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Volumn 120, Issue 5, 2016, Pages 936-944

Utility of 5-Cyanotryptophan Fluorescence as a Sensitive Probe of Protein Hydration

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINARY MIXTURES; BINDING ENERGY; BINS; DIMETHYL SULFOXIDE; HYDRATION; PEPTIDES; PROTEINS;

EID: 84958568618     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b12233     Document Type: Article
Times cited : (47)

References (51)
  • 1
    • 33646918845 scopus 로고    scopus 로고
    • Probing Protein Folding and Conformational Transitions with Fluorescence
    • Royer, C. A. Probing Protein Folding and Conformational Transitions with Fluorescence Chem. Rev. 2006, 106, 1769-1784 10.1021/cr0404390
    • (2006) Chem. Rev. , vol.106 , pp. 1769-1784
    • Royer, C.A.1
  • 3
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of Tryptophan Fluorescence Shifts in Proteins
    • Vivian, J. T.; Callis, P. R. Mechanisms of Tryptophan Fluorescence Shifts in Proteins Biophys. J. 2001, 80, 2093-2109 10.1016/S0006-3495(01)76183-8
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 4
    • 0037133342 scopus 로고    scopus 로고
    • Biological Water at the Protein Surface: Dynamical Solvation Probed Directly with Femtosecond Resolution
    • Pal, S. K.; Peon, J.; Zewail, A. H. Biological Water at the Protein Surface: Dynamical Solvation Probed Directly with Femtosecond Resolution Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 1763-1768 10.1073/pnas.042697899
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1763-1768
    • Pal, S.K.1    Peon, J.2    Zewail, A.H.3
  • 5
    • 0032478116 scopus 로고    scopus 로고
    • Tryptophan Fluorescence Quenching by Methionine and Selenomethionine Residues of Calmodulin: Orientation of Peptide and Protein Binding
    • Yuan, T.; Weljie, A. M.; Vogel, H. J. Tryptophan Fluorescence Quenching by Methionine and Selenomethionine Residues of Calmodulin: Orientation of Peptide and Protein Binding Biochemistry 1998, 37, 3187-3195 10.1021/bi9716579
    • (1998) Biochemistry , vol.37 , pp. 3187-3195
    • Yuan, T.1    Weljie, A.M.2    Vogel, H.J.3
  • 6
    • 66049120630 scopus 로고    scopus 로고
    • Ultrafast Quenching of Tryptophan Fluorescence in Proteins: Interresidue and Intrahelical Electron Transfer
    • Qiu, W. H.; Li, T. P.; Zhang, L. Y.; Yang, Y.; Kao, Y. T.; Wang, L. J.; Zhong, D. P. Ultrafast Quenching of Tryptophan Fluorescence in Proteins: Interresidue and Intrahelical Electron Transfer Chem. Phys. 2008, 350, 154-164 10.1016/j.chemphys.2008.01.061
    • (2008) Chem. Phys. , vol.350 , pp. 154-164
    • Qiu, W.H.1    Li, T.P.2    Zhang, L.Y.3    Yang, Y.4    Kao, Y.T.5    Wang, L.J.6    Zhong, D.P.7
  • 7
    • 44049102957 scopus 로고    scopus 로고
    • Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence
    • Alston, R. W.; Lasagna, M.; Grimsley, G. R.; Scholtz, J. M.; Reinhart, G. D.; Pace, C. N. Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence Biophys. J. 2008, 94, 2280-2287 10.1529/biophysj.107.116921
    • (2008) Biophys. J. , vol.94 , pp. 2280-2287
    • Alston, R.W.1    Lasagna, M.2    Grimsley, G.R.3    Scholtz, J.M.4    Reinhart, G.D.5    Pace, C.N.6
  • 8
    • 0015230409 scopus 로고
    • Solute Perturbation of Protein Fluorescence. Quenching of the Tryptophyl Fluorescence of Model Compounds and of Lysozyme by Iodide Ion
    • Lehrer, S. Solute Perturbation of Protein Fluorescence. Quenching of the Tryptophyl Fluorescence of Model Compounds and of Lysozyme by Iodide Ion Biochemistry 1971, 10, 3254-3263 10.1021/bi00793a015
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.1
  • 9
    • 0019593952 scopus 로고
    • Fluorescence Quenching Studies with Proteins
    • Eftink, M. R.; Ghiron, C. A. Fluorescence Quenching Studies with Proteins Anal. Biochem. 1981, 114, 199-227 10.1016/0003-2697(81)90474-7
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 10
    • 0344734168 scopus 로고    scopus 로고
    • Time-Resolved and Steady-State Fluorescence Quenching of N-Acetyl-L-Tryptophanamide by Acrylamide and Iodide
    • Zelent, B.; Kuśba, J.; Gryczynski, I.; Johnson, M. L.; Lakowicz, J. R. Time-Resolved and Steady-State Fluorescence Quenching of N-Acetyl-L-Tryptophanamide by Acrylamide and Iodide Biophys. Chem. 1998, 73, 53-75 10.1016/S0301-4622(98)00137-9
    • (1998) Biophys. Chem. , vol.73 , pp. 53-75
    • Zelent, B.1    Kuśba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 11
    • 65249138942 scopus 로고    scopus 로고
    • Solvent Effects on the Fluorescence Quenching of Tryptophan by Amides Via Electron Transfer. Experimental and Computational Studies
    • Muiño, P. L.; Callis, P. R. Solvent Effects on the Fluorescence Quenching of Tryptophan by Amides Via Electron Transfer. Experimental and Computational Studies J. Phys. Chem. B 2009, 113, 2572-2577 10.1021/jp711513b
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2572-2577
    • Muiño, P.L.1    Callis, P.R.2
  • 12
    • 33749599714 scopus 로고    scopus 로고
    • Femtosecond Studies of Tryptophan Fluorescence Dynamics in Proteins: Local Solvation and Electronic Quenching
    • Zhang, L.; Kao, Y.-T.; Qiu, W.; Wang, L.; Zhong, D. Femtosecond Studies of Tryptophan Fluorescence Dynamics in Proteins: Local Solvation and Electronic Quenching J. Phys. Chem. B 2006, 110, 18097-18103 10.1021/jp063025e
    • (2006) J. Phys. Chem. B , vol.110 , pp. 18097-18103
    • Zhang, L.1    Kao, Y.-T.2    Qiu, W.3    Wang, L.4    Zhong, D.5
  • 13
    • 84945799762 scopus 로고
    • Fluorescence Quantum Yields of Tryptophan and Tyrosine
    • Chen, R. F. Fluorescence Quantum Yields of Tryptophan and Tyrosine Anal. Lett. 1967, 1, 35-42 10.1080/00032716708051097
    • (1967) Anal. Lett. , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 14
    • 0020763601 scopus 로고
    • On the Origin of Nonexponential Fluorescence Decay in Tryptophan and Its Derivatives
    • Petrich, J. W.; Chang, M. C.; McDonald, D. B.; Fleming, G. R. On the Origin of Nonexponential Fluorescence Decay in Tryptophan and Its Derivatives J. Am. Chem. Soc. 1983, 105, 3824-3832 10.1021/ja00350a014
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 15
    • 0000810656 scopus 로고
    • The Tryptophan Fluorescence Lifetime Puzzle. A Study of Decay Times in Aqueous Solution as a Function of pH and Buffer Composition
    • Gudgin, E.; Lopez-Delgado, R.; Ware, W. R. The Tryptophan Fluorescence Lifetime Puzzle. A Study of Decay Times in Aqueous Solution as a Function of pH and Buffer Composition Can. J. Chem. 1981, 59, 1037-1044 10.1139/v81-154
    • (1981) Can. J. Chem. , vol.59 , pp. 1037-1044
    • Gudgin, E.1    Lopez-Delgado, R.2    Ware, W.R.3
  • 16
    • 0029904741 scopus 로고    scopus 로고
    • The Peptide Bond Quenches Indole Fluorescence
    • Chen, Y.; Liu, B.; Yu, H. T.; Barkley, M. D. The Peptide Bond Quenches Indole Fluorescence J. Am. Chem. Soc. 1996, 118, 9271-9278 10.1021/ja961307u
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9271-9278
    • Chen, Y.1    Liu, B.2    Yu, H.T.3    Barkley, M.D.4
  • 18
    • 0030010286 scopus 로고    scopus 로고
    • Characterization of the Fluorescence Emission Properties of 7-Azatryptophan in Reverse Micellar Environments
    • Guharay, J.; Sengupta, P. K. Characterization of the Fluorescence Emission Properties of 7-Azatryptophan in Reverse Micellar Environments Biochem. Biophys. Res. Commun. 1996, 219, 388-392 10.1006/bbrc.1996.0243
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 388-392
    • Guharay, J.1    Sengupta, P.K.2
  • 19
    • 0030896834 scopus 로고    scopus 로고
    • Biosynthetic Incorporation of Tryptophan Analogues into Staphylococcal Nuclease: Effect of 5-Hydroxytryptophan and 7-Azatryptophan on Structure and Stability
    • Wong, C.-Y.; Eftink, M. R. Biosynthetic Incorporation of Tryptophan Analogues into Staphylococcal Nuclease: Effect of 5-Hydroxytryptophan and 7-Azatryptophan on Structure and Stability Protein Sci. 1997, 6, 689-697 10.1002/pro.5560060318
    • (1997) Protein Sci. , vol.6 , pp. 689-697
    • Wong, C.-Y.1    Eftink, M.R.2
  • 20
    • 0347129833 scopus 로고    scopus 로고
    • In Vivo Synthesized Proteins with Monoexponential Fluorescence Decay Kinetics
    • Broos, J.; Maddalena, F.; Hesp, B. H. In Vivo Synthesized Proteins with Monoexponential Fluorescence Decay Kinetics J. Am. Chem. Soc. 2004, 126, 22-23 10.1021/ja0385585
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 22-23
    • Broos, J.1    Maddalena, F.2    Hesp, B.H.3
  • 21
    • 84925070975 scopus 로고    scopus 로고
    • Picosecond Fluorescence Dynamics of Tryptophan and 5-Fluorotryptophan in Monellin: Slow Water-Protein Relaxation Unmasked
    • Xu, J. H.; Chen, B. B.; Callis, P.; Muino, P. L.; Rozeboom, H.; Broos, J.; Toptygin, D.; Brand, L.; Knutson, J. R. Picosecond Fluorescence Dynamics of Tryptophan and 5-Fluorotryptophan in Monellin: Slow Water-Protein Relaxation Unmasked J. Phys. Chem. B 2015, 119, 4230-4239 10.1021/acs.jpcb.5b01651
    • (2015) J. Phys. Chem. B , vol.119 , pp. 4230-4239
    • Xu, J.H.1    Chen, B.B.2    Callis, P.3    Muino, P.L.4    Rozeboom, H.5    Broos, J.6    Toptygin, D.7    Brand, L.8    Knutson, J.R.9
  • 23
    • 84925047401 scopus 로고    scopus 로고
    • Beta-(1-Azulenyl)-L-Alanine - a Functional Probe for Determination of Pka of Histidine Residues
    • Gosavi, P. M.; Moroz, Y. S.; Korendovych, I. V. Beta-(1-Azulenyl)-L-Alanine-a Functional Probe for Determination of Pka of Histidine Residues Chem. Commun. 2015, 51, 5347-5350 10.1039/C4CC08720H
    • (2015) Chem. Commun. , vol.51 , pp. 5347-5350
    • Gosavi, P.M.1    Moroz, Y.S.2    Korendovych, I.V.3
  • 24
    • 33748630492 scopus 로고    scopus 로고
    • Fluorescence Properties of Electropolymerised 5-Substituted Indoles in Solution
    • Jennings, P.; Jones, A. C.; Mount, A. R. Fluorescence Properties of Electropolymerised 5-Substituted Indoles in Solution J. Chem. Soc., Faraday Trans. 1998, 94, 3619-3624 10.1039/a806721j
    • (1998) J. Chem. Soc., Faraday Trans. , vol.94 , pp. 3619-3624
    • Jennings, P.1    Jones, A.C.2    Mount, A.R.3
  • 25
    • 68049083816 scopus 로고    scopus 로고
    • Substituent Effects on Xenon Binding Affinity and Solution Behavior of Water-Soluble Cryptophanes
    • Hill, P. A.; Wei, Q.; Troxler, T.; Dmochowski, I. J. Substituent Effects on Xenon Binding Affinity and Solution Behavior of Water-Soluble Cryptophanes J. Am. Chem. Soc. 2009, 131, 3069-3077 10.1021/ja8100566
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3069-3077
    • Hill, P.A.1    Wei, Q.2    Troxler, T.3    Dmochowski, I.J.4
  • 26
    • 84863675790 scopus 로고    scopus 로고
    • The Structure of 5-Cyanoindole in the Ground and the Lowest Electronically Excited Singlet States, Deduced from Rotationally Resolved Electronic Spectroscopy and Ab Initio Theory
    • Oeltermann, O.; Brand, C.; Engels, B.; Tatchen, J.; Schmitt, M. The Structure of 5-Cyanoindole in the Ground and the Lowest Electronically Excited Singlet States, Deduced from Rotationally Resolved Electronic Spectroscopy and Ab Initio Theory Phys. Chem. Chem. Phys. 2012, 14, 10266-10270 10.1039/c2cp41094j
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 10266-10270
    • Oeltermann, O.1    Brand, C.2    Engels, B.3    Tatchen, J.4    Schmitt, M.5
  • 27
    • 33947295202 scopus 로고
    • Influence of Solvent and Temperature Upon the Fluorescence of Indole Derivatives
    • Kirby, E. P.; Steiner, R. F. Influence of Solvent and Temperature Upon the Fluorescence of Indole Derivatives J. Phys. Chem. 1970, 74, 4480-4490 10.1021/j100720a004
    • (1970) J. Phys. Chem. , vol.74 , pp. 4480-4490
    • Kirby, E.P.1    Steiner, R.F.2
  • 28
    • 33751158095 scopus 로고
    • Single-Exponential Fluorescence Decay of the Nonnatural Amino Acid 7-Azatryptophan and the Nonexponential Fluorescence Decay of Tryptophan in Water
    • Chen, Y.; Gai, F.; Petrich, J. W. Single-Exponential Fluorescence Decay of the Nonnatural Amino Acid 7-Azatryptophan and the Nonexponential Fluorescence Decay of Tryptophan in Water J. Phys. Chem. 1994, 98, 2203-2209 10.1021/j100059a039
    • (1994) J. Phys. Chem. , vol.98 , pp. 2203-2209
    • Chen, Y.1    Gai, F.2    Petrich, J.W.3
  • 29
    • 68949105971 scopus 로고    scopus 로고
    • 5-Cyanotryptophan as an Infrared Probe of Local Hydration Status of Proteins
    • Waegele, M. M.; Tucker, M. J.; Gai, F. 5-Cyanotryptophan as an Infrared Probe of Local Hydration Status of Proteins Chem. Phys. Lett. 2009, 478, 249-253 10.1016/j.cplett.2009.07.058
    • (2009) Chem. Phys. Lett. , vol.478 , pp. 249-253
    • Waegele, M.M.1    Tucker, M.J.2    Gai, F.3
  • 30
    • 0001706944 scopus 로고
    • Trifluoroethanol Quenches Indole Fluorescence by Excited-State Proton Transfer
    • Chen, Y.; Liu, B.; Barkley, M. D. Trifluoroethanol Quenches Indole Fluorescence by Excited-State Proton Transfer J. Am. Chem. Soc. 1995, 117, 5608-5609 10.1021/ja00125a032
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5608-5609
    • Chen, Y.1    Liu, B.2    Barkley, M.D.3
  • 31
    • 0026476548 scopus 로고
    • Fluorescence Quenching in Indoles by Excited-State Proton Transfer
    • Yu, H. T.; Colucci, W. J.; McLaughlin, M. L.; Barkley, M. D. Fluorescence Quenching in Indoles by Excited-State Proton Transfer J. Am. Chem. Soc. 1992, 114, 8449-8454 10.1021/ja00048a015
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8449-8454
    • Yu, H.T.1    Colucci, W.J.2    McLaughlin, M.L.3    Barkley, M.D.4
  • 32
    • 84969354944 scopus 로고    scopus 로고
    • C≡N Stretching Vibration of 5-Cyanotryptophan as an Infrared Probe of Protein Local Environment: What Determines Its Frequency?
    • Zhang, W.; Markiewicz, B. N.; Doerksen, R. S.; Smith, III, A. B.; Gai, F. C≡N Stretching Vibration of 5-Cyanotryptophan as an Infrared Probe of Protein Local Environment: What Determines Its Frequency? Phys. Chem. Chem. Phys. 2015, DOI: 10.1039/C1035CP04413H.
    • (2015) Phys. Chem. Chem. Phys.
    • Zhang, W.1    Markiewicz, B.N.2    Doerksen, R.S.3    Smith, A.B.4    Gai, F.5
  • 34
    • 69149100640 scopus 로고    scopus 로고
    • Solvation in Protein (Un)Folding of Melittin Tetramer-Monomer Transition
    • Othon, C. M.; Kwon, O.-H.; Lin, M. M.; Zewail, A. H. Solvation in Protein (Un)Folding of Melittin Tetramer-Monomer Transition Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 12593-12598 10.1073/pnas.0905967106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 12593-12598
    • Othon, C.M.1    Kwon, O.-H.2    Lin, M.M.3    Zewail, A.H.4
  • 35
    • 84929359609 scopus 로고    scopus 로고
    • Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins
    • Johnston, A. J.; Zhang, Y.; Busch, S.; Pardo, L. C.; Imberti, S.; McLain, S. E. Amphipathic Solvation of Indole: Implications for the Role of Tryptophan in Membrane Proteins J. Phys. Chem. B 2015, 119, 5979-5987 10.1021/acs.jpcb.5b02476
    • (2015) J. Phys. Chem. B , vol.119 , pp. 5979-5987
    • Johnston, A.J.1    Zhang, Y.2    Busch, S.3    Pardo, L.C.4    Imberti, S.5    McLain, S.E.6
  • 36
    • 3142562502 scopus 로고    scopus 로고
    • The Ground and Singlet Excited-State Hydrogen-Bonding Interactions of N-Methylindole with Trifluoroethanol in N-Hexane: A Model to Explain the Anomalous Fluorescence of Indole in Polar Protic Solvents
    • Muñoz, M. a. A.; Carmona, C.; Balón, M. The Ground and Singlet Excited-State Hydrogen-Bonding Interactions of N-Methylindole with Trifluoroethanol in N-Hexane: A Model to Explain the Anomalous Fluorescence of Indole in Polar Protic Solvents Chem. Phys. Lett. 2004, 393, 217-221 10.1016/j.cplett.2004.06.033
    • (2004) Chem. Phys. Lett. , vol.393 , pp. 217-221
    • Muñoz, M.A.A.1    Carmona, C.2    Balón, M.3
  • 37
    • 0035899738 scopus 로고    scopus 로고
    • Determination of the Potential of Mean Force of Aromatic Amino Acid Complexes in Various Solvents Using Molecular Dynamics Simulations: the Case of the Tryptophan-Histidine Pair
    • Gervasio, F. L.; Chelli, R.; Marchi, M.; Procacci, P.; Schettino, V. Determination of the Potential of Mean Force of Aromatic Amino Acid Complexes in Various Solvents Using Molecular Dynamics Simulations: The Case of the Tryptophan-Histidine Pair J. Phys. Chem. B 2001, 105, 7835-7846 10.1021/jp010434w
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7835-7846
    • Gervasio, F.L.1    Chelli, R.2    Marchi, M.3    Procacci, P.4    Schettino, V.5
  • 38
    • 84894566908 scopus 로고    scopus 로고
    • Origin of Tryptophan Fluorescence Lifetimes Part 1. Fluorescence Lifetimes Origin of Tryptophan Free in Solution
    • Albani, J. R. Origin of Tryptophan Fluorescence Lifetimes Part 1. Fluorescence Lifetimes Origin of Tryptophan Free in Solution J. Fluoresc. 2014, 24, 93-104 10.1007/s10895-013-1277-8
    • (2014) J. Fluoresc. , vol.24 , pp. 93-104
    • Albani, J.R.1
  • 39
    • 84887554711 scopus 로고    scopus 로고
    • Solvation Dynamics of Tryptophan in Water-Dimethyl Sulfoxide Binary Mixture: in Search of Molecular Origin of Composition Dependent Multiple Anomalies
    • Roy, S.; Bagchi, B. Solvation Dynamics of Tryptophan in Water-Dimethyl Sulfoxide Binary Mixture: In Search of Molecular Origin of Composition Dependent Multiple Anomalies J. Chem. Phys. 2013, 139, 034308 10.1063/1.4813417
    • (2013) J. Chem. Phys. , vol.139 , pp. 034308
    • Roy, S.1    Bagchi, B.2
  • 40
    • 84859256621 scopus 로고    scopus 로고
    • Hydrogen Bonding in Mixtures of Dimethyl Sulfoxide and Cosolvents
    • Kiefer, J.; Noack, K.; Kirchner, B. Hydrogen Bonding in Mixtures of Dimethyl Sulfoxide and Cosolvents Curr. Phys. Chem. 2011, 1, 340-351 10.2174/1877946811101040340
    • (2011) Curr. Phys. Chem. , vol.1 , pp. 340-351
    • Kiefer, J.1    Noack, K.2    Kirchner, B.3
  • 41
    • 0001479101 scopus 로고
    • Dielectric Spectrum of Dimethyl Sulfoxide/Water Mixtures as a Function of Composition
    • Kaatze, U.; Pottel, R.; Schäfer, M. Dielectric Spectrum of Dimethyl Sulfoxide/Water Mixtures as a Function of Composition J. Phys. Chem. 1989, 93, 5623-5627 10.1021/j100351a057
    • (1989) J. Phys. Chem. , vol.93 , pp. 5623-5627
    • Kaatze, U.1    Pottel, R.2    Schäfer, M.3
  • 42
    • 74249115771 scopus 로고    scopus 로고
    • Effects of Co-Solvents on Peptide Hydration Water Structure and Dynamics
    • Johnson, M. E.; Malardier-Jugroot, C.; Head-Gordon, T. Effects of Co-Solvents on Peptide Hydration Water Structure and Dynamics Phys. Chem. Chem. Phys. 2010, 12, 393-405 10.1039/B915888J
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 393-405
    • Johnson, M.E.1    Malardier-Jugroot, C.2    Head-Gordon, T.3
  • 43
    • 35748974824 scopus 로고    scopus 로고
    • Protein Precipitation and Denaturation by Dimethyl Sulfoxide
    • Arakawa, T.; Kita, Y.; Timasheff, S. N. Protein Precipitation and Denaturation by Dimethyl Sulfoxide Biophys. Chem. 2007, 131, 62-70 10.1016/j.bpc.2007.09.004
    • (2007) Biophys. Chem. , vol.131 , pp. 62-70
    • Arakawa, T.1    Kita, Y.2    Timasheff, S.N.3
  • 44
    • 84859238646 scopus 로고    scopus 로고
    • Dimethyl Sulfoxide Induced Structural Transformations and Non-Monotonic Concentration Dependence of Conformational Fluctuation around Active Site of Lysozyme
    • Roy, S.; Jana, B.; Bagchi, B. Dimethyl Sulfoxide Induced Structural Transformations and Non-Monotonic Concentration Dependence of Conformational Fluctuation around Active Site of Lysozyme J. Chem. Phys. 2012, 136, 115103 10.1063/1.3694268
    • (2012) J. Chem. Phys. , vol.136 , pp. 115103
    • Roy, S.1    Jana, B.2    Bagchi, B.3
  • 45
    • 39149144878 scopus 로고    scopus 로고
    • b Bands of Trp Resolve Position-Specific Features in Tear Lipocalin
    • b Bands of Trp Resolve Position-Specific Features in Tear Lipocalin Anal. Biochem. 2008, 374, 386-395 10.1016/j.ab.2007.11.002
    • (2008) Anal. Biochem. , vol.374 , pp. 386-395
    • Gasymov, O.K.1    Abduragimov, A.R.2    Glasgow, B.J.3
  • 46
    • 77649302590 scopus 로고    scopus 로고
    • Dielectric Relaxation in Dimethyl Sulfoxide/Water Mixtures Studied by Microwave Dielectric Relaxation Spectroscopy
    • Lu, Z.; Manias, E.; Macdonald, D. D.; Lanagan, M. Dielectric Relaxation in Dimethyl Sulfoxide/Water Mixtures Studied by Microwave Dielectric Relaxation Spectroscopy J. Phys. Chem. A 2009, 113, 12207-12214 10.1021/jp9059246
    • (2009) J. Phys. Chem. A , vol.113 , pp. 12207-12214
    • Lu, Z.1    Manias, E.2    Macdonald, D.D.3    Lanagan, M.4
  • 48
    • 15944403901 scopus 로고    scopus 로고
    • Conformational Distribution of a 14-Residue Peptide in Solution: A Fluorescence Resonance Energy Transfer Study
    • Tucker, M. J.; Oyola, R.; Gai, F. Conformational Distribution of a 14-Residue Peptide in Solution: A Fluorescence Resonance Energy Transfer Study J. Phys. Chem. B 2005, 109, 4788-4795 10.1021/jp044347q
    • (2005) J. Phys. Chem. B , vol.109 , pp. 4788-4795
    • Tucker, M.J.1    Oyola, R.2    Gai, F.3
  • 49
    • 33644880010 scopus 로고    scopus 로고
    • Ultrafast Folding of a Computationally Designed Trp-Cage Mutant: Trp(2)-Cage
    • Bunagan, M. R.; Yang, X.; Saven, J. G.; Gai, F. Ultrafast Folding of a Computationally Designed Trp-Cage Mutant: Trp(2)-Cage J. Phys. Chem. B 2006, 110, 3759-3763 10.1021/jp055288z
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3759-3763
    • Bunagan, M.R.1    Yang, X.2    Saven, J.G.3    Gai, F.4
  • 51
    • 84926459121 scopus 로고    scopus 로고
    • Site-Specific Infrared Probes of Proteins
    • Ma, J.; Pazos, I. M.; Zhang, W.; Culik, R. M.; Gai, F. Site-Specific Infrared Probes of Proteins Annu. Rev. Phys. Chem. 2015, 66, 357-377 10.1146/annurev-physchem-040214-121802
    • (2015) Annu. Rev. Phys. Chem. , vol.66 , pp. 357-377
    • Ma, J.1    Pazos, I.M.2    Zhang, W.3    Culik, R.M.4    Gai, F.5


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