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Volumn 81, Issue 2, 2013, Pages 326-340

Influence of pressure on the low-frequency vibrational modes of lysozyme and water: A complementary inelastic neutron scattering and molecular dynamics simulation study

Author keywords

Protein vibrational dynamics; Structure and dynamics of hydration water; Vibrational density of states

Indexed keywords

GLOBULAR PROTEIN; LYSOZYME; WATER;

EID: 84872603365     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24189     Document Type: Article
Times cited : (27)

References (87)
  • 1
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditons
    • Jaenicke R. Protein stability and molecular adaptation to extreme conditons. Eur J Biochem 1991; 202: 715-728.
    • (1991) Eur J Biochem , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 2
    • 20144369761 scopus 로고    scopus 로고
    • Stability of proteins: Temperature, pressure and the role of the solvent
    • Scharnagl C, Reif M, Friedrich J. Stability of proteins: Temperature, pressure and the role of the solvent. Biochim Biophys Acta 2005; 1749: 187-213.
    • (2005) Biochim Biophys Acta , vol.1749 , pp. 187-213
    • Scharnagl, C.1    Reif, M.2    Friedrich, J.3
  • 3
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamics in the pressure-temperature plane
    • Meersman F, Smeller L, Heremans K. Protein stability and dynamics in the pressure-temperature plane. Biochim Biophys Acta 2006; 1764: 346-354.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 4
    • 0037437224 scopus 로고    scopus 로고
    • On the temperature-pressure free-energy landscape of proteins
    • Ravindra R, Winter R. On the temperature-pressure free-energy landscape of proteins. ChemPhysChem 2003; 4: 359-365.
    • (2003) ChemPhysChem , vol.4 , pp. 359-365
    • Ravindra, R.1    Winter, R.2
  • 5
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva JL, Weber G. Pressure stability of proteins. Annu Rev Phys Chem 1993; 44: 89-113.
    • (1993) Annu Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2
  • 7
    • 0037171124 scopus 로고    scopus 로고
    • High pressure simulations of biomolecules
    • Paci E. High pressure simulations of biomolecules. Biochim Biophys Acta 2002; 1595: 185-200.
    • (2002) Biochim Biophys Acta , vol.1595 , pp. 185-200
    • Paci, E.1
  • 9
    • 0026785575 scopus 로고
    • Molecular dynamics simulation of solvated protein at high pressure
    • Kitchen DB, Reed LH, Levy RM. Molecular dynamics simulation of solvated protein at high pressure. Biochemistry 1992; 31: 10083-10093.
    • (1992) Biochemistry , vol.31 , pp. 10083-10093
    • Kitchen, D.B.1    Reed, L.H.2    Levy, R.M.3
  • 10
    • 28944435120 scopus 로고    scopus 로고
    • Effect of pressure on the conformation of proteins. A molecular dynamics simulation of lysozyme
    • McCarthy AN, Grigera JR. Effect of pressure on the conformation of proteins. A molecular dynamics simulation of lysozyme. J Mol Graph Model 2006; 24: 254-261.
    • (2006) J Mol Graph Model , vol.24 , pp. 254-261
    • McCarthy, A.N.1    Grigera, J.R.2
  • 11
    • 41849146789 scopus 로고    scopus 로고
    • Relaxation dynamics of lysozyme in solution under pressure: combining molecular dynamics simulations and quasielastic neutron scattering
    • Calandrini V, Hamon V, Hinsen K, Calligari P, Bellissent-Funel M-C, Kneller GR. Relaxation dynamics of lysozyme in solution under pressure: combining molecular dynamics simulations and quasielastic neutron scattering. Chem Phys 2008; 345: 289-297.
    • (2008) Chem Phys , vol.345 , pp. 289-297
    • Calandrini, V.1    Hamon, V.2    Hinsen, K.3    Calligari, P.4    Bellissent-Funel, M.-C.5    Kneller, G.R.6
  • 12
    • 37648998898 scopus 로고    scopus 로고
    • A high pressure cell for small angle neutron scattering up to 500 MPa in combination with light scattering to investigate liquid samples
    • Kohlbrecher J, Bollhalder A, Vavrin R, Meier G. A high pressure cell for small angle neutron scattering up to 500 MPa in combination with light scattering to investigate liquid samples. Rev Sci Instrum 2007; 78: 125101.
    • (2007) Rev Sci Instrum , vol.78 , pp. 125101
    • Kohlbrecher, J.1    Bollhalder, A.2    Vavrin, R.3    Meier, G.4
  • 14
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • Refaee M, Tezuka T, Akasaka K, Williamson MP. Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J Mol Biol 2003; 327: 857-865.
    • (2003) J Mol Biol , vol.327 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 15
    • 0033932840 scopus 로고    scopus 로고
    • Protein compressibility, dynamics, and pressure
    • Kharakoz DP. Protein compressibility, dynamics, and pressure. Biophys J 2000; 79: 511-525.
    • (2000) Biophys J , vol.79 , pp. 511-525
    • Kharakoz, D.P.1
  • 16
    • 33244458851 scopus 로고    scopus 로고
    • Pressure-dependent transition in protein dynamics at about 4kbar revealed by molecular dynamics simulation
    • Meinhold L, Smith JC. Pressure-dependent transition in protein dynamics at about 4kbar revealed by molecular dynamics simulation. Phys Rev E 2005; 72: 061908.
    • (2005) Phys Rev E , vol.72 , pp. 061908
    • Meinhold, L.1    Smith, J.C.2
  • 18
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva JL, Foguel D, Royer CA. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem Sci 2001; 26: 612-618.
    • (2001) Trends Biochem Sci , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 19
    • 79958163072 scopus 로고    scopus 로고
    • Analysis of the mechanism of lysozyme pressure denaturation from Raman spectroscopy investigations, and comparison with thermal denaturation
    • Hédoux A, Guinet Y, Paccou L. Analysis of the mechanism of lysozyme pressure denaturation from Raman spectroscopy investigations, and comparison with thermal denaturation. J Phys Chem B 2011; 115: 6740-6748.
    • (2011) J Phys Chem B , vol.115 , pp. 6740-6748
    • Hédoux, A.1    Guinet, Y.2    Paccou, L.3
  • 20
    • 0031837399 scopus 로고    scopus 로고
    • Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
    • Vidugiris GJA, Royer CA. Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states. Biophys J 1998; 75: 463-470.
    • (1998) Biophys J , vol.75 , pp. 463-470
    • Vidugiris, G.J.A.1    Royer, C.A.2
  • 21
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G, Garde S, Garcia AE, Paulaitis ME, Pratt LR. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc Natl Acad Sci USA 1998; 95: 1552-1555.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 22
    • 77951232650 scopus 로고    scopus 로고
    • Studying pressure denaturation of a protein by molecular dynamics simulations
    • Sarupria S, Ghosh T, García AE, Garde S. Studying pressure denaturation of a protein by molecular dynamics simulations. Proteins 2010; 78: 1641-1651.
    • (2010) Proteins , vol.78 , pp. 1641-1651
    • Sarupria, S.1    Ghosh, T.2    García, A.E.3    Garde, S.4
  • 23
    • 33845422105 scopus 로고    scopus 로고
    • Decomposition of protein experimental compressibility into intrinsic and hydration shell contributions
    • Dadarlat VM, Post CB. Decomposition of protein experimental compressibility into intrinsic and hydration shell contributions. Biophys J 2006; 91: 4544-4554.
    • (2006) Biophys J , vol.91 , pp. 4544-4554
    • Dadarlat, V.M.1    Post, C.B.2
  • 24
    • 56649083699 scopus 로고    scopus 로고
    • Computing the stability diagram of the Trp-cage miniprotein
    • Paschek D, Hempel S, Garcia AE. Computing the stability diagram of the Trp-cage miniprotein. Proc Natl Acad Sci USA 2008; 105: 17754-17759.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17754-17759
    • Paschek, D.1    Hempel, S.2    Garcia, A.E.3
  • 25
    • 0000170769 scopus 로고    scopus 로고
    • Structures of high-density and low-density water
    • K
    • Soper AK, Ricci MA. Structures of high-density and low-density water. Phys Rev Lett 2000; 84: 2881-2884.
    • (2000) Phys Rev Lett , vol.84 , pp. 2881-2884
    • Soper, A.1    Ricci, M.A.2
  • 27
    • 0027732618 scopus 로고
    • Effect of solvent on collective motions in globular protein
    • Hayward S, Kitao A, Hirata F, Go N. Effect of solvent on collective motions in globular protein. J Mol Biol 1993; 234: 1207-1217.
    • (1993) J Mol Biol , vol.234 , pp. 1207-1217
    • Hayward, S.1    Kitao, A.2    Hirata, F.3    Go, N.4
  • 28
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A, Huang P, Caughey WS. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990; 29: 3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 29
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe PK, Long FA. Use of glass electrodes to measure acidities in deuterium oxide. J Phys Chem 1960; 64: 188-190.
    • (1960) J Phys Chem , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 31
    • 0043194670 scopus 로고    scopus 로고
    • Evolution of the internal dynamics of two globular proteins from dry powder to solution
    • Pérez J, Zanotti J-M, Durand D. Evolution of the internal dynamics of two globular proteins from dry powder to solution. Biophys J 1999; 77: 454-469.
    • (1999) Biophys J , vol.77 , pp. 454-469
    • Pérez, J.1    Zanotti, J.-M.2    Durand, D.3
  • 34
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell AD, Feig M, Brooks CL. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 2004; 25: 1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • MacKerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 36
    • 0037067102 scopus 로고    scopus 로고
    • Water rotational relaxation and diffusion in hydrated lysozyme
    • Marchi M, Sterpone F, Ceccarelli M. Water rotational relaxation and diffusion in hydrated lysozyme. J Am Chem Soc 2002; 124: 6787-6791.
    • (2002) J Am Chem Soc , vol.124 , pp. 6787-6791
    • Marchi, M.1    Sterpone, F.2    Ceccarelli, M.3
  • 37
    • 84857817727 scopus 로고    scopus 로고
    • Magnitude and molecular origin of water slowdown next to a protein
    • Sterpone F, Stirnemann G, Laage D. Magnitude and molecular origin of water slowdown next to a protein. J Am Chem Soc 2012; 134: 4116-4119.
    • (2012) J Am Chem Soc , vol.134 , pp. 4116-4119
    • Sterpone, F.1    Stirnemann, G.2    Laage, D.3
  • 38
    • 0035526029 scopus 로고    scopus 로고
    • Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K
    • Mark P, Nilsson L. Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K. J Phys Chem A 2001; 105: 9954-9960.
    • (2001) J Phys Chem A , vol.105 , pp. 9954-9960
    • Mark, P.1    Nilsson, L.2
  • 39
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert J-P, Ciccotti G, Berendsen HJC. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977; 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 40
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P. Knowledge-based protein secondary structure assignment. Proteins 1995; 23: 566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 41
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface: calculated from simulation, using Voronoi Polyhedra
    • Gerstein M, Tsai J, Levitt M. The volume of atoms on the protein surface: calculated from simulation, using Voronoi Polyhedra. J Mol Biol 1995; 249: 955-966.
    • (1995) J Mol Biol , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 42
    • 39749155117 scopus 로고    scopus 로고
    • Water penetration in the low and high pressure native states of ubiquitin
    • Day R, García AE. Water penetration in the low and high pressure native states of ubiquitin. Proteins 2008; 70: 1175-1184.
    • (2008) Proteins , vol.70 , pp. 1175-1184
    • Day, R.1    García, A.E.2
  • 43
    • 36749116946 scopus 로고
    • Molecular motions in compressed liquid water
    • Jonas J, DeFries T, Wilbur DJ. Molecular motions in compressed liquid water. J Chem Phys 1976; 65: 582-588.
    • (1976) J Chem Phys , vol.65 , pp. 582-588
    • Jonas, J.1    DeFries, T.2    Wilbur, D.J.3
  • 45
    • 48549083172 scopus 로고    scopus 로고
    • Conformational entropy of biomolecules: beyond the quasi-harmonic approximation
    • Numata J, Wan M, Knapp E-W. Conformational entropy of biomolecules: beyond the quasi-harmonic approximation. Genome Inform 2007; 18: 192-205.
    • (2007) Genome Inform , vol.18 , pp. 192-205
    • Numata, J.1    Wan, M.2    Knapp, E.-W.3
  • 46
    • 0030057862 scopus 로고    scopus 로고
    • The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation
    • Abseher R, Schreiber H, Steinhauser O. The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation. Proteins 1996; 25: 366-378.
    • (1996) Proteins , vol.25 , pp. 366-378
    • Abseher, R.1    Schreiber, H.2    Steinhauser, O.3
  • 47
    • 0000866097 scopus 로고
    • Hydrogen bonds in water
    • Rapaport DC. Hydrogen bonds in water. Mol Phys 1983; 50: 1151-1162.
    • (1983) Mol Phys , vol.50 , pp. 1151-1162
    • Rapaport, D.C.1
  • 48
    • 0035905815 scopus 로고    scopus 로고
    • Relationship between structural order and the anomalies of liquid water
    • Errington JR, Debenedetti PG. Relationship between structural order and the anomalies of liquid water. Nature 2001; 409: 318-321.
    • (2001) Nature , vol.409 , pp. 318-321
    • Errington, J.R.1    Debenedetti, P.G.2
  • 50
    • 0025333959 scopus 로고
    • Temperature dependence of the low frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering
    • Cusack S, Doster W. Temperature dependence of the low frequency dynamics of myoglobin. Measurement of the vibrational frequency distribution by inelastic neutron scattering. Biophys J 1990; 58: 243-251.
    • (1990) Biophys J , vol.58 , pp. 243-251
    • Cusack, S.1    Doster, W.2
  • 51
    • 4043156208 scopus 로고    scopus 로고
    • Direct determination of vibrational density of states change on ligand binding to a protein
    • Balog E, Becker T, Oettl M, Lechner R, Daniel R, Finney J, Smith J. Direct determination of vibrational density of states change on ligand binding to a protein. Phys Rev Lett 2004; 93: 028103.
    • (2004) Phys Rev Lett , vol.93 , pp. 028103
    • Balog, E.1    Becker, T.2    Oettl, M.3    Lechner, R.4    Daniel, R.5    Finney, J.6    Smith, J.7
  • 52
    • 33749590375 scopus 로고    scopus 로고
    • Picosecond dynamics of T and R forms of aspartate transcarbamylase: A neutron scattering study
    • Zanotti J-M, Hervé G, Bellissent-Funel M-C. Picosecond dynamics of T and R forms of aspartate transcarbamylase: A neutron scattering study. Biochim Biophys Acta 2006; 1764: 1527-1535.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1527-1535
    • Zanotti, J.-M.1    Hervé, G.2    Bellissent-Funel, M.-C.3
  • 53
    • 0041320758 scopus 로고    scopus 로고
    • Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES spectroscopy
    • Giraud G, Karolin J, Wynne K. Low-frequency modes of peptides and globular proteins in solution observed by ultrafast OHD-RIKES spectroscopy. Biophys J 2003; 85: 1903-1913.
    • (2003) Biophys J , vol.85 , pp. 1903-1913
    • Giraud, G.1    Karolin, J.2    Wynne, K.3
  • 54
    • 0001611784 scopus 로고    scopus 로고
    • Analysis of calculated normal modes of a set of native and partially unfolded proteins
    • van Vlijmen HWT, Karplus M. Analysis of calculated normal modes of a set of native and partially unfolded proteins. J Phys Chem B 1999; 103: 3009-3021.
    • (1999) J Phys Chem B , vol.103 , pp. 3009-3021
    • van Vlijmen, H.W.T.1    Karplus, M.2
  • 55
    • 33751534910 scopus 로고    scopus 로고
    • Conformational heterogeneity and low-frequency vibrational modes of proteins
    • Balog E, Smith JC, Perahia D. Conformational heterogeneity and low-frequency vibrational modes of proteins. Phys Chem Chem Phys 2006; 8: 5543-5548.
    • (2006) Phys Chem Chem Phys , vol.8 , pp. 5543-5548
    • Balog, E.1    Smith, J.C.2    Perahia, D.3
  • 56
    • 73649096212 scopus 로고    scopus 로고
    • Low-frequency vibrational properties of lysozyme in sugar aqueous solutions: a Raman scattering and molecular dynamics simulation study
    • Lerbret A, Affouard F, Bordat P, Hédoux A, Guinet Y, Descamps M. Low-frequency vibrational properties of lysozyme in sugar aqueous solutions: a Raman scattering and molecular dynamics simulation study. J Chem Phys 2009; 131: 245103.
    • (2009) J Chem Phys , vol.131 , pp. 245103
    • Lerbret, A.1    Affouard, F.2    Bordat, P.3    Hédoux, A.4    Guinet, Y.5    Descamps, M.6
  • 57
    • 71649083072 scopus 로고    scopus 로고
    • The protein-solvent glass transition
    • Doster W. The protein-solvent glass transition. Biochim Biophys Acta 2010; 1804: 3-14.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 3-14
    • Doster, W.1
  • 58
    • 36849074084 scopus 로고    scopus 로고
    • Picosecond fluctuating protein energy landscape mapped by pressure-temperature molecular dynamics simulation
    • Meinhold L, Smith JC, Kitao A, Zewail AH. Picosecond fluctuating protein energy landscape mapped by pressure-temperature molecular dynamics simulation. Proc Natl Acad Sci USA 2007; 104: 17261-17265.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17261-17265
    • Meinhold, L.1    Smith, J.C.2    Kitao, A.3    Zewail, A.H.4
  • 59
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • Akasaka K, Tezuka T, Yamada H. Pressure-induced changes in the folded structure of lysozyme. J Mol Biol 1997; 271: 671-678.
    • (1997) J Mol Biol , vol.271 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 60
    • 78249233614 scopus 로고    scopus 로고
    • Normal mode analysis and applications in biological physics
    • Dykeman EC, Sankey OF. Normal mode analysis and applications in biological physics. J Phys Condens Matter 2010; 22: 423202.
    • (2010) J Phys Condens Matter , vol.22 , pp. 423202
    • Dykeman, E.C.1    Sankey, O.F.2
  • 61
    • 78649784550 scopus 로고    scopus 로고
    • Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit
    • Skjaerven L, Martinez A, Reuter N. Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit. Proteins 2011; 79: 232-243.
    • (2011) Proteins , vol.79 , pp. 232-243
    • Skjaerven, L.1    Martinez, A.2    Reuter, N.3
  • 62
    • 0000129552 scopus 로고
    • Single-particle dynamics of water molecules in confined space
    • Bellissent-Funel M-C, Chen SH, Zanotti J-M. Single-particle dynamics of water molecules in confined space. Phys Rev E 1995; 51: 4558-4569.
    • (1995) Phys Rev E , vol.51 , pp. 4558-4569
    • Bellissent-Funel, M.-C.1    Chen, S.H.2    Zanotti, J.-M.3
  • 63
    • 2742571585 scopus 로고    scopus 로고
    • Slow dynamics of water molecules on the surface of a globular protein
    • Bellissent-Funel M-C, Zanotti J-M, Chen SH. Slow dynamics of water molecules on the surface of a globular protein. Faraday Discuss 1996; 103: 281-294.
    • (1996) Faraday Discuss , vol.103 , pp. 281-294
    • Bellissent-Funel, M.-C.1    Zanotti, J.-M.2    Chen, S.H.3
  • 64
    • 36849125881 scopus 로고
    • Raman spectral studies of water structure
    • Walrafen GE. Raman spectral studies of water structure. J Chem Phys 1964; 40: 3249-3256.
    • (1964) J Chem Phys , vol.40 , pp. 3249-3256
    • Walrafen, G.E.1
  • 66
    • 79953026819 scopus 로고    scopus 로고
    • Short-range structural transformations in water at high pressures
    • Khusnutdinoff RM, Mokshin AV. Short-range structural transformations in water at high pressures. J Non-Cryst Solids 2011; 357: 1677-1684.
    • (2011) J Non-Cryst Solids , vol.357 , pp. 1677-1684
    • Khusnutdinoff, R.M.1    Mokshin, A.V.2
  • 67
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • Merzel F, Smith JC. Is the first hydration shell of lysozyme of higher density than bulk water? Proc Natl Acad Sci USA 2002; 99: 5378-5383.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 68
    • 34547485422 scopus 로고    scopus 로고
    • How protein surfaces induce anomalous dynamics of hydration water
    • Pizzitutti F, Marchi M, Sterpone F, Rossky PJ. How protein surfaces induce anomalous dynamics of hydration water. J Phys Chem B 2007; 111: 7584-7590.
    • (2007) J Phys Chem B , vol.111 , pp. 7584-7590
    • Pizzitutti, F.1    Marchi, M.2    Sterpone, F.3    Rossky, P.J.4
  • 70
    • 73949137828 scopus 로고    scopus 로고
    • Tetrahedral ordering in water: Raman profiles and their temperature dependence
    • Paolantoni M, Faginas Lago N, Albertí M, Laganà A. Tetrahedral ordering in water: Raman profiles and their temperature dependence. J Phys Chem A 2009; 113: 15100-15105.
    • (2009) J Phys Chem A , vol.113 , pp. 15100-15105
    • Paolantoni, M.1    Faginas Lago, N.2    Albertí, M.3    Laganà, A.4
  • 71
    • 0001156416 scopus 로고    scopus 로고
    • The effects of pressure on structural and dynamical properties of associated liquids: molecular dynamics calculations for the extended simple point charge model of water
    • Bagchi K, Balasubramanian S, Klein ML. The effects of pressure on structural and dynamical properties of associated liquids: molecular dynamics calculations for the extended simple point charge model of water. J Chem Phys 1997; 107: 8561-8567.
    • (1997) J Chem Phys , vol.107 , pp. 8561-8567
    • Bagchi, K.1    Balasubramanian, S.2    Klein, M.L.3
  • 73
    • 0037899660 scopus 로고    scopus 로고
    • Polarizable atomic multipole water model for molecular mechanics simulation
    • Ren P, Ponder JW. Polarizable atomic multipole water model for molecular mechanics simulation. J Phys Chem B 2003; 107: 5933-5947.
    • (2003) J Phys Chem B , vol.107 , pp. 5933-5947
    • Ren, P.1    Ponder, J.W.2
  • 74
    • 33144482975 scopus 로고    scopus 로고
    • Relation between rotational and translational dynamic heterogeneities in water
    • Mazza MG, Giovambattista N, Starr FW, Stanley HE. Relation between rotational and translational dynamic heterogeneities in water. Phys Rev Lett 2006; 96: 057803.
    • (2006) Phys Rev Lett , vol.96 , pp. 057803
    • Mazza, M.G.1    Giovambattista, N.2    Starr, F.W.3    Stanley, H.E.4
  • 76
    • 0345498055 scopus 로고    scopus 로고
    • Anomalous diffusion of adsorbed water: a neutron scattering study of hydrated myoglobin
    • Settles M, Doster W. Anomalous diffusion of adsorbed water: a neutron scattering study of hydrated myoglobin. Faraday Discuss 1996; 103: 269-279.
    • (1996) Faraday Discuss , vol.103 , pp. 269-279
    • Settles, M.1    Doster, W.2
  • 77
    • 36549103625 scopus 로고
    • Temperature dependence of the low- and high-frequency Raman scattering from liquid water
    • Walrafen GE, Fisher MR, Hokmabadi MS, Yang W-H. Temperature dependence of the low- and high-frequency Raman scattering from liquid water. J Chem Phys 1986; 85: 6970-6982.
    • (1986) J Chem Phys , vol.85 , pp. 6970-6982
    • Walrafen, G.E.1    Fisher, M.R.2    Hokmabadi, M.S.3    Yang, W.-H.4
  • 78
    • 0037257527 scopus 로고    scopus 로고
    • An interpretation of the low-frequency spectrum of liquid water
    • Padró JA, Martí J. An interpretation of the low-frequency spectrum of liquid water. J Chem Phys 2003; 118: 452-453.
    • (2003) J Chem Phys , vol.118 , pp. 452-453
    • Padró, J.A.1    Martí, J.2
  • 79
    • 77956209545 scopus 로고    scopus 로고
    • Combining THz spectroscopy and MD simulations to study protein-hydration coupling
    • Heyden M, Havenith M. Combining THz spectroscopy and MD simulations to study protein-hydration coupling. Methods 2010; 52: 74-83.
    • (2010) Methods , vol.52 , pp. 74-83
    • Heyden, M.1    Havenith, M.2
  • 80
    • 37249045537 scopus 로고    scopus 로고
    • Low-frequency vibrational spectrum of water in the hydration layer of a protein: a molecular dynamics simulation study
    • Chakraborty S, Sinha SK, Bandyopadhyay S. Low-frequency vibrational spectrum of water in the hydration layer of a protein: a molecular dynamics simulation study. J Phys Chem B 2007; 111: 13626-13631.
    • (2007) J Phys Chem B , vol.111 , pp. 13626-13631
    • Chakraborty, S.1    Sinha, S.K.2    Bandyopadhyay, S.3
  • 81
    • 57049116557 scopus 로고    scopus 로고
    • On the molecular mechanism of water reorientation
    • Laage D, Hynes JT. On the molecular mechanism of water reorientation. J Phys Chem B 2008; 112: 14230-14242.
    • (2008) J Phys Chem B , vol.112 , pp. 14230-14242
    • Laage, D.1    Hynes, J.T.2
  • 82
    • 38949207174 scopus 로고    scopus 로고
    • Effect of temperature, pressure, and cosolvents on structural and dynamic properties of the hydration shell of SNase: a molecular dynamics computer simulation study
    • Smolin N, Winter R. Effect of temperature, pressure, and cosolvents on structural and dynamic properties of the hydration shell of SNase: a molecular dynamics computer simulation study. J Phy Chem B 2008; 112: 997-1006.
    • (2008) J Phy Chem B , vol.112 , pp. 997-1006
    • Smolin, N.1    Winter, R.2
  • 85
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25°C
    • Gekko K, Noguchi H. Compressibility of globular proteins in water at 25°C. J Phys Chem 1979; 83: 2706-2714.
    • (1979) J Phys Chem , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 87
    • 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 Struct Biol 1997; 4: 396-404.
    • (1997) Nature Struct Biol , vol.4 , pp. 396-404
    • Otting, G.1    Liepinsh, E.2    Halle, B.3    Frey, U.4


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