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Volumn 43, Issue 2, 2010, Pages 231-239

Water in the half shell: Structure of water, focusing on angular structure and solvation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; WATER;

EID: 77249111728     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar900154j     Document Type: Article
Times cited : (74)

References (60)
  • 1
    • 36149072937 scopus 로고
    • The crystal structure of ice
    • Bragg, W. H. The crystal structure of ice. Proc. Phys. Soc. London 1921, 34, 98-103.
    • (1921) Proc. Phys. Soc. London , vol.34 , pp. 98-103
    • Bragg, W.H.1
  • 2
    • 0343017595 scopus 로고
    • Liquid water: Molecular correlation functions from x-ray diffraction
    • Narten, A.; Levy, H. Liquid water: Molecular correlation functions from x-ray diffraction. J. Chem. Phys. 1971, 55, 2263-2269.
    • (1971) J. Chem. Phys. , vol.55 , pp. 2263-2269
    • Narten, A.1    Levy, H.2
  • 3
    • 4544303857 scopus 로고
    • Isochoric temperature differential of the x-ray structure factor and structural rearrangements in low-temperature heavy water
    • Bosio, L; Chen, S.; Teixeira, J. Isochoric temperature differential of the x-ray structure factor and structural rearrangements In low-temperature heavy water. Phys. Rev. A 1983, 27, 1468-1475.
    • (1983) Phys. Rev. A , vol.27 , pp. 1468-1475
    • Bosio, L.1    Chen, S.2    Teixeira, J.3
  • 4
    • 77249087496 scopus 로고    scopus 로고
    • The radial distribution functions of water and Ice
    • Sopor, A. K. The radial distribution functions of water and Ice. Chem. Phys. 2002, 258, 121-137.
    • (2002) Chem. Phys. , vol.258 , pp. 121-137
    • Sopor, A.K.1
  • 5
    • 33845790250 scopus 로고
    • Molecular dynamics study of liquid water
    • Rahman, A.; Stillinger, F. Molecular dynamics study of liquid water. J. Chem. Phys. 1971, 55, 3336-3359.
    • (1971) J. Chem. Phys. , vol.55 , pp. 3336-3359
    • Rahman, A.1    Stillinger, F.2
  • 6
    • 0000322192 scopus 로고
    • The effect of apolar solutes on water structure: Alcohols and tetraalkylammonium ions
    • Turner, J.; Soper, A. The effect of apolar solutes on water structure: Alcohols and tetraalkylammonium ions. J. Chem. Phys. 1994, 101, 6116-6125.
    • (1994) J. Chem. Phys. , vol.101 , pp. 6116-6125
    • Turner, J.1    Soper, A.2
  • 7
    • 36449007251 scopus 로고
    • Ionic versus apolar behavior of the teramethylammonium ion in water
    • Turner, J.; Soper, A.; Finney, J. Ionic versus apolar behavior of the teramethylammonium ion in water. J. Chem. Phys. 1995, 102, 5438-5443.
    • (1995) J. Chem. Phys. , vol.102 , pp. 5438-5443
    • Turner, J.1    Soper, A.2    Finney, J.3
  • 8
    • 0000685148 scopus 로고    scopus 로고
    • A new order parameter for tetrahedral configurations
    • Chau, P.: Hardwick, A. A new order parameter for tetrahedral configurations. Mol. Phys. 1998, 93, 511-518.
    • (1998) Mol. Phys. , vol.93 , pp. 511-518
    • Chau, P.1    Hardwick, A.2
  • 9
    • 0035905815 scopus 로고    scopus 로고
    • Relationship between structural order and the anomalies of liquid water
    • DOI 10.1038/35053024
    • Errington, J.; Debenedetti, P. Relationship between structural order and the anomolies of liquid water. Nature 2001, 409, 318-321. (Pubitemid 32151231)
    • (2001) Nature , vol.409 , Issue.6818 , pp. 318-321
    • Errington, J.R.1    Debenedetti, P.G.2
  • 10
    • 0023537267 scopus 로고
    • Shape of the delaunay simplices in dense random packings of hard and soft spheres
    • Medvedev, N.; Naberukhin, Y. Shape of the Delaunay Simplexes In dense random packings of hard and soft spheres. J. Non-Cryst. Solids 1987, 94, 402-406. (Pubitemid 18551305)
    • (1987) Journal of Non-Crystalline Solids , vol.94 , Issue.3 , pp. 402-406
    • Medvedev, N.N.1    Naberukhin, Y.2
  • 11
    • 44949256219 scopus 로고    scopus 로고
    • Formation of ice-like water structure on the surface of an antifreeze protein
    • Smolin, N.; Daggett, V. Formation of ice-like water structure on the surface of an antifreeze protein. J. Phys. Chem. B2008, 112, 6193-6202.
    • J. Phys. Chem. , vol.B2008 , Issue.112 , pp. 6193-6202
    • Smolin, N.1    Daggett, V.2
  • 12
    • 17444392480 scopus 로고
    • Structure in liquid water: A study of spatial distribution functions
    • Svishchev, L.; Kusalik, P. Structure In liquid water: A study of spatial distribution functions. J. Chem. Phys. 1993, 99, 3049-3061.
    • (1993) J. Chem. Phys. , vol.99 , pp. 3049-3061
    • Svishchev, L.1    Kusalik, P.2
  • 13
    • 0034662893 scopus 로고    scopus 로고
    • Solvation structures in three dimensions
    • Svishchev, L. M.; Zassetsky, A.; Kusalik, P. Solvation structures in three dimensions. Chem. Phys. 2000, 258, 181-186.
    • (2000) Chem. Phys. , vol.258 , pp. 181-186
    • Svishchev, L.M.1    Zassetsky, A.2    Kusalik, P.3
  • 14
    • 0000170769 scopus 로고    scopus 로고
    • Structures of high-density and low-density water
    • Soper, A.; Ricci, M. 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.2
  • 15
    • 0033906678 scopus 로고    scopus 로고
    • Probing the structure of water around biological molecules: Concepts, constructs and consequences
    • Soper, A. K. Probing the structure of water around biological molecules: Concepts, constructs and consequences. Physica B 2000, 276, 12-16.
    • (2000) Physica B , vol.276 , pp. 12-16
    • Soper, A.K.1
  • 16
    • 0001332057 scopus 로고
    • Equation of state of a random network, continuum model of liquid water
    • Henn, A. R.; Kauzmann, W. Equation of state of a random network, continuum model of liquid water. J. Phys. Chem. 1989, 93, 3770-3783.
    • (1989) J. Phys. Chem. , vol.93 , pp. 3770-3783
    • Henn, A.R.1    Kauzmann, W.2
  • 18
    • 0001053436 scopus 로고
    • A zeroth order random network model of liquid water
    • Sceats, M. G.; Stavola, M.; Rice, S. A. A zeroth order random network model of liquid water. J. Chem. Phys. 1979, 70, 3927-3938.
    • (1979) J. Chem. Phys. , vol.70 , pp. 3927-3938
    • Sceats, M.G.1    Stavola, M.2    Rice, S.A.3
  • 19
    • 36749113661 scopus 로고
    • A random network model calculation of the free energy of liquid water
    • Sceats, M. G.; Rice, S. A. A random network model calculation of the free energy of liquid water. J. Chem. Phys. 1980, 72, 6183-6191.
    • (1980) J. Chem. Phys. , vol.72 , pp. 6183-6191
    • Sceats, M.G.1    Rice, S.A.2
  • 20
    • 33845556487 scopus 로고
    • A random network model for water
    • Rice, S. A.; Sceats, M. G. A random network model for water. J. Phys. Chem. 1981, 85, 1108-1119.
    • (1981) J. Phys. Chem. , vol.85 , pp. 1108-1119
    • Rice, S.A.1    Sceats, M.G.2
  • 21
    • 0041624164 scopus 로고    scopus 로고
    • A new angle on heat capacity changes in hydrophobic solvation
    • Gallagher, K.; Sharp, K. A. A new angle on heat capacity changes in hydrophobic solvation. J. Am. Chem. Soc. 2003, 125, 9863-9870.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9863-9870
    • Gallagher, K.1    Sharp, K.A.2
  • 23
    • 34249933138 scopus 로고    scopus 로고
    • Hydrogen bonding definitions and dynamics in liquid water
    • Kumar, R.; Schmidt, J.; Skinner, J. Hydrogen bonding definitions and dynamics in liquid water. J. Chem. Phys. 2007, 126, 204107.
    • (2007) J. Chem. Phys. , vol.126 , pp. 204107
    • Kumar, R.1    Schmidt, J.2    Skinner, J.3
  • 24
    • 0041327357 scopus 로고    scopus 로고
    • Understanding all of water's anomalies with a nonlocal potential
    • Cho, H.; Singh, S.; Robinson, G. Understanding all of water's anomalies with a nonlocal potential. J. Chem. Phys. 1997, 107, 7979-7988. (Pubitemid 127564326)
    • (1997) Journal of Chemical Physics , vol.107 , Issue.19 , pp. 7979-7988
    • Cho, C.H.1    Singh, S.2    Robinson, G.3
  • 25
    • 0033045501 scopus 로고    scopus 로고
    • Changes in water structure induced by a hydrophobic solute probed by simulation of the water hydrogen bond angle and radial distribution functions
    • DOI 10.1016/S0301-4622(98)00227-0, PII S0301462298002270
    • Madan, B.; Sharp, K. Changes In water structure induced by a hydrophobic solute proved by simulation of the water hydrogen bond angle and radial distribution functions. Biophys. Chem. 1999, 78, 33-41. (Pubitemid 29206656)
    • (1999) Biophysical Chemistry , vol.78 , Issue.1-2 , pp. 33-41
    • Madan, B.1    Sharp, K.2
  • 26
    • 33748543287 scopus 로고    scopus 로고
    • Heat capacity changes accompanying hydrophobic and ionic solvation: A Monte Carlo and random network model study
    • Madan, B.; Sharp, K. Heat capacity chages accompanying hydrophobic and Ionic solvation: A Monte Carlo and random network model study. J. Phys. Chem. 1996, 100, 7713-7721. (Pubitemid 126789455)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.18 , pp. 7713-7721
    • Madan, B.1    Sharp, K.2
  • 27
    • 0031375098 scopus 로고    scopus 로고
    • Molecular origin of hydration heat capacity changes of hydrophobic solutes: Perturbation of water structure around alkanes
    • Madan, B.; Sharp, K. Molecular origin of hydration heat capacity chages of hydrophbic solutes: Perturbation of water structure around alkanes. J. Phys. Chem. B 1997, 101, 11237-11242. (Pubitemid 127627980)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.51 , pp. 11237-11242
    • Madan, B.1    Sharp, K.2
  • 28
    • 0008023849 scopus 로고    scopus 로고
    • Hydrophobic effect, water structure, and heat capacity changes
    • Sharp, K. A.; Madan, B. Hydrophobic effect, water structure, and heat capacity changes. J. Phys. Chem. B 1997, 101, 4343-4348. (Pubitemid 127609268)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.21 , pp. 4343-4348
    • Sharp, K.A.1    Madan, B.2
  • 29
    • 0032556206 scopus 로고    scopus 로고
    • Effect of the protein denaturants urea and guanidinium on water structure: A structural and thermodynamic study
    • DOI 10.1021/ja981529n
    • Vanzi, F.; Madan, B.; Sharp, K. Effect of the protein denaturants urea and guanidinium on water structure: A structural and thermodynamic study. J. Am. Chem. Soc. 1998, 120, 10748-10753. (Pubitemid 28498822)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.41 , pp. 10748-10753
    • Vanzi, F.1    Madan, B.2    Sharp, K.3
  • 30
    • 0034805049 scopus 로고    scopus 로고
    • Hydration heat capacity of nucleic add constituents determined from the random network model
    • Madan, B.; Sharp, K. A. Hydration heat capacity of nucleic add constituents determined from the random network model. Biophys. J. 2001, 81, 1881-1887.
    • (2001) Biophys. J. , vol.81 , pp. 1881-1887
    • Madan, B.1    Sharp, K.A.2
  • 31
    • 0141449051 scopus 로고    scopus 로고
    • Analysis of thermal hysteresis protein hydration using the random network model
    • Gallagher, K. R.; Sharp, K. A. Analysis of thermal hysteresis protein hydration using the random network model. Biophys. Chem. 2003, 105, 195-209.
    • (2003) Biophys. Chem. , vol.105 , pp. 195-209
    • Gallagher, K.R.1    Sharp, K.A.2
  • 32
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to protein folding
    • Spolar, R. S.; Livingstone, J. R.; Record, M. T., Jr. Use of liquid hydrocarbon and amide transfer data to estimate contributions to protein folding. Biochemistry 1992, 31, 3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record Jr., M.T.3
  • 33
  • 34
    • 0041624164 scopus 로고    scopus 로고
    • A new angle on heat capacity changes in hydrophobic solvation
    • Gallagher, K. R.; Sharp, K. A. A new angle on heat capacity changes in hydrophobic solvation. J. Am. Chem. Soc. 2003, 125, 9853-9860.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9853-9860
    • Gallagher, K.R.1    Sharp, K.A.2
  • 35
    • 2542436054 scopus 로고
    • Structural aspects of ion-solvent interaction in aqueous solutions: A suggested picture of water structure
    • Frank, H. S.; Wen, W. Y. Structural aspects of ion-solvent interaction in aqueous solutions: A suggested picture of water structure. Discuss. Faraday Soc. 1957, 24, 133.
    • (1957) Discuss. Faraday Soc. , vol.24 , pp. 133
    • Frank, H.S.1    Wen, W.Y.2
  • 36
    • 24544464348 scopus 로고
    • Structure of water and hydrophobic bonding. I. A model for the thermodynamic properties of liquid water
    • Nemethy, G.; Scheraga, H. Structure of water and hydrophobic bonding. I. A model for the thermodynamic properties of liquid water. J. Chem. Phys. 1962, 36, 33823400.
    • (1962) J. Chem. Phys. , vol.36 , pp. 33823400
    • Nemethy, G.1    Scheraga, H.2
  • 37
    • 0000124533 scopus 로고
    • Raman spectral studies of the effects of temperature on water structure
    • Walrafen, G. E. Raman spectral studies of the effects of temperature on water structure. J. Chem. Phys. 1967, 47, 114-126.
    • (1967) J. Chem. Phys. , vol.47 , pp. 114-126
    • Walrafen, G.E.1
  • 40
    • 7444231098 scopus 로고    scopus 로고
    • Energetics of hydrogen bond network rearrangements in liquid water
    • DOI 10.1126/science.1102560
    • Smith, J.; Cappa, C.; Wilson, K.; Messer, B.; Cohen, R.; Saykally, R. Energetics of hydrogen bond network rearrangements in liquid water. Science 2004, 306, 851853. (Pubitemid 39446989)
    • (2004) Science , vol.306 , Issue.5697 , pp. 851-853
    • Smith, J.D.1    Cappa, C.D.2    Wilson, K.R.3    Messer, B.M.4    Cohen, R.C.5    Saykally, R.J.6
  • 42
    • 20344399637 scopus 로고    scopus 로고
    • Temperature excursion infrared (TEIR) spectroscopy used to study hydrogen bonding between water and biomolecules
    • DOI 10.1016/j.bbapap.2005.03.008, PII S1570963905000981, Solvent Effects
    • Vanderkooi, J. M.; Dashnau, J. L; Zelent, B. Temperature excursion Infrared (TBR) spectroscopy used to study hydrogen bonding between water and blomolecules. Biochim. Biophys. Acta 2005, 1749, 214-233. (Pubitemid 40778666)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1749 , Issue.2 , pp. 214-233
    • Vanderkooi, J.M.1    Dashnau, J.L.2    Zelent, B.3
  • 43
    • 0035104083 scopus 로고    scopus 로고
    • Water structure changes Induced by hydrophobic and polar solutes revealed by simulations and Infrared spectroscopy
    • Sharp, K. A.; Madan, B.; Manas, E. S.; Vanderkooi, J. M. Water structure changes Induced by hydrophobic and polar solutes revealed by simulations and Infrared spectroscopy. J. Chem. Phys.2001, 114, 1791-1796.
    • (2001) J. Chem. Phys. , vol.114 , pp. 1791-1796
    • Sharp, K.A.1    Madan, B.2    Manas, E.S.3    Vanderkooi, J.M.4
  • 44
    • 52949140194 scopus 로고    scopus 로고
    • Effects of salts of the Hofmeister series on the hydrogen bond network of water
    • Nucci, N. V.; Vanderkooi, J. M. Effects of salts of the Hofmeister series on the hydrogen bond network of water. J. Mol. Liq. 2008, 143, 160-170.
    • (2008) J. Mol. Liq. , vol.143 , pp. 160-170
    • Nucci, N.V.1    Vanderkooi, J.M.2
  • 45
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • Collins, K. D. Charge density-dependent strength of hydration and biological structure. Biophys. J. 1997, 72, 65-76.
    • (1997) Biophys. J. , vol.72 , pp. 65-76
    • Collins, K.D.1
  • 46
    • 33746376611 scopus 로고    scopus 로고
    • Hydrogen bonding and the cryoprotective properties of glycerol/water mixtures
    • DOI 10.1021/jp0618680
    • Dashnau, J. L; Nucci, N. V.; Sharp, K.; Vanderkooi, J. M. Hydrogen bonding and the cryoprotective properties of gflycerol/water mixtures. J. Phys. Chem. B 2006, 110, 13670-13677. (Pubitemid 44115607)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.27 , pp. 13670-13677
    • Dashnau, J.L.1    Nucci, N.V.2    Sharp, K.A.3    Vanderkooi, J.M.4
  • 47
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 1986, 131, 266-280. (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.VOL. 131 , pp. 266-280
    • Pace, C.N.1
  • 49
    • 0141560450 scopus 로고    scopus 로고
    • Impact of urea on water structure: A clue to its properties as a denaturant?
    • DOI 10.1016/S0301-4622(03)00095-4
    • Soper, A. K.; Castner, E. W.; Luzar, A. Impact of urea on water structure: A clue to its properties as a denaturant? Biophys Chem. 2003, 105, 649-666. (Pubitemid 37123089)
    • (2003) Biophysical Chemistry , vol.105 , Issue.2-3 , pp. 649-666
    • Soper, A.K.1    Castner, E.W.2    Luzar, A.3
  • 50
    • 56049116742 scopus 로고    scopus 로고
    • Changes in water structure induced by the guanidinium cation and implications for protein denaturation
    • Scott, J. N.; Nucci, N. V.; Vanderkooi, J. M. Changes In water structure induced by the guanidinium cation and implications for protein denaturation. J. Phys. Chem. A 2008, 112, 10939-10948.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 10939-10948
    • Scott, J.N.1    Nucci, N.V.2    Vanderkooi, J.M.3
  • 51
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 52
    • 0034684214 scopus 로고    scopus 로고
    • Infrared spectra of amide groups in α-helical proteins: Evidence for hydrogen bonding between helices and water
    • Manas, E. S.; Getahun, Z.; Wright, W. W.; DeGrado, W. F.; Vanderkooi, J. M. Infrared spectra of amide groups In α-helical proteins: Evidence for hydrogen bonding between helices and water. J. Am. Chem. Soc. 2000, 122, 9883-9890.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9883-9890
    • Manas, E.S.1    Getahun, Z.2    Wright, W.W.3    Degrado, W.F.4    Vanderkooi, J.M.5
  • 53
    • 0037370999 scopus 로고    scopus 로고
    • The hydration of amides in helices: A comprehensive picture from molecular dynamics, IR and NMR
    • Walsh, S. T. R.; Cheng, R. P.; Daggett, V.; Vanderkooi, J. M.; DeGrado, W. F. The hydration of amides In helices: A comprehensive picture from molecular dynamics, IR and NMR. Protein Sci. 2003, 12, 520-531.
    • (2003) Protein Sci. , vol.12 , pp. 520-531
    • Walsh, S.T.R.1    Cheng, R.P.2    Daggett, V.3    Vanderkooi, J.M.4    Degrado, W.F.5
  • 54
    • 33846090722 scopus 로고    scopus 로고
    • Structural disorder of the CD3ξ transmembrane domain studied with 2D IR spectroscopy and molecular dynamics simulations
    • Mukherjee, P.; Kass, I.; Arkin, I. T.; Zanni, M. T. Structural disorder of the CD3ξ transmembrane domain studied with 2D IR spectroscopy and molecular dynamics simulations. J. Phys. Chem. B 2006, 110, 24740-24749.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 24740-24749
    • Mukherjee, P.1    Kass, I.2    Arkin, I.T.3    Zanni, M.T.4
  • 55
    • 16344378406 scopus 로고    scopus 로고
    • Hydrophobic tendency of polar group hydration as a major force in type i antifreeze protein recognition
    • Yang, C.; Sharp, K. Hydrophobic tendency of polar group hydration as a major force in type I antifreeze protein recognition. Proteins 2005, 59, 266-274.
    • (2005) Proteins , vol.59 , pp. 266-274
    • Yang, C.1    Sharp, K.2
  • 56
    • 1642587769 scopus 로고    scopus 로고
    • The mechanism of the type III antifreeze protein action: A computational study
    • Yang, C.; Sharp, K. A. The mechanism of the type III antifreeze protein action: A computational study. Biophys. Chem. 2004, 109, 137-148.
    • (2004) Biophys. Chem. , vol.109 , pp. 137-148
    • Yang, C.1    Sharp, K.A.2
  • 57
    • 48249090027 scopus 로고    scopus 로고
    • Mirror image forms of snow flea antifreeze protein (sfAFP) prepared by total chemical synthesis have identical antifreeze activities
    • Pentelute, B. L; Gates, Z.; Dashnau, J. L; Vanderkooi, J. M.; Kent, S. B. H. Mirror image forms of snow flea antifreeze protein (sfAFP) prepared by total chemical synthesis have identical antifreeze activities. J. Am. Chem. Soc. 2008, 130, 97029707.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 97029707
    • Pentelute, B.L.1    Gates, Z.2    Dashnau, J.L.3    Vanderkooi, J.M.4    Kent, S.B.H.5
  • 58
    • 62549117748 scopus 로고    scopus 로고
    • Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy
    • Zelent, B.; Bryan, M. A.; Sharp, K. A.; Vanderkooi, J. M. Influence of surface groups of proteins on water studied by freezing/thawing hysteresis and infrared spectroscopy. Biophys. Chem. 2009, 141, 222-230.
    • (2009) Biophys. Chem. , vol.141 , pp. 222-230
    • Zelent, B.1    Bryan, M.A.2    Sharp, K.A.3    Vanderkooi, J.M.4
  • 59
    • 46149133757 scopus 로고
    • A new determination of the structure of water at 25degrees-C
    • Soper, A. K.; Phillips, M. G. A new determination of the structure of water at 25degrees-C. Chem. Phys. 1986, 107, 47-60.
    • (1986) Chem. Phys. , vol.107 , pp. 47-60
    • Soper, A.K.1    Phillips, M.G.2
  • 60
    • 10944261571 scopus 로고    scopus 로고
    • Liquid and Ice water and glycerol/water glasses compared by Infrared spectroscopy from 295 to 12 K
    • Zelent, B.; Nucci, N. V.; Vanderkooi, J. M. Liquid and Ice water and glycerol/water glasses compared by Infrared spectroscopy from 295 to 12 K. J. Phys. Chem. A 2004, 108, 11141-11150.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 11141-11150
    • Zelent, B.1    Nucci, N.V.2    Vanderkooi, J.M.3


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