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Volumn 95, Issue 11, 2008, Pages 5257-5267

Hydration dynamics in a partially denatured ensemble of the globular protein human α-lactalbumin investigated with molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

LACTALBUMIN; SOLVENT; WATER;

EID: 58149340605     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.136531     Document Type: Article
Times cited : (30)

References (81)
  • 1
    • 0001529088 scopus 로고
    • Quasielastic light scattering from human α-lactalbumin: Comparison of molecular dimensions in native and "molten globule" states
    • Gast, K., D. Zirwer, H. Welfle, V. E. Bychkova, and O. B. Ptitsyn. 1986. Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and "molten globule" states. Int. J. Biol. Macromol. 8:231-236.
    • (1986) Int. J. Biol. Macromol , vol.8 , pp. 231-236
    • Gast, K.1    Zirwer, D.2    Welfle, H.3    Bychkova, V.E.4    Ptitsyn, O.B.5
  • 2
    • 0037028161 scopus 로고    scopus 로고
    • Biological water: Femtosecond dynamics of macromolecular hydration
    • Pal, S. K., J. Peon, B. Bagchi, and A. H. Zewail. 2002. Biological water: femtosecond dynamics of macromolecular hydration. J. Phys. Chem. B. 106:12376-12395.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12376-12395
    • Pal, S.K.1    Peon, J.2    Bagchi, B.3    Zewail, A.H.4
  • 6
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand, M., A. J. Dianoux, W. Petry, and G. Zaccai. 1993. Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA. 90:9668-9672.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 8
    • 0035949666 scopus 로고    scopus 로고
    • On the nature of a glassy state of matter in a hydrated protein: Relation to protein function
    • Teeter, M. M., A. Yamano, B. Stec, and U. Mohanty. 2001. On the nature of a glassy state of matter in a hydrated protein: relation to protein function. Proc. Natl. Acad. Sci. USA. 98:11242-11247.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11242-11247
    • Teeter, M.M.1    Yamano, A.2    Stec, B.3    Mohanty, U.4
  • 9
    • 20144366574 scopus 로고    scopus 로고
    • Protein-water displacement distributions
    • Doster, W., and M. Settles. 2005. Protein-water displacement distributions. Biochim. Biophys. Acta. 1749:173-186.
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 173-186
    • Doster, W.1    Settles, M.2
  • 11
    • 41849097415 scopus 로고    scopus 로고
    • Coincidence of dynamical transitions in a soluble protein and its hydration water: Direct measurements by neutron scattering and MD simulations
    • Wood, K., A. Frolich, A. Paciaroni, M. Moulin, M. Hartlein, G. Zaccai, D. J. Tobias, and M. Weik. 2008. Coincidence of dynamical transitions in a soluble protein and its hydration water: direct measurements by neutron scattering and MD simulations. J. Am. Chem. Soc. 130:4586-4587.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 4586-4587
    • Wood, K.1    Frolich, A.2    Paciaroni, A.3    Moulin, M.4    Hartlein, M.5    Zaccai, G.6    Tobias, D.J.7    Weik, M.8
  • 12
    • 41649116070 scopus 로고    scopus 로고
    • Protein structure and hydration probed by SANS and osmotic stress
    • Stanley, C., S. Krueger, V. A. Parsegian, and D. C. Rau. 2008. Protein structure and hydration probed by SANS and osmotic stress. Biophys. J. 94:2777-2789.
    • (2008) Biophys. J , vol.94 , pp. 2777-2789
    • Stanley, C.1    Krueger, S.2    Parsegian, V.A.3    Rau, D.C.4
  • 13
    • 0033842337 scopus 로고    scopus 로고
    • Water-protein interactions in the molten-globule state of carbonic anhydrase b: An NMR spin-diffusion study
    • Kutyshenko, V. P., and M. Cortijo. 2000. Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Protein Sci. 9:1540-1547.
    • (2000) Protein Sci , vol.9 , pp. 1540-1547
    • Kutyshenko, V.P.1    Cortijo, M.2
  • 14
    • 38049091066 scopus 로고    scopus 로고
    • Investigation of water bound to photosystem I with multiquantum filtered 17O nuclear magnetic resonance
    • Krzystyniak, M., G. Shen, J. H. Golbeck, and M. L. Antonkine. 2008. Investigation of water bound to photosystem I with multiquantum filtered 17O nuclear magnetic resonance. J. Chem. Phys. 128:014503-014515.
    • (2008) J. Chem. Phys , vol.128 , pp. 014503-014515
    • Krzystyniak, M.1    Shen, G.2    Golbeck, J.H.3    Antonkine, M.L.4
  • 15
    • 21244437631 scopus 로고    scopus 로고
    • NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins
    • Bokor, M., V. Csizmok, D. Kovacs, P. Banki, P. Friedrich, P. Tompa, and K. Tompa. 2005. NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophys. J. 88:2030-2037.
    • (2005) Biophys. J , vol.88 , pp. 2030-2037
    • Bokor, M.1    Csizmok, V.2    Kovacs, D.3    Banki, P.4    Friedrich, P.5    Tompa, P.6    Tompa, K.7
  • 16
    • 0028948786 scopus 로고
    • Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion
    • Denisov, V. P., and B. Halle. 1995. Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245:682-697.
    • (1995) J. Mol. Biol , vol.245 , pp. 682-697
    • Denisov, V.P.1    Halle, B.2
  • 17
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in aqueous solution
    • Denisov, V. P., and B. Halle. 1996. Protein hydration dynamics in aqueous solution. Faraday Disc. 103:227-244.
    • (1996) Faraday Disc , vol.103 , pp. 227-244
    • Denisov, V.P.1    Halle, B.2
  • 18
    • 0033012840 scopus 로고    scopus 로고
    • Hydration of denatured and molten globule proteins
    • Denisov, V. P., B. H. Jonsson, and B. Halle. 1999. Hydration of denatured and molten globule proteins. Nat. Struct. Biol. 6:253-260.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 253-260
    • Denisov, V.P.1    Jonsson, B.H.2    Halle, B.3
  • 19
    • 0142123115 scopus 로고    scopus 로고
    • Biomolecular hydration: From water dynamics to hydrodynamics
    • Halle, B., and M. Davidovic. 2003. Biomolecular hydration: from water dynamics to hydrodynamics. Proc. Natl. Acad. Sci. USA. 100:12135-12140.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12135-12140
    • Halle, B.1    Davidovic, M.2
  • 21
    • 33746689781 scopus 로고    scopus 로고
    • Role of solvent on protein-matrix coupling in MbCO embedded in water-saccharide systems: A Fourier transform infrared spectroscopy study
    • Giuffrida, S., G. Cottone, and L. Cordone. 2006. Role of solvent on protein-matrix coupling in MbCO embedded in water-saccharide systems: a Fourier transform infrared spectroscopy study. Biophys. J. 91:968-980.
    • (2006) Biophys. J , vol.91 , pp. 968-980
    • Giuffrida, S.1    Cottone, G.2    Cordone, L.3
  • 22
    • 33646170638 scopus 로고    scopus 로고
    • Hydration dependence of conformational dielectric relaxation of lysozyme
    • Knab, J., J.-Y. Chen, and A. Markelz. 2006. Hydration dependence of conformational dielectric relaxation of lysozyme. Biophys. J. 90:2576-2581.
    • (2006) Biophys. J , vol.90 , pp. 2576-2581
    • Knab, J.1    Chen, J.-Y.2    Markelz, A.3
  • 23
    • 33646155117 scopus 로고    scopus 로고
    • Probing the collective vibrational dynamics of a protein in liquid water by terahertz absorption spectroscopy
    • Xu, J., K. W. Plaxco, and S. J. Allen. 2006. Probing the collective vibrational dynamics of a protein in liquid water by terahertz absorption spectroscopy. Protein Sci. 15:1175-1181.
    • (2006) Protein Sci , vol.15 , pp. 1175-1181
    • Xu, J.1    Plaxco, K.W.2    Allen, S.J.3
  • 26
    • 0027957222 scopus 로고
    • Distribution function implied dynamics versus residence times and correlations: Solvation shells of myoglobin
    • Lounnas, V., and B. M. Pettitt. 1994. Distribution function implied dynamics versus residence times and correlations: solvation shells of myoglobin. Proteins. 18:148-160.
    • (1994) Proteins , vol.18 , pp. 148-160
    • Lounnas, V.1    Pettitt, B.M.2
  • 27
    • 0001030002 scopus 로고    scopus 로고
    • Water dynamical anomalies evidenced by molecular-dynamics simulations at the solvent-protein interface
    • Rocchi, C., A. R. Bizzarri, and S. Cannistraro. 1998. Water dynamical anomalies evidenced by molecular-dynamics simulations at the solvent-protein interface. Phys. Rev. E. 57:3315-3325.
    • (1998) Phys. Rev. E , vol.57 , pp. 3315-3325
    • Rocchi, C.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 28
    • 0037067102 scopus 로고    scopus 로고
    • Water rotational relaxation and diffusion in hydrated lysozyme
    • Marchi, M., F. Sterpone, and M. Ceccarelli. 2002. Water rotational relaxation and diffusion in hydrated lysozyme. J. Am. Chem. Soc. 124:6787-6791.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6787-6791
    • Marchi, M.1    Sterpone, F.2    Ceccarelli, M.3
  • 29
    • 0032757044 scopus 로고    scopus 로고
    • Environmental dependence of the dynamics of protein hydration water
    • Tarek, M., and D. J. Tobias. 1999. Environmental dependence of the dynamics of protein hydration water. J. Am. Chem. Soc. 121:9740-9741.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9740-9741
    • Tarek, M.1    Tobias, D.J.2
  • 30
    • 34547485422 scopus 로고    scopus 로고
    • How protein surfaces induce anomalous dynamics of hydration water
    • Pizzitutti, F., M. Marchi, F. Sterpone, and P. J. Rossky. 2007. How protein surfaces induce anomalous dynamics of hydration water. J. Phys. Chem. B. 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
  • 32
    • 34247599780 scopus 로고    scopus 로고
    • Accurate, conformation-dependent predictions of solvent effects on protein ionization constants
    • Barth, P., T. Alber, and P. B. Harbury. 2007. Accurate, conformation-dependent predictions of solvent effects on protein ionization constants. Proc. Natl. Acad. Sci. USA. 104:4898-4903.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4898-4903
    • Barth, P.1    Alber, T.2    Harbury, P.B.3
  • 34
    • 0034715463 scopus 로고    scopus 로고
    • Amplitudes and frequencies of protein dynamics: Analysis of discrepancies between neutron scattering and molecular dynamics simulations
    • Tarek, M., G. J. Martyna, and D. J. Tobias. 2000. Amplitudes and frequencies of protein dynamics: analysis of discrepancies between neutron scattering and molecular dynamics simulations. J. Am. Chem. Soc. 122:10450-10451.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 10450-10451
    • Tarek, M.1    Martyna, G.J.2    Tobias, D.J.3
  • 35
    • 0033921496 scopus 로고    scopus 로고
    • Bacteriorhodopsin: The functional details of a molecular machine are being resolved
    • Heberle, J., J. Fitter, H. J. Sass, and G. Büldt. 2000. Bacteriorhodopsin: the functional details of a molecular machine are being resolved. Biophys. Chem. 85:229-248.
    • (2000) Biophys. Chem , vol.85 , pp. 229-248
    • Heberle, J.1    Fitter, J.2    Sass, H.J.3    Büldt, G.4
  • 36
    • 0036534542 scopus 로고    scopus 로고
    • Protein-water interactions in a dynamic world
    • Mattos, C. 2002. Protein-water interactions in a dynamic world. Trends Biochem. Sci. 27:203-208.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 203-208
    • Mattos, C.1
  • 38
    • 33646904758 scopus 로고    scopus 로고
    • Protein folding-simulation
    • Daggett, V. 2006. Protein folding-simulation. Chem. Rev. 106:1898-1916.
    • (2006) Chem. Rev , vol.106 , pp. 1898-1916
    • Daggett, V.1
  • 39
    • 33745032291 scopus 로고    scopus 로고
    • Water mediation in protein folding and molecular recognition
    • Levy, Y., and J. N. Onuchic. 2006. Water mediation in protein folding and molecular recognition. Annu. Rev. Biophys. Biomol. Struct. 35:389-415.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 389-415
    • Levy, Y.1    Onuchic, J.N.2
  • 40
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung, M. S., A. E. Garcia, and J. N. Onuchic. 2002. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl. Acad. Sci. USA. 99:685-690.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 685-690
    • Cheung, M.S.1    Garcia, A.E.2    Onuchic, J.N.3
  • 41
    • 10944273651 scopus 로고    scopus 로고
    • Large gain in translational entropy of water is a major driving force in protein folding
    • Harano, Y., and M. Kinoshita. 2004. Large gain in translational entropy of water is a major driving force in protein folding. Chem Phys. Lett. 399:342-348.
    • (2004) Chem Phys. Lett , vol.399 , pp. 342-348
    • Harano, Y.1    Kinoshita, M.2
  • 42
    • 0035128362 scopus 로고    scopus 로고
    • Effect of viscosity on the kinetics of α-helix and β-hairpin formation
    • Jas, G. S., W. A. Eaton, and J. Hofrichter. 2001. Effect of viscosity on the kinetics of α-helix and β-hairpin formation. J. Phys. Chem. B. 105:261-272.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 261-272
    • Jas, G.S.1    Eaton, W.A.2    Hofrichter, J.3
  • 43
    • 33846617642 scopus 로고    scopus 로고
    • Diffusional barrier in the unfolding of a small protein
    • Pradeep, L., and J. B. Udgaonkar. 2007. Diffusional barrier in the unfolding of a small protein. J. Mol. Biol. 366:1016-1028.
    • (2007) J. Mol. Biol , vol.366 , pp. 1016-1028
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 44
    • 0031851978 scopus 로고    scopus 로고
    • Equilibrium NMR studies of unfolded and partially folded proteins
    • Dyson, H. J., and P. E. Wright. 1998. Equilibrium NMR studies of unfolded and partially folded proteins. Nat. Struct. Mol. Biol. 5:499-503.
    • (1998) Nat. Struct. Mol. Biol , vol.5 , pp. 499-503
    • Dyson, H.J.1    Wright, P.E.2
  • 45
    • 0345862090 scopus 로고    scopus 로고
    • The energy landscape for protein folding and possible connections to function
    • Cheung, M. S., L. L. Chavez, and J. N. Onuchic. 2004. The energy landscape for protein folding and possible connections to function. Polymer. 45:547-555.
    • (2004) Polymer , vol.45 , pp. 547-555
    • Cheung, M.S.1    Chavez, L.L.2    Onuchic, J.N.3
  • 46
    • 33751297109 scopus 로고    scopus 로고
    • Exploration of the secondary structure specific differential solvation dynamics between the native and molten globule states of the protein HP-36
    • Bandyopadhyay, S., S. Chakraborty, and B. Bagchi. 2006. Exploration of the secondary structure specific differential solvation dynamics between the native and molten globule states of the protein HP-36. J. Phys. Chem. B. 110:20629-20634.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 20629-20634
    • Bandyopadhyay, S.1    Chakraborty, S.2    Bagchi, B.3
  • 47
    • 48549092515 scopus 로고    scopus 로고
    • Dynamics of water in the hydration layer of a partially unfolded structure of the protein HP-36
    • Chakraborty, S., and S. Bandyopadhyay. 2008. Dynamics of water in the hydration layer of a partially unfolded structure of the protein HP-36. J. Phys. Chem. B. 112:6500-6507.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6500-6507
    • Chakraborty, S.1    Bandyopadhyay, S.2
  • 48
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins. 6:87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 49
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47:83-229.
    • (1995) Adv. Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 51
    • 2342424239 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: Implications for its physiological activities
    • Sutovsky, H., and E. Gazit. 2004. The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. J. Biol. Chem. 279:17190-17196.
    • (2004) J. Biol. Chem , vol.279 , pp. 17190-17196
    • Sutovsky, H.1    Gazit, E.2
  • 52
    • 33745740540 scopus 로고    scopus 로고
    • Apolipoprotein (apo) E4 and Alzheimer's disease: Unique conformational and biophysical properties of apoE4 can modulate neuropathology
    • Mahley, R. W., and Y. Huang. 2006. Apolipoprotein (apo) E4 and Alzheimer's disease: unique conformational and biophysical properties of apoE4 can modulate neuropathology. Acta. Neurolog. Scand. 114:8-14.
    • (2006) Acta. Neurolog. Scand , vol.114 , pp. 8-14
    • Mahley, R.W.1    Huang, Y.2
  • 53
    • 0033637521 scopus 로고    scopus 로고
    • The dynamics of protein hydration water: A quantitative comparison of molecular dynamics simulations and neutron-scattering experiments
    • Tarek, M., and D. J. Tobias. 2000. The dynamics of protein hydration water: a quantitative comparison of molecular dynamics simulations and neutron-scattering experiments. Biophys. J. 79:3244-3257.
    • (2000) Biophys. J , vol.79 , pp. 3244-3257
    • Tarek, M.1    Tobias, D.J.2
  • 54
    • 0030057862 scopus 로고    scopus 로고
    • The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation
    • Abseher, R., H. Schreiber, and O. Steinhauser. 1996. The influence of a protein on water dynamics in its vicinity investigated by molecular dynamics simulation. Proteins. 25:366-378.
    • (1996) Proteins , vol.25 , pp. 366-378
    • Abseher, R.1    Schreiber, H.2    Steinhauser, O.3
  • 55
    • 0345498055 scopus 로고    scopus 로고
    • Anomalous diffusion of adsorbed water: A neutron scattering study of hydrated myoglobin
    • Settles, M., and W. Doster. 1996. Anomalous diffusion of adsorbed water: a neutron scattering study of hydrated myoglobin. Faraday Disc. 103:269-279.
    • (1996) Faraday Disc , vol.103 , pp. 269-279
    • Settles, M.1    Doster, W.2
  • 56
    • 0031019791 scopus 로고    scopus 로고
    • Molten globule of human α-lactalbumin: Hydration, density, and compressibility of the interior
    • Kharakoz, D. P., and V. E. Bychkova. 1997. Molten globule of human α-lactalbumin: hydration, density, and compressibility of the interior. Biochemistry. 36:1882-1890.
    • (1997) Biochemistry , vol.36 , pp. 1882-1890
    • Kharakoz, D.P.1    Bychkova, V.E.2
  • 57
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink, A. L. 1995. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 58
    • 0035895427 scopus 로고    scopus 로고
    • Exploration of partially unfolded states of human α-lactalbumin by molecular dynamics simulation
    • Paci, E., L. J. Smith, C. M. Dobson, and M. Karplus. 2001. Exploration of partially unfolded states of human α-lactalbumin by molecular dynamics simulation. J. Mol. Biol. 306:329-347.
    • (2001) J. Mol. Biol , vol.306 , pp. 329-347
    • Paci, E.1    Smith, L.J.2    Dobson, C.M.3    Karplus, M.4
  • 59
  • 60
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • Qiu, D., P. S. Shenkin, F. P. Hollinger, and W. C. Still. 1997. The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii. J. Phys. Chem. A. 101:3005-3014.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 61
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima, K., Y. Hiraoka, M. Ikeguchi, and S. Sugai. 1985. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 65
    • 36449003554 scopus 로고
    • Constant pressure molecular dynamics algorithms
    • Martyna, G. J., D. J. Tobias, and M. L. Klein. 1994. Constant pressure molecular dynamics algorithms. J. Chem. Phys. 101:4177-4189.
    • (1994) J. Chem. Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 66
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller S. E., Y. Zhang, R. W. Pastor, and B. R. Brooks. 1995. Constant pressure molecular dynamics simulation: the Langevin piston method. J. Chem. Phys. 103:4613-4621.
    • (1995) J. Chem. Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 67
    • 0000026966 scopus 로고    scopus 로고
    • Explicit reversible integrators for extended systems dynamics
    • Martyna, G. J., M. E. Tuckerman, D. J. Tobias, and M. L. Klein. 1996. Explicit reversible integrators for extended systems dynamics. Mol. Phys. 87:1117-1157.
    • (1996) Mol. Phys , vol.87 , pp. 1117-1157
    • Martyna, G.J.1    Tuckerman, M.E.2    Tobias, D.J.3    Klein, M.L.4
  • 70
    • 0002550755 scopus 로고
    • Nearly exponential quadrupolar relaxation. A perturbation treatment
    • Halle, B., and H. Wennerstroem. 1981. Nearly exponential quadrupolar relaxation. A perturbation treatment. J. Magn. Reson. 44:89-100.
    • (1981) J. Magn. Reson , vol.44 , pp. 89-100
    • Halle, B.1    Wennerstroem, H.2
  • 71
    • 0031556719 scopus 로고    scopus 로고
    • Orientational disorder and entropy of water in protein cavities
    • Denisov, V. P., K. Venu, J. Peters, H. D. Horlein, and B. Halle. 1997. Orientational disorder and entropy of water in protein cavities. J. Phys. Chem. B. 101:9380-9389.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 9380-9389
    • Denisov, V.P.1    Venu, K.2    Peters, J.3    Horlein, H.D.4    Halle, B.5
  • 73
    • 10044267947 scopus 로고    scopus 로고
    • Stabilization of internal charges in a protein: Water penetration or conformational change?
    • Denisov, V. P., J. L. Schlessman, B. E. Garcia-Moreno, and B. Halle. 2004. Stabilization of internal charges in a protein: water penetration or conformational change? Biophys. J. 87:3982-3994.
    • (2004) Biophys. J , vol.87 , pp. 3982-3994
    • Denisov, V.P.1    Schlessman, J.L.2    Garcia-Moreno, B.E.3    Halle, B.4
  • 74
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F. T., W. I. Weis, K. M. Flaherty, and A. T. Brunger. 1996. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science. 271:72-77.
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 75
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • Merzel, F., and J. C. Smith. 2002. Is the first hydration shell of lysozyme of higher density than bulk water? Proc. Natl. Acad. Sci. USA. 99:5378-5383.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 76
    • 0036286851 scopus 로고    scopus 로고
    • Solvation and hydration of proteins and nucleic acids: A theoretical view of simulation and experiment
    • Makarov, V., B. M. Pettitt, and M. Feig. 2002. Solvation and hydration of proteins and nucleic acids: a theoretical view of simulation and experiment. Acc. Chem. Res. 35:376-384.
    • (2002) Acc. Chem. Res , vol.35 , pp. 376-384
    • Makarov, V.1    Pettitt, B.M.2    Feig, M.3
  • 77
    • 84889854751 scopus 로고    scopus 로고
    • Protein conformational transitions as seen from the solvent: Magnetic relaxation dispersion studies of water, co-solvent, and denaturant interactions with nonnative proteins
    • J. Buchner and T. Kiefhaber, editors. Wiley-VCH, Weinheim, Germany
    • Halle, B., V. P. Denisov, K. Modig, and M. Davidoc. 2005. Protein conformational transitions as seen from the solvent: magnetic relaxation dispersion studies of water, co-solvent, and denaturant interactions with nonnative proteins. In Protein Folding Handbook. J. Buchner and T. Kiefhaber, editors. Wiley-VCH, Weinheim, Germany. 201-242.
    • (2005) Protein Folding Handbook , pp. 201-242
    • Halle, B.1    Denisov, V.P.2    Modig, K.3    Davidoc, M.4
  • 78
    • 0033016906 scopus 로고    scopus 로고
    • Protein folding as seen from water's perspective
    • Shortle, D. 1999. Protein folding as seen from water's perspective. Nat. Struct. Biol. 6:203-205.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 203-205
    • Shortle, D.1
  • 79
    • 0032825667 scopus 로고    scopus 로고
    • α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds
    • Redfield, C., B. A. Schulman, M. A. Milhollen, P. S. Kim, and C. M. Dobson. 1999. α-Lactalbumin forms a compact molten globule in the absence of disulfide bonds. Nat. Struct. Biol. 6:948-952.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 948-952
    • Redfield, C.1    Schulman, B.A.2    Milhollen, M.A.3    Kim, P.S.4    Dobson, C.M.5
  • 80
    • 0034697642 scopus 로고    scopus 로고
    • Compaction during protein folding studied by realtime NMR diffusion experiments
    • Balbach, J. 2000. Compaction during protein folding studied by realtime NMR diffusion experiments. J. Am. Chem. Soc. 122:5887-5888.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5887-5888
    • Balbach, J.1
  • 81
    • 0035912911 scopus 로고    scopus 로고
    • Structure and dynamics of the α-lactalbumin molten globule: Fluorescence studies using proteins containing a single tryptophan residue
    • Chakraborty, S., V. Ittah, P. Bai, L. Luo, E. Haas, and Z. Y. Peng. 2001. Structure and dynamics of the α-lactalbumin molten globule: fluorescence studies using proteins containing a single tryptophan residue. Biochemistry. 40:7228-7238.
    • (2001) Biochemistry , vol.40 , pp. 7228-7238
    • Chakraborty, S.1    Ittah, V.2    Bai, P.3    Luo, L.4    Haas, E.5    Peng, Z.Y.6


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