 915-923. (Pubitemid 38702950)
    • (2004) Proteins: Structure, Function and Genetics , vol.55 , Issue.4 , pp. 915-923
    • Sanjeev, B.S.1    Vishveshwara, S.2
  • 23
    • 0027957222 scopus 로고
    • Distribution function implied dynamics versus residence times and correlations: Solvation shells of myoglobin
    • V. Lounnas, B.M. Pettitt, Distribution function implied dynamics versus residence times and correlations: solvation shells of myoglobin, Proteins 18 (1994) 148-160. (Pubitemid 24055077)
    • (1994) Proteins: Structure, Function and Genetics , vol.18 , Issue.2 , pp. 148-160
    • Lounnas, V.1    Pettitt, B.M.2
  • 24
    • 0035839052 scopus 로고    scopus 로고
    • Dynamics of hydration in hen egg white lysozyme
    • F. Sterpone, M. Ceccarelli, M. Marchi, Dynamics of hydration in hen egg white lysozyme, J. Mol. Biol. 311 (2001) 409-419.
    • (2001) J. Mol. Biol. , vol.311 , pp. 409-419
    • Sterpone, F.1    Ceccarelli, M.2    Marchi, M.3
  • 25
    • 6444228146 scopus 로고    scopus 로고
    • Molecular dynamics simulations of staphylococcal nuclease: Properties of waters at the protein surface
    • N. Somolin, R. Winter, Molecular dynamics simulations of staphylococcal nuclease: properties of waters at the protein surface, J. Phys. Chem. B 108 (2004) 15928-15937.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 15928-15937
    • Somolin, N.1    Winter, R.2
  • 26
    • 0035744176 scopus 로고    scopus 로고
    • A faster way to characterize by triple-quantum- filtered 17O NMR water molecules strongly bound to macromolecules in solution
    • A. Lehoux, M. Krzystyniak, E. Baguet, A faster way to characterize by triple-quantum- filtered 17O NMR water molecules strongly bound to macromolecules in solution, J. Magn. Reson. 148 (2001) 11-22.
    • (2001) J. Magn. Reson. , vol.148 , pp. 11-22
    • Lehoux, A.1    Krzystyniak, M.2    Baguet, E.3
  • 27
    • 38949183943 scopus 로고    scopus 로고
    • Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules
    • DOI 10.1021/ja0775873
    • E. Persson, B. Halle, Nanosecond to microsecond protein dynamics probed by magnetic relaxation dispersion of buried water molecules, J. Am. Chem. Soc. 130 (2008) 1774-1787. (Pubitemid 351214099)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.5 , pp. 1774-1787
    • Persson, E.1    Halle, B.2
  • 28
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • G. Otting, E. Liepinsh, K. Wüthrich, Protein hydration in aqueous solution, Science 254 (1991) 974-980. (Pubitemid 21917420)
    • (1991) Science , vol.254 , Issue.5034 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wuthrich, K.3
  • 29
    • 2542589513 scopus 로고    scopus 로고
    • NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A-a marginally stable state in folded protein
    • A. Yokota, K. Hirai, H. Miyauchi, S. Iimura, Y. Noda, K. Inoue, K. Akasaka, H. Tachibana, S. Segawa, NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A-a marginally stable state in folded protein, Biochemistry 43 (2004) 6663-6669.
    • (2004) Biochemistry , vol.43 , pp. 6663-6669
    • Yokota, A.1    Hirai, K.2    Miyauchi, H.3    Iimura, S.4    Noda, Y.5    Inoue, K.6    Akasaka, K.7    Tachibana, H.8    Segawa, S.9
  • 32
    • 38949201628 scopus 로고    scopus 로고
    • On the molecular origins of volumetric data
    • T. Chalikian, On the molecular origins of volumetric data, J. Phys. Chem. B 112 (2008) 911-917.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 911-917
    • Chalikian, T.1
  • 35
    • 0030694240 scopus 로고    scopus 로고
    • Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography
    • DOI 10.1038/nsb1197-909
    • N. Niimura, Y. Minezaki, T. Nonaka, J.-C. Castagna, F. Cipriani, P. Høghøj, M.S. Lehmann, C. Wilkinson, Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography, Nature Struct. Mol. Biol. 4 (1997) 909-914. (Pubitemid 27479441)
    • (1997) Nature Structural Biology , vol.4 , Issue.11 , pp. 909-914
    • Niimura, N.1    Minezaki, Y.2    Nonaka, T.3    Castagna, J.-C.4    Cipriani, F.5    Hoghoj, P.6    Lehmann, M.S.7    Wilkinson, C.8
  • 36
    • 33847308554 scopus 로고    scopus 로고
    • Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography
    • M.D. Collins, M.L. Quillin, G. Hummer, B.W. Matthews, S.M. Gruner, Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography, J. Mol. Biol. 367 (2007) 752-763.
    • (2007) J. Mol. Biol. , vol.367 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 37
    • 35349013541 scopus 로고    scopus 로고
    • Role of flexibility and polarity as determinants of the hydration of internal cavities and pockets in proteins
    • DOI 10.1529/biophysj.107.104182
    • A. Damjanovic, J.L. Schlessman, C.A. Fitch, A.E. Garcia, B. Garcia-Moreno, Role of flexibility and polarity as determinants of the hydration of internal cavities and pockets in proteins, Biophys. J. 93 (2007) 2791-2804. (Pubitemid 47607815)
    • (2007) Biophysical Journal , vol.93 , Issue.8 , pp. 2791-2804
    • Damjanovic, A.1    Schlessman, J.L.2    Fitch, C.A.3    Garcia, A.E.4    Garcia-Moreno, E.B.5
  • 38
    • 0030892956 scopus 로고    scopus 로고
    • NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules
    • G. Otting, E. Liepinsh, B. Halle, U. Frey, NMR identification of hydrophobic cavities with low water occupancies in protein structures using small gas molecules, Nature Struct. Biol. 4 (1997) 396-404.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 396-404
    • Otting, G.1    Liepinsh, E.2    Halle, B.3    Frey, U.4
  • 39
    • 33847010225 scopus 로고    scopus 로고
    • Locating missing water molecules in protein cavities by the three-dimensional reference interaction site model theory of molecular solvation
    • T. Imai, R. Hiraoka, A. Kovalenko, F. Hirata, Locating missing water molecules in protein cavities by the three-dimensional reference interaction site model theory of molecular solvation, Proteins 66 (2007) 804-813.
    • (2007) Proteins , vol.66 , pp. 804-813
    • Imai, T.1    Hiraoka, R.2    Kovalenko, A.3    Hirata, F.4
  • 40
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • DOI 10.1016/j.jmb.2005.01.052
    • R. Kitahara, S. Yokoyama, K. Akasaka, NMR snapshots of a fluctuating protein structure. Ubiquitin at 30 bar-3 kbar, J. Mol. Biol. 347 (2005) 277-285. (Pubitemid 40312458)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 41
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • M. Karplus, J.A. McCammon, Molecular dynamics simulations of biomolecules, Nature Struct. Biol. 9 (2002) 646-652.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 44
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, C. Kutzner, D. van der Spoel, E. Lindahl, GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation, J. Chem. Theory Comput. 4 (2008) 435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 45
    • 84943502952 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • S. Nose, A unified formulation of the constant temperature molecular dynamics methods, Mol. Phys. 52 (1984) 255-268.
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 46
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distribution
    • W.G. Hoover, Canonical dynamics: equilibrium phase-space distribution, Phys. Rev. A 31 (1985) 1695-1697.
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 47
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • H.C. Andersen, Molecular dynamics simulations at constant pressure and/or temperature, J. Chem. Phys. 72 (1980) 2384-2393.
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 48
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • S. Nose, M.L. Klein, Constant pressure molecular dynamics for molecular systems, Mol. Phys. 50 (1983) 1055-1076.
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 50
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • DOI 10.1529/biophysj.104.051938
    • E.J. Sorin, V.S. Pande, Exploring the helix-coil transition via all-atom equilibrium ensemble simulations, Biophysical J. 88 (2005) 2472-2493. (Pubitemid 40976118)
    • (2005) Biophysical Journal , vol.88 , Issue.4 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 51
    • 2942622288 scopus 로고    scopus 로고
    • Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew
    • H.W. Horn, W.C. Swope, J.W. Pitera, J.D. Madura, T.J. Dick, Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew, J. Chem. Phys. 120 (2004) 9665-9678.
    • (2004) J. Chem. Phys. , vol.120 , pp. 9665-9678
    • Horn, H.W.1    Swope, W.C.2    Pitera, J.W.3    Madura, J.D.4    Dick, T.J.5
  • 52
    • 49449085241 scopus 로고    scopus 로고
    • Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations
    • I.S. Joung, T.E. Cheatham, Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations, J. Phys. Chem. B 112 (2008) 9020-9041.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9020-9041
    • Joung, I.S.1    Cheatham, T.E.2
  • 53
    • 33745299454 scopus 로고    scopus 로고
    • Is the Ewald summation still necessary? Pairwise alternatives to the accepted standard for long-range electrostatics
    • C.J. Fennell, J.D. Gezelter, Is the Ewald summation still necessary? Pairwise alternatives to the accepted standard for long-range electrostatics, J. Chem. Phys. 124 (2006) 234104.
    • (2006) J. Chem. Phys. , vol.124 , pp. 234104
    • Fennell, C.J.1    Gezelter, J.D.2
  • 54
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • I.K. McDonald, J.M. Thornton, Satisfying hydrogen bonding potential in proteins, J. Mol. Biol. 238 (1994) 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 55
    • 0033516705 scopus 로고    scopus 로고
    • Packing density in proteins: Standard radii and volumes
    • J. Tsai, R. Taylor, C. Chothia, M. Gerstein, Packing density in proteins: standard radii and volumes, J. Mol. Biol. 290 (1999) 253-266.
    • (1999) J. Mol. Biol. , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 56
    • 0034662899 scopus 로고    scopus 로고
    • The radial distribution functions of water and ice from 220 K to 673 K and at pressures up to 400 MPa
    • A.K. Soper, The radial distribution functions of water and ice from 220 K to 673 K and at pressures up to 400 MPa, Chem. Phys. 258 (2000) 121-137.
    • (2000) Chem. Phys. , vol.258 , pp. 121-137
    • Soper, A.K.1
  • 57
    • 0026757625 scopus 로고
    • Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme
    • K.P. Wilson, B.A. Malcolm, B.W. Matthews, Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme, J. Biol. Chem. 267 (1992) 10842-10849.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10842-10849
    • Wilson, K.P.1    Malcolm, B.A.2    Matthews, B.W.3
  • 58
    • 0028785353 scopus 로고
    • Thermal stability determinants of chicken egg-white lysozyme core mutants: Hydrophobicity, packing volume, and conserved buried water molecules
    • P. Shih, D.R. Holland, J.F. Kirsch, Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules, Protein Sci. 4 (1995) 2050-2062.
    • (1995) Protein Sci. , vol.4 , pp. 2050-2062
    • Shih, P.1    Holland, D.R.2    Kirsch, J.F.3
  • 59
    • 0037246110 scopus 로고    scopus 로고
    • Buried water molecules contribute to the conformational stability of a protein
    • K. Takano, Y. Yamagata, K. Yutani, Buried water molecules contribute to the conformational stability of a protein, Protein Eng. 16 (2003) 5-9. (Pubitemid 36407059)
    • (2003) Protein Engineering , vol.16 , Issue.1 , pp. 5-9
    • Takano, K.1    Yamagata, Y.2    Yutani, K.3
  • 60
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • M. Refaee, T. Tezuka, K. Akasaka, M.P. Williamson, Pressure-dependent changes in the solution structure of hen egg-white lysozyme, J. Mol. Biol. 327 (2003) 857-865.
    • (2003) J. Mol. Biol. , vol.327 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 62
    • 0025281494 scopus 로고
    • Molecular interactions in protein crystals: Solvent accessible surface and stability
    • DOI 10.1002/prot.340080103
    • S.A. Islam, D.L.Weaver,Molecular interactions in protein crystals: solvent accessible surface and stability, Proteins 8 (1990) 1-5. (Pubitemid 20235326)
    • (1990) Proteins: Structure, Function and Genetics , vol.8 , Issue.1 , pp. 1-5
    • Islam, S.A.1    Weaver, D.L.2
  • 63
    • 0000276909 scopus 로고
    • Water structure associated with proteins and its role in crystallization
    • M. Frey,Water structure associated with proteins and its role in crystallization, Acta Crystallogr. D 50 (1994) 663-666.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 663-666
    • Frey, M.1
  • 64
    • 0028921637 scopus 로고
    • Structure and dynamics of the water around myoglobin
    • G.N. Phillips, B.M. Pettitt, Structure and dynamics of the water around myoglobin, Protein Sci. 4 (1995) 149-158.
    • (1995) Protein Sci. , vol.4 , pp. 149-158
    • Phillips, G.N.1    Pettitt, B.M.2
  • 65
    • 0028218493 scopus 로고
    • A globalmodel of the protein-solvent interface
    • V. Lounnas, B.M. Pettitt, G.N. Phillips, A globalmodel of the protein-solvent interface, Biophys. J. 66 (1994) 601-614.
    • (1994) Biophys. J. , vol.66 , pp. 601-614
    • Lounnas, V.1    Pettitt, B.M.2    Phillips, G.N.3
  • 66
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction
    • J.S. Jiang, A.T. Brunger, Protein hydration observed by X-ray diffraction, J. Mol. Biol. 243 (1994) 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.