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Volumn 113, Issue 46, 2009, Pages 15382-15391

Ultrafast vibrational spectroscopy of a degenerate mode of guanidinium chloride

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; CHLORINE COMPOUNDS; DEUTERIUM; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROBES; VIBRATIONAL SPECTROSCOPY;

EID: 70449562714     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9069256     Document Type: Article
Times cited : (28)

References (55)
  • 2
    • 0035916258 scopus 로고    scopus 로고
    • Effect of salts on the stability and folding of staphylococcal nuclease
    • DOI 10.1021/bi000861k
    • (2) Nishimura, C.; Uversky, V. N.; Fink, A. L. Effect of Salts on the Stability and Folding of Staphylococcal Nuclease. Biochemistry 2001, 40 (7), 2113-2128. (Pubitemid 32165682)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2113-2128
    • Nishimura, C.1    Uversky, V.N.2    Fink, A.L.3
  • 3
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the hofmeister effect
    • Ramos, C. H. I.; Baldwin, R. L. Sulfate Anion Stabilization of Native Ribonuclease A Both by Anion Binding and by the Hofmeister Effect. Protein Sci. 2002, 11 (7), 1771-1778.
    • (2002) Protein Sci. , vol.11 , Issue.7 , pp. 1771-1778
    • Ramos, C.H.I.1    Baldwin, R.L.2
  • 4
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E. Y.; Krishnan, S.; Randolph, T. W.; Carpenter, J. F. Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation. Pharm. Res. 2003, 20 (9), 1325-1336.
    • (2003) Pharm. Res. , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 5
    • 1942519360 scopus 로고    scopus 로고
    • The efficiency of different salts to screen charge interactions in proteins: A hofmeister effect?
    • Perez-Jimenez, R.; Godoy-Ruiz, R.; Ibarra-Molero, B.; SanchezRuiz, J. M. The Efficiency of Different Salts to Screen Charge Interactions in Proteins: A Hofmeister Effect? Biophys. J. 2004, 86 (4), 2414-2429.
    • (2004) Biophys. J. , vol.86 , Issue.4 , pp. 2414-2429
    • Perez-Jimenez, R.1    Godoy-Ruiz, R.2    Ibarra-Molero, B.3    Sanchezruiz, J.M.4
  • 6
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process
    • Collins, K. D. Ions from the Hofmeister Series and Osmolytes: Effects on Proteins in Solution and in the Crystallization Process. Methods 2004,34(3), 300-311.
    • (2004) Methods , vol.34 , Issue.3 , pp. 300-311
    • Collins, K.D.1
  • 7
    • 1642409882 scopus 로고    scopus 로고
    • Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: An FT-IR study on staphylococcal nuclease
    • DOI 10.1021/bi036106z
    • (7) Herberhold, H.; Royer, C. A.; Winter, R. Effects of Chaotropic and Kosmotropic Cosolvents on the Pressure-Induced Unfolding and Denaturation of Proteins: An FT-IR Study on Staphylococcal Nuclease. Biochemistry 2004, 43 (12), 3336-3345. (Pubitemid 38391690)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3336-3345
    • Herberhold, H.1    Royer, C.A.2    Winter, R.3
  • 8
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: The Hofmeister series
    • DOI 10.1016/j.cbpa.2006.09.020, PII S1367593106001517
    • (8) Zhang, Y. J.; Cremer, P. S. Interactions between Macromolecules and Ions: The Hofmeister Series. Curr. Opin. Chem. Biol. 2006, 70 (6), 658-663. (Pubitemid 44821892)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.6 , pp. 658-663
    • Zhang, Y.1    Cremer, P.S.2
  • 9
    • 33646336616 scopus 로고    scopus 로고
    • Specific ion effects at protein surfaces: A molecular dynamics study of bovine pancreatic trypsin inhibitor and horseradish peroxidase in selected salt solutions
    • DOI 10.1021/jp0567624
    • (9) Vrbka, L.; Jungwirth, P.; Bauduin, P.; Touraud, D.; Kunz, W. Specific Ion Effects at Protein Surfaces: A Molecular Dynamics Study of Bovine Pancreatic Trypsin Inhibitor and Horseradish Peroxidase in Selected Salt Solutions. J. Phys. Chem. B 2006, 110 (13), 7036-7043. (Pubitemid 43672178)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.13 , pp. 7036-7043
    • Vrbka, L.1    Jungwirth, P.2    Bauduin, P.3    Touraud, D.4    Kunz, W.5
  • 10
    • 25444514520 scopus 로고    scopus 로고
    • Water dynamics in the hydration layer around proteins and micelles
    • DOI 10.1021/cr020661+
    • (10) Bagchi, B. Water Dynamics in the Hydration Layer around Proteins and Micelles. Chem. Rev. 2005, 105 (9), 3197-3219. (Pubitemid 41430808)
    • (2005) Chemical Reviews , vol.105 , Issue.9 , pp. 3197-3219
    • Bagchi, B.1
  • 12
    • 43149121362 scopus 로고    scopus 로고
    • Structural dynamics of aqueous salt solutions
    • Bakker, H. J. Structural Dynamics of Aqueous Salt Solutions. Chem. Rev. 2008, 108 (4), 1456-1473.
    • (2008) Chem. Rev. , vol.108 , Issue.4 , pp. 1456-1473
    • Bakker, H.J.1
  • 13
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition-state for folding of chymotrypsin inhibitor-2-A critical test of the protein engineering method of analysis
    • Jackson, S. E.; Elmasry, N.; Fersht, A. R. Structure of the Hydrophobic Core in the Transition-State for Folding of Chymotrypsin Inhibitor-2-A Critical Test of the Protein Engineering Method of Analysis. Biochemistry 1993, 32 (42), 11270-11278.
    • (1993) Biochemistry , vol.32 , Issue.42 , pp. 11270-11278
    • Jackson, S.E.1    Elmasry, N.2    Fersht, A.R.3
  • 14
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • (14) Mayo, S. L.; Baldwin, R. L. Guanidinium Chloride Induction of Partial Unfolding in Amide Proton-Exchange in Rnase-A. Science 1993, 262 (5135), 873-876. (Pubitemid 24014074)
    • (1993) Science , vol.262 , Issue.5135 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 15
    • 0029643523 scopus 로고
    • Proteinfolding intermediates-native-state hydrogen-exchange
    • Bai, Y. W.; Sosnick, T. R.; Mayne, L.; Englander, S. W. ProteinFolding Intermediates-Native-State Hydrogen-Exchange. Science 1995,269 (5221), 192-197.
    • (1995) Science , vol.269 , Issue.5221 , pp. 192-197
    • Bai, Y.W.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 16
    • 0000397280 scopus 로고
    • Water-structure in concentrated lithium-chloride solutions
    • Tromp, R. H.; Neilson, G. W.; Soper, A. K. Water-Structure in Concentrated Lithium-Chloride Solutions. J. Chem. Phys. 1992, 96 (11), 8460-8469.
    • (1992) J. Chem. Phys. , vol.96 , Issue.11 , pp. 8460-8469
    • Tromp, R.H.1    Neilson, G.W.2    Soper, A.K.3
  • 17
    • 0002619244 scopus 로고
    • Effect of high-salt concentrations on water-structure
    • Leberman, R.; Soper, A. K. Effect of High-Salt Concentrations on Water-Structure. Nature 1995, 378 (6555), 364-366.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 364-366
    • Leberman, R.1    Soper, A.K.2
  • 18
    • 0013934923 scopus 로고
    • Interactions of protein-denaturing salts with model amides
    • Bello, J.; Haas, D.; Bello, H. R. Interactions of Protein-Denaturing Salts with Model Amides. Biochemistry 1966, 5 (8), 2539.
    • (1966) Biochemistry , vol.5 , Issue.8 , pp. 2539
    • Bello, J.1    Haas, D.2    Bello, H.R.3
  • 19
    • 20544461199 scopus 로고    scopus 로고
    • Thermodynamics of protein interactions with urea and guanidinium hydrochloride
    • Makhatadze, G. I. Thermodynamics of Protein Interactions with Urea and Guanidinium Hydrochloride. J. Phys. Chem. B 1999, 103 (23), 4781-4785.
    • (1999) J. Phys. Chem. B , vol.103 , Issue.23 , pp. 4781-4785
    • Makhatadze, G.I.1
  • 20
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride-a calorimetric study
    • Makhatadze, G. I.; Privalov, P. L. Protein Interactions with Urea and Guanidinium Chloride-A Calorimetric Study. J. Mol. Biol. 1992, 226 (2), 491-505.
    • (1992) J. Mol. Biol. , vol.226 , Issue.2 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 21
    • 33947485233 scopus 로고
    • Nonpolar group participation in denaturation of proteins by urea and guanidinium salts. Model compound studies
    • Wetlaufer, D. B.; Coffin, R. L.; Malik, S. K.; Stoller, L. Nonpolar Group Participation in Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies. J. Am. Chem. Soc. 1964, 86 (3), 508-514.
    • (1964) J. Am. Chem. Soc. , vol.86 , Issue.3 , pp. 508-514
    • Wetlaufer, D.B.1    Coffin, R.L.2    Malik, S.K.3    Stoller, L.4
  • 22
    • 0021755210 scopus 로고
    • Protein stabilization and destabilization by guanidinium salts
    • Arakawa, T.; Timasheff, S. N. Protein Stabilization and Destabilization by Guanidinium Salts. Biochemistry 1984, 23 (25), 5924-5929.
    • (1984) Biochemistry , vol.23 , Issue.25 , pp. 5924-5929
    • Arakawa, T.1    Timasheff, S.N.2
  • 23
    • 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 (43), 10939-10948.
    • (2008) J. Phys. Chem. A , vol.112 , Issue.43 , pp. 10939-10948
    • Scott, J.N.1    Nucci, N.V.2    Vanderkooi, J.M.3
  • 24
    • 9644310200 scopus 로고    scopus 로고
    • Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains
    • DOI 10.1016/j.jmb.2004.10.036, PII S0022283604013282
    • (24) Moglich, A.; Krieger, F.; Kiefhaber, T. Molecular Basis for the Effect of Urea and Guanidinium Chloride on the Dynamics of Unfolded Polypeptide Chains. J. Mol. Biol. 2005, 345 (1), 153-162. (Pubitemid 39572832)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.1 , pp. 153-162
    • Moglich, A.1    Krieger, F.2    Kiefhaber, T.3
  • 26
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein Folding and Misfolding. Nature 2003, 426 (6968), 884-890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 27
    • 0035873370 scopus 로고    scopus 로고
    • Two-dimensional IR-spectroscopy: Polarization anisotropy effects
    • DOI 10.1016/S0301-0104(01)00232-4, PII S0301010401002324
    • (27) Hochstrasser, R. M. Two-Dimensional IR-Spectroscopy: Polarization Anisotropy Effects. Chem. Phys. 2001, 266 (2-3), 273-284. (Pubitemid 32416844)
    • (2001) Chemical Physics , vol.266 , Issue.2-3 , pp. 273-284
    • Hochstrasser, R.M.1
  • 28
    • 84962439297 scopus 로고    scopus 로고
    • Density-functional methods for the study of the ground-state vibrations of the guanidinium ion
    • Magalhaes, A. L.; Gomes, J. A. N. F. Density-Functional Methods for the Study of the Ground-State Vibrations of the Guanidinium Ion. Int. J. Quantum Chem. 1997, 61, 725-739.
    • (1997) Int. J. Quantum Chem. , vol.61 , pp. 725-739
    • Magalhaes, A.L.1    Gomes, J.A.N.F.2
  • 29
    • 33845447890 scopus 로고    scopus 로고
    • Molecular structure and infrared spectra of guanidinium cation-a combined theoretical and spectroscopic study
    • Drozd, M. Molecular Structure and Infrared Spectra of Guanidinium Cation-A Combined Theoretical and Spectroscopic Study. Mater. Sci. Eng., B 2007, 136 (1), 20-28.
    • (2007) Mater. Sci. Eng., B , vol.136 , Issue.1 , pp. 20-28
    • Drozd, M.1
  • 30
    • 0013288246 scopus 로고    scopus 로고
    • NIST Chemistry WebBook, NIST Standard Reference Database Number 69, Gaithersburg, MD
    • Lemmon, E. W. Thermophysical Properties of Fluid Systems; NIST Chemistry WebBook, NIST Standard Reference Database Number 69, Gaithersburg, MD.
    • Thermophysical Properties of Fluid Systems
    • Lemmon, E.W.1
  • 31
    • 85024611673 scopus 로고
    • Viscosity of glycerol and its aqueous solutions
    • Segur, J. B.; Oberstar, H. E. Viscosity of Glycerol and Its Aqueous Solutions. Ind. Eng. Chem. 1951, 43 (9), 2117-2120.
    • (1951) Ind. Eng. Chem. , vol.43 , Issue.9 , pp. 2117-2120
    • Segur, J.B.1    Oberstar, H.E.2
  • 32
    • 38148999351 scopus 로고    scopus 로고
    • Correlation of the vibrations of the aqueous azide ion with the O-H modes of bound water molecules
    • Kuo, C. H.; Vorobyev, D. Y.; Chen, J. X.; Hochstrasser, R. M. Correlation of the Vibrations of the Aqueous Azide Ion with the O-H Modes of Bound Water Molecules. J. Phys. Chem. B 2007, 111 (50), 14028-14033.
    • (2007) J. Phys. Chem. B , vol.111 , Issue.50 , pp. 14028-14033
    • Kuo, C.H.1    Vorobyev, D.Y.2    Chen, J.X.3    Hochstrasser, R.M.4
  • 33
    • 21844500452 scopus 로고
    • The theory of ultrafast vibrational spectroscopy
    • Wynne, K.; Hochstrasser, R. M. The Theory of Ultrafast Vibrational Spectroscopy. Chem. Phys. 1995, 193 (3), 211-236.
    • (1995) Chem. Phys. , vol.193 , Issue.3 , pp. 211-236
    • Wynne, K.1    Hochstrasser, R.M.2
  • 35
    • 3343002676 scopus 로고
    • Resonance raman studies of guanidinium and substituted guanidinium ions
    • Sension, R. J.; Hudson, B.; Callis, P. R. Resonance Raman Studies of Guanidinium and Substituted Guanidinium Ions. J. Phys. Chem. 1990, 94 (10), 4015-4025.
    • (1990) J. Phys. Chem. , vol.94 , Issue.10 , pp. 4015-4025
    • Sension, R.J.1    Hudson, B.2    Callis, P.R.3
  • 39
    • 0037075409 scopus 로고    scopus 로고
    • Effects of vibrational frequency correlations on two-dimensional infrared spectra
    • Ge, N. H.; Zanni, M. T.; Hochstrasser, R. M. Effects of Vibrational Frequency Correlations on Two-Dimensional Infrared Spectra. J. Phys. Chem. A 2002, 106 (6), 962-972.
    • (2002) J. Phys. Chem. A , vol.106 , Issue.6 , pp. 962-972
    • Ge, N.H.1    Zanni, M.T.2    Hochstrasser, R.M.3
  • 41
    • 4043164722 scopus 로고    scopus 로고
    • Vibrational and rotational dynamics of cyanoferrates in solution
    • Sando, G. M.; Zhong, Q.; Owrutsky, J. C. Vibrational and Rotational Dynamics of Cyanoferrates in Solution. J. Chem Phys. 2004, 121 (5), 2158-2168.
    • (2004) J. Chem Phys. , vol.121 , Issue.5 , pp. 2158-2168
    • Sando, G.M.1    Zhong, Q.2    Owrutsky, J.C.3
  • 42
    • 36449002031 scopus 로고
    • Homogeneous vibrational dynamics and inhomogeneous broadening in glass-forming liquids-infrared photonecho experiments from room-temperature to 10 K
    • Tokmakoff, A.; Fayer, M. D. Homogeneous Vibrational Dynamics and Inhomogeneous Broadening in Glass-Forming Liquids-Infrared PhotonEcho Experiments from Room-Temperature to 10 K. J. Chem. Phys. 1995, 103 (8), 2810-2826.
    • (1995) J. Chem. Phys. , vol.103 , Issue.8 , pp. 2810-2826
    • Tokmakoff, A.1    Fayer, M.D.2
  • 43
    • 36449008351 scopus 로고
    • Vibrational spectral diffusion and population-dynamics in a glass-forming liquid-variable bandwidth picosecond infraredspectroscopy
    • Tokmakoff, A.; Urdahl, R. S.; Zimdars, D.; Francis, R. S.; Kwok, A. S.; Fayer, M. D. Vibrational Spectral Diffusion and Population-Dynamics in a Glass-Forming Liquid-Variable Bandwidth Picosecond InfraredSpectroscopy. J. Chem. Phys. 1995, 102 (10), 3919-3931.
    • (1995) J. Chem. Phys. , vol.102 , Issue.10 , pp. 3919-3931
    • Tokmakoff, A.1    Urdahl, R.S.2    Zimdars, D.3    Francis, R.S.4    Kwok, A.S.5    Fayer, M.D.6
  • 44
    • 17144453728 scopus 로고    scopus 로고
    • Vibrational coherence transfer characterized with fourier-transform 2D IR spectroscopy
    • Khalil, M.; Demirdoven, N.; Tokmakoff, A. Vibrational Coherence Transfer Characterized with Fourier-Transform 2D IR Spectroscopy. J. Chem. Phys. 2004, 121 (1), 362-373.
    • (2004) J. Chem. Phys. , vol.121 , Issue.1 , pp. 362-373
    • Khalil, M.1    Demirdoven, N.2    Tokmakoff, A.3
  • 45
    • 85022461682 scopus 로고
    • The theory of relaxation processes
    • Waugh, J. S., Ed.; Academic Press: New York
    • Redfield, A. G. The Theory of Relaxation Processes. In Advances in Magnetic Resonance; Waugh, J. S., Ed.; Academic Press: New York, 1965; Vol.1, pp 1-32.
    • (1965) Advances in Magnetic Resonance , vol.1 , pp. 1-32
    • Redfield, A.G.1
  • 46
    • 0035935381 scopus 로고    scopus 로고
    • Unusual vibrational dynamics of the acetic acid dimer
    • DOI 10.1063/1.1404144
    • (46) Lim, M.; Hochstrasser, R. M. Unusual Vibrational Dynamics of the Acetic Acid Dimer. J. Chem. Phys. 2001, 115 (16), 7629-7643. (Pubitemid 33047858)
    • (2001) Journal of Chemical Physics , vol.115 , Issue.16 , pp. 7629-7643
    • Lim, M.1    Hochstrasser, R.M.2
  • 47
    • 84906364290 scopus 로고
    • Studies on the aqueous-solutions of guanidinium salts 0.13. NMR-study of the interactions between guanidinium salt and tetraalkylammonium salts in water
    • Miyajima, K.; Yoshida, H.; Kuroda, Y.; Nakagaki, M. Studies on the Aqueous-Solutions of Guanidinium Salts 0.13. NMR-Study of the Interactions between Guanidinium Salt and Tetraalkylammonium Salts in Water. Bull. Chem. Soc. Jpn. 1980, 53 (8), 2212-2216.
    • (1980) Bull. Chem. Soc. Jpn. , vol.53 , Issue.8 , pp. 2212-2216
    • Miyajima, K.1    Yoshida, H.2    Kuroda, Y.3    Nakagaki, M.4
  • 49
    • 34047270526 scopus 로고
    • Femtosecond laser studies of the Cis-stilbene photoisomerization reactions
    • Sension, R. J.; Repinec, S. T.; Szarka, A. Z.; Hochstrasser, R. M. Femtosecond Laser Studies of the Cis-Stilbene Photoisomerization Reactions. J. Chem. Phys. 1993, 98 (8), 6291-6315.
    • (1993) J. Chem. Phys. , vol.98 , Issue.8 , pp. 6291-6315
    • Sension, R.J.1    Repinec, S.T.2    Szarka, A.Z.3    Hochstrasser, R.M.4
  • 50
    • 36749108527 scopus 로고
    • Rotational friction coefficients for spheroids with slipping boundary-condition
    • Hu, C. M.; Zwanzig, R. Rotational Friction Coefficients for Spheroids with Slipping Boundary-Condition. J. Chem. Phys. 1974, 60 (11), 4354-4357.
    • (1974) J. Chem. Phys. , vol.60 , Issue.11 , pp. 4354-4357
    • Hu, C.M.1    Zwanzig, R.2
  • 51
    • 45849084663 scopus 로고    scopus 로고
    • Urea and guanidinium chloride denature protein L in different ways in molecular dynamics simulations
    • Camilloni, C.; Rocco, A. G.; Eberini, I.; Gianazza, E.; Broglia, R. A.; Tiana, G. Urea and Guanidinium Chloride Denature Protein L in Different Ways in Molecular Dynamics Simulations. Biophys. J. 2008, 94 (12), 4654-4661.
    • (2008) Biophys. J. , vol.94 , Issue.12 , pp. 4654-4661
    • Camilloni, C.1    Rocco, A.G.2    Eberini, I.3    Gianazza, E.4    Broglia, R.A.5    Tiana, G.6
  • 52
    • 0010914883 scopus 로고
    • Molecular-dynamics simulation of a small calcium complex in aqueous-solution
    • Teleman, O.; Ahlstrom, P. Molecular-Dynamics Simulation of a Small Calcium Complex in Aqueous-Solution. J. Am. Chem. Soc. 1986, 108 (15), 4333-4341.
    • (1986) J. Am. Chem. Soc. , vol.108 , Issue.15 , pp. 4333-4341
    • Teleman, O.1    Ahlstrom, P.2
  • 53
    • 84946636446 scopus 로고
    • Spectroscopic and transport-properties of water model-calculations and the interpretation of experimental results
    • Impey, R. W.; Madden, P. A.; Mcdonald, I. R. Spectroscopic and Transport-Properties of Water Model-Calculations and the Interpretation of Experimental Results. Mol. Phys. 1982, 46 (3), 513-539.
    • (1982) Mol. Phys. , vol.46 , Issue.3 , pp. 513-539
    • Impey, R.W.1    Madden, P.A.2    Mcdonald, I.R.3
  • 54
    • 0028268952 scopus 로고
    • Molecular-dynamics simulations of oxidized and reduced clostridium-beijerinckii flavodoxin
    • Leenders, R.; Vangunsteren, W. F.; Berendsen, H. J. C.; Visser, A. J. W. G. Molecular-Dynamics Simulations of Oxidized and Reduced Clostridium- Beijerinckii Flavodoxin. Biophys. J. 1994, 66 (3), 634-645.
    • (1994) Biophys. J. , vol.66 , Issue.3 , pp. 634-645
    • Leenders, R.1    Vangunsteren, W.F.2    Berendsen, H.J.C.3    Visser, A.J.W.G.4


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