메뉴 건너뛰기




Volumn 50, Issue 25, 2011, Pages 5799-5805

Influence of histidine tag attachment on picosecond protein dynamics

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY TAGS; ELECTROSTATIC ENVIRONMENTS; FOURIER TRANSFORM INFRARED SPECTRA; GLOBULAR PROTEINS; HEME POCKETS; HIS-TAG; INFRARED VIBRATIONAL ECHO SPECTROSCOPY; PICOSECONDS; POLYHISTIDINE; PROTEIN DYNAMICS; PROTEIN FUNCTIONS; PROTEIN MOTION; PROTEIN STRUCTURES; SHORT TIME SCALE; TIME-SCALES;

EID: 79959429158     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2003923     Document Type: Article
Times cited : (42)

References (68)
  • 1
    • 0026910385 scopus 로고
    • Immobilized metal ion affinity chromatography
    • Porath, J. (1992) Immobilized metal ion affinity chromatography Protein Expression Purif. 3, 263-281
    • (1992) Protein Expression Purif. , vol.3 , pp. 263-281
    • Porath, J.1
  • 2
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. (2003) Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems Appl. Microbiol. Biotechnol. 60, 523-533 (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 4
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins
    • Smith, M. C., Furman, T. C., Ingolia, T. D., and Pidgeon, C. (1988) Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins J. Biol. Chem. 263, 7211-7215
    • (1988) J. Biol. Chem. , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Furman, T.C.2    Ingolia, T.D.3    Pidgeon, C.4
  • 5
    • 0033117468 scopus 로고    scopus 로고
    • Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases
    • DOI 10.1006/prep.1999.1038
    • Pedersen, J., Lauritzen, C., Madsen, M. T., and Weis Dahl, S. (1999) Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases Protein Expression Purif. 15, 389-400 (Pubitemid 29326387)
    • (1999) Protein Expression and Purification , vol.15 , Issue.3 , pp. 389-400
    • Pedersen, J.1    Lauritzen, C.2    Madsen, M.T.3    Weis Dahl, S.4
  • 6
    • 0141539517 scopus 로고    scopus 로고
    • A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa
    • DOI 10.1016/S1046-5928(03)00168-2
    • Jenny, R. J., Mann, K. G., and Lundblad, R. L. (2003) A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa Protein Expression Purif. 31, 1-11 (Pubitemid 37207638)
    • (2003) Protein Expression and Purification , vol.31 , Issue.1 , pp. 1-11
    • Jenny, R.J.1    Mann, K.G.2    Lundblad, R.L.3
  • 7
    • 74549196928 scopus 로고    scopus 로고
    • Current strategies for polypeptide fusion tags removal
    • Hao, X., Cheng, Y., and Li-E, C. (2009) Current strategies for polypeptide fusion tags removal Prog. Biochem. Biophys. 36, 1364-1669
    • (2009) Prog. Biochem. Biophys. , vol.36 , pp. 1364-1669
    • Hao, X.1    Cheng, Y.2    Li-E, C.3
  • 8
    • 0037044317 scopus 로고    scopus 로고
    • Structure-based kinetic modeling of excited-state transfer and trapping in histidine-tagged photosystem II core complexes from Synechocystis
    • Vassiliev, S., Lee, C.-I., Brudvig, G. W., and Bruce, D. (2002) Structure-based kinetic modeling of excited-state transfer and trapping in histidine-tagged photosystem II core complexes from Synechocystis Biochemistry 41, 12236-12243
    • (2002) Biochemistry , vol.41 , pp. 12236-12243
    • Vassiliev, S.1    Lee, C.-I.2    Brudvig, G.W.3    Bruce, D.4
  • 9
    • 44949168516 scopus 로고    scopus 로고
    • Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis
    • Yao, L., Vogeli, B., Torchia, D. A., and Bax, A. (2008) Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis J. Phys. Chem. B 112, 6045-6056
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6045-6056
    • Yao, L.1    Vogeli, B.2    Torchia, D.A.3    Bax, A.4
  • 11
    • 33746349251 scopus 로고    scopus 로고
    • Spectroscopic study of substrate binding to the carbonmonoxy form of dehaloperoxidase from amphitrite ornata
    • DOI 10.1021/jp060278z
    • Nienhaus, K., Deng, P., Belyea, J., Franzen, S., and Nienhaus, G. U. (2006) Spectroscopic study of substrate binding to the carbonmonoxy form of dehaloperoxidase from Amphitrite ornata J. Phys. Chem. B 110, 13264-13276 (Pubitemid 44115665)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.26 , pp. 13264-13276
    • Nienhaus, K.1    Deng, P.2    Belyea, J.3    Franzen, S.4    Nienhaus, G.U.5
  • 14
    • 44949196798 scopus 로고    scopus 로고
    • Protein structure modeling indicates hexahistidine-tag interference with enzyme activity
    • DOI 10.1002/prot.21905
    • Freydank, A. C., Brandt, W., and Dräger, B. (2008) Protein structure modeling indicates hexahistidine-tag interference with enzyme activity Proteins: Struct., Funct., Bioinf. 72, 173-183 (Pubitemid 351809156)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 173-183
    • Freydank, A.-C.1    Brandt, W.2    Drager, B.3
  • 15
    • 33847714692 scopus 로고    scopus 로고
    • Cautionary tail: The presence of an N-terminal tag on dynein light-chain roadblock/LC7 affects its interaction with a functional partner
    • DOI 10.2174/092986607780090801
    • Song, J. and Markley, J. L. (2007) Cautionary tail: The presence of an N-terminal tag on dynein light-chain roadblock/lc7 affects its interaction with a functional partner Protein Pept. Lett. 14, 265-268 (Pubitemid 46376858)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.3 , pp. 265-268
    • Song, J.1    Markley, J.L.2
  • 16
    • 79958133183 scopus 로고    scopus 로고
    • Molecular modeling and dynamics simulation of a histidine-tagged cytochrome
    • Lin, Y. W., Ying, T. L., and Liao, L. F. (2011) Molecular modeling and dynamics simulation of a histidine-tagged cytochrome J. Mol. Model. 17, 971-978
    • (2011) J. Mol. Model. , vol.17 , pp. 971-978
    • Lin, Y.W.1    Ying, T.L.2    Liao, L.F.3
  • 17
    • 4344563213 scopus 로고    scopus 로고
    • Hexa-histidin tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a
    • DOI 10.1110/ps.04835904
    • Klose, J., Wendt, N., Kubald, S., Krause, E., Fechner, K., Beyermann, M., Bienert, M., Rudolph, R., and Rothemund, S. (2004) Hexa-histidine tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a Protein Sci. 13, 2470-2475 (Pubitemid 39128867)
    • (2004) Protein Science , vol.13 , Issue.9 , pp. 2470-2475
    • Klose, J.1    Wendt, N.2    Kubald, S.3    Krause, E.4    Fechner, K.5    Beyermann, M.6    Bienert, M.7    Rudolph, R.8    Rothemund, S.9
  • 18
    • 74749103579 scopus 로고    scopus 로고
    • Effects of histidine-tag on recombinant human cytochrome p450 3a5 catalytic activity in reconstitution systems
    • Emoto, C., Murayama, N., Wakiya, S., and Yamazaki, H. (2009) Effects of histidine-tag on recombinant human cytochrome p450 3a5 catalytic activity in reconstitution systems Drug Metab. Lett. 3, 207-211
    • (2009) Drug Metab. Lett. , vol.3 , pp. 207-211
    • Emoto, C.1    Murayama, N.2    Wakiya, S.3    Yamazaki, H.4
  • 19
    • 11844272620 scopus 로고    scopus 로고
    • Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site
    • DOI 10.1016/j.pep.2004.10.017, PII S1046592804003547
    • Chant, A., Kraemer-Pecore, C. M., Watkin, R., and Kneale, G. G. (2005) Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein area causes a conformational change at the DNA-binding site Protein Expression Purif. 39, 152-159 (Pubitemid 40084600)
    • (2005) Protein Expression and Purification , vol.39 , Issue.2 , pp. 152-159
    • Chant, A.1    Kraemer-Pecore, C.M.2    Watkin, R.3    Kneale, G.G.4
  • 20
    • 0034283337 scopus 로고    scopus 로고
    • Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain fv construct
    • Goel, A., Colcher, D., Koo, J.-S., Booth, B. J. M., Pavlinkova, G., and Batra, S. K. (2000) Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain fv construct Biochim. Biophys. Acta 1523, 13-20
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 13-20
    • Goel, A.1    Colcher, D.2    Koo, J.-S.3    Booth, B.J.M.4    Pavlinkova, G.5    Batra, S.K.6
  • 21
    • 0035007293 scopus 로고    scopus 로고
    • Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase
    • DOI 10.1107/S0907444901002918
    • Kim, K. M., Yi, E. C., Baker, D., and Zhang, K. Y. J. (2001) Post-translational modification of the N-terminal his tag interferes with the crystallization of the wild-type and mutant sh3 domains from chicken src tyrosine kinase Acta Crystallogr. D57, 759-762 (Pubitemid 32418124)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.5 , pp. 759-762
    • Kim, K.M.1    Yi, E.C.2    Baker, D.3    Zhang, K.Y.J.4
  • 23
    • 70450284404 scopus 로고    scopus 로고
    • Interactions between eb1 and microtubules: Dramatic effect of affinity tags and evidence for cooperative behavior
    • Zhu, Z. C., Gupta, K. K., Slabbekoorn, A. R., Paulson, B. A., Folker, E. S., and Goodson, H. V. (2009) Interactions between eb1 and microtubules: Dramatic effect of affinity tags and evidence for cooperative behavior J. Biol. Chem. 284, 32651-32661
    • (2009) J. Biol. Chem. , vol.284 , pp. 32651-32661
    • Zhu, Z.C.1    Gupta, K.K.2    Slabbekoorn, A.R.3    Paulson, B.A.4    Folker, E.S.5    Goodson, H.V.6
  • 24
    • 0014226042 scopus 로고
    • An Infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls
    • Alben, J. O. and Caughy, W. S. (1968) An Infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls Biochemistry 7, 175-183
    • (1968) Biochemistry , vol.7 , pp. 175-183
    • Alben, J.O.1    Caughy, W.S.2
  • 25
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T. S., Quillin, M. L., Phillips, G. N., Jr., and Olson, J. S. (1994) Structural determinants of the stretching frequency of CO bound to myoglobin Biochemistry 33, 1433-1446 (Pubitemid 24093691)
    • (1994) Biochemistry , vol.33 , Issue.6 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 26
    • 0001257322 scopus 로고    scopus 로고
    • Vibrational stark spectroscopy in proteins: A probe and calibration for electrostatic fields
    • Park, E., Andrews, S., and Boxer, S. G. (1999) Vibrational stark spectroscopy in proteins: A probe and calibration for electrostatic fields J. Phys. Chem. B 103, 9813-9817 (Pubitemid 129614020)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.45 , pp. 9813-9817
    • Park, E.S.1    Andrews, S.S.2    Hu, R.B.3    Boxer, S.G.4
  • 27
    • 0000348848 scopus 로고    scopus 로고
    • Bound CO Is a Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin
    • Phillips, G. N., Jr., Teodoro, M. N., Li, T., Smith, B., and Olson, J. S. (1999) Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin J. Phys. Chem. B 103, 8817-8829 (Pubitemid 129613930)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.42 , pp. 8817-8829
    • Phillips Jr., G.N.1    Teodora, M.L.2    Li, T.3    Smith, B.4    Olson, J.S.5
  • 28
    • 10444269414 scopus 로고    scopus 로고
    • CO as a vibrational probe of heme protein active sites
    • DOI 10.1016/j.jinorgbio.2004.09.026, PII S0162013404002934, Heme-Diatomic Interactions, Part 1
    • Spiro, T. G. and Wasbotten, I. H. (2005) CO as a vibrational probe of heme protein active sites J. Inorg. Biochem. 99, 34-44 (Pubitemid 39642970)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 34-44
    • Spiro, T.G.1    Wasbotten, I.H.2
  • 30
    • 0037426830 scopus 로고    scopus 로고
    • Structural assignments and dynamics of the A substates of MbCO: Spectrally resolved vibrational echo experiments and molecular dynamics simulations
    • Merchant, K. A., Noid, W. G., Thompson, D. E., Akiyama, R., Loring, R. F., and Fayer, M. D. (2003) Structural assignments and dynamics of the A substates of MbCO: Spectrally resolved vibrational echo experiments and molecular dynamics simulations J. Phys. Chem. B 107, 4-7
    • (2003) J. Phys. Chem. B , vol.107 , pp. 4-7
    • Merchant, K.A.1    Noid, W.G.2    Thompson, D.E.3    Akiyama, R.4    Loring, R.F.5    Fayer, M.D.6
  • 31
    • 78650592402 scopus 로고    scopus 로고
    • Dynamics of a myoglobin mutant enzyme: 2D-IR vibrational echo experiments and simulations
    • Bagchi, S., Nebgen, B. T., Loring, R. F., and Fayer, M. D. (2010) Dynamics of a myoglobin mutant enzyme: 2D-IR vibrational echo experiments and simulations J. Am. Chem. Soc. 132, 18367-18376
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18367-18376
    • Bagchi, S.1    Nebgen, B.T.2    Loring, R.F.3    Fayer, M.D.4
  • 32
    • 0036105752 scopus 로고    scopus 로고
    • Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations
    • Merchant, K. A., Thompson, D. E., Xu, Q.-H., Williams, R. B., Loring, R. F., and Fayer, M. D. (2002) Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations Biophys. J. 82, 3277-3288 (Pubitemid 34547671)
    • (2002) Biophysical Journal , vol.82 , Issue.6 , pp. 3277-3288
    • Merchant, K.A.1    Thompson, D.E.2    Xu, Q.-H.3    Williams, R.B.4    Loring, R.F.5    Fayer, M.D.6
  • 33
    • 50549086964 scopus 로고    scopus 로고
    • Native and unfolded cytochrome c: Comparison of dynamics using 2D-IR vibrational echo spectroscopy
    • Kim, S., Chung, J. K., Kwak, K., Bowman, S. E., Bren, K. L., Bagchi, B., and Fayer, M. D. (2008) Native and unfolded cytochrome c: Comparison of dynamics using 2D-IR vibrational echo spectroscopy J. Phys. Chem. B 112, 10054-10063
    • (2008) J. Phys. Chem. B , vol.112 , pp. 10054-10063
    • Kim, S.1    Chung, J.K.2    Kwak, K.3    Bowman, S.E.4    Bren, K.L.5    Bagchi, B.6    Fayer, M.D.7
  • 35
    • 79952775409 scopus 로고    scopus 로고
    • Protein dynamics in cytochrome p450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy
    • Thielges, M. C., Chung, J. K., and Fayer, M. D. (2011) Protein dynamics in cytochrome p450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy J. Am. Chem. Soc. 133, 3995-4004
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3995-4004
    • Thielges, M.C.1    Chung, J.K.2    Fayer, M.D.3
  • 36
    • 79952751402 scopus 로고    scopus 로고
    • Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations
    • Bagchi, S., Thorpe, D. G., Thorpe, I. F., Voth, G. A., and Fayer, M. D. (2010) Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations J. Phys. Chem. B 114, 17187-17193
    • (2010) J. Phys. Chem. B , vol.114 , pp. 17187-17193
    • Bagchi, S.1    Thorpe, D.G.2    Thorpe, I.F.3    Voth, G.A.4    Fayer, M.D.5
  • 37
    • 0001281879 scopus 로고
    • Vibrational dynamics of carbon monoxide at the active site of myoglobin: Picosecond infrared free-electron laser pump-probe experiments
    • Hill, J. R., Tokmakoff, A., Peterson, K. A., Sauter, B., Zimdars, D. A., Dlott, D. D., and Fayer, M. D. (1994) Vibrational dynamics of carbon monoxide at the active site of myoglobin: Picosecond infrared free-electron laser pump-probe experiments J. Phys. Chem. 98, 11213-11219
    • (1994) J. Phys. Chem. , vol.98 , pp. 11213-11219
    • Hill, J.R.1    Tokmakoff, A.2    Peterson, K.A.3    Sauter, B.4    Zimdars, D.A.5    Dlott, D.D.6    Fayer, M.D.7
  • 40
    • 0000364565 scopus 로고    scopus 로고
    • Vibrational echoes: A new approach to condensed-matter vibrational spectroscopy
    • Rector, K. D. and Fayer, M. D. (1998) Vibrational echoes: A new approach to condensed matter vibrational spectroscopy Int. Rev. Phys. Chem. 17, 261-306 (Pubitemid 128442645)
    • (1998) International Reviews in Physical Chemistry , vol.17 , Issue.3 , pp. 261-306
    • Rector, K.D.1    Fayer, M.D.2
  • 41
    • 0002298149 scopus 로고    scopus 로고
    • Myoglobin dynamics measured with vibrational echo experiments
    • Rector, K. D. and Fayer, M. D. (1999) Myoglobin dynamics measured with vibrational echo experiments Laser Chem. 19, 19-34
    • (1999) Laser Chem. , vol.19 , pp. 19-34
    • Rector, K.D.1    Fayer, M.D.2
  • 42
    • 0000403383 scopus 로고    scopus 로고
    • Dynamics in globular proteins: Vibrational echo experiments
    • Rector, K. D., Thompson, D. E., Merchant, K., and Fayer, M. D. (2000) Dynamics in globular proteins: Vibrational echo experiments Chem. Phys. Lett. 316, 122-128
    • (2000) Chem. Phys. Lett. , vol.316 , pp. 122-128
    • Rector, K.D.1    Thompson, D.E.2    Merchant, K.3    Fayer, M.D.4
  • 43
    • 0035937871 scopus 로고    scopus 로고
    • Two-dimensional time-frequency ultrafast infrared vibrational echo spectroscopy
    • DOI 10.1103/PhysRevLett.86.3899
    • Merchant, K. A., Thompson, D. E., and Fayer, M. D. (2001) Two-dimensional time-frequency ultrafast infrared vibrational echo spectroscopy Phys. Rev. Lett. 86, 3899-3902 (Pubitemid 32425359)
    • (2001) Physical Review Letters , vol.86 , Issue.17 , pp. 3899-3902
    • Merchant, K.A.1    Thompson, D.E.2    Fayer, M.D.3
  • 44
    • 0037180023 scopus 로고    scopus 로고
    • Frequency selected ultrafast infrared vibrational echo studies of liquids, glasses, and proteins
    • DOI 10.1021/jp021145q
    • Merchant, K. A., Xu, Q.-H., Thompson, D. E., and Fayer, M. D. (2002) Frequency selected ultrafast infrared vibrational echo studies of liquids, glasses and proteins J. Phys. Chem. A 106, 8839-8849 (Pubitemid 35382389)
    • (2002) Journal of Physical Chemistry A , vol.106 , Issue.38 , pp. 8839-8849
    • Merchant, K.A.1    Xu, Q.-H.2    Thompson, D.E.3    Fayer, M.D.4
  • 45
    • 25444521271 scopus 로고    scopus 로고
    • Ultrafast dynamics of myoglobin without the distal histidine: Stimulated vibrational echo experiments and molecular dynamics simulations
    • DOI 10.1021/jp0517201
    • Finkelstein, I. J., Goj, A., McClain, B. L., Massari, A. M., Merchant, K. A., Loring, R. F., and Fayer, M. D. (2005) Ultrafast dynamics of myoglobin without the distal histidine: Stimulated vibrational echo experiments and molecular dynamics simulations J. Phys. Chem. B 109, 16959-16966 (Pubitemid 41372079)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.35 , pp. 16959-16966
    • Finkelstein, I.J.1    Goj, A.2    McClain, B.L.3    Massari, A.M.4    Merchant, K.A.5    Loring, R.F.6    Fayer, M.D.7
  • 46
    • 26844437371 scopus 로고    scopus 로고
    • The influence of aqueous versus glassy solvents on protein dynamics: Vibrational echo experiments and molecular dynamics simulations
    • DOI 10.1021/ja053627w
    • Massari, A. M., Finkelstein, I. J., McClain, B. L., Goj, A., Wen, X., Bren, K. L., Loring, R. F., and Fayer, M. D. (2005) The influence of aqueous vs. glassy solvents on protein dynamics: Vibrational echo experiments and molecular dynamics simulations J. Am. Chem. Soc. 127, 14279-14289 (Pubitemid 41457592)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.41 , pp. 14279-14289
    • Massari, A.M.1    Finkelstein, I.J.2    McClain, B.L.3    Goj, A.4    Wen, X.5    Bren, K.L.6    Loring, R.F.7    Fayer, M.D.8
  • 47
    • 34147201258 scopus 로고    scopus 로고
    • Probing dynamics of complex molecular systems with ultrafast 2D IR vibrational echo spectroscopy
    • Finkelstein, I. J., Zheng, J., Ishikawa, H., Kim, S., Kwak, K., and Fayer, M. D. (2007) Probing dynamics of complex molecular systems with ultrafast 2D IR vibrational echo spectroscopy Phys. Chem. Chem. Phys. 9, 1533-1549
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1533-1549
    • Finkelstein, I.J.1    Zheng, J.2    Ishikawa, H.3    Kim, S.4    Kwak, K.5    Fayer, M.D.6
  • 48
    • 0019764210 scopus 로고
    • Self-association in highly concentrated-solutions of myoglobin: A novel analysis of sedimentation equilibrium of highly nonideal solutions
    • Minton, A. P. and Lewis, M. S. (1981) Self-association in highly concentrated-solutions of myoglobin: A novel analysis of sedimentation equilibrium of highly nonideal solutions Biophys. Chem. 14, 317-324
    • (1981) Biophys. Chem. , vol.14 , pp. 317-324
    • Minton, A.P.1    Lewis, M.S.2
  • 49
    • 34848915033 scopus 로고    scopus 로고
    • Ultrafast 2D-IR vibrational echo spectroscopy: A probe of molecular dynamics
    • Park, S., Kwak, K., and Fayer, M. D. (2007) Ultrafast 2D-IR vibrational echo spectroscopy: A probe of molecular dynamics Laser Phys. Lett. 4, 704-718
    • (2007) Laser Phys. Lett. , vol.4 , pp. 704-718
    • Park, S.1    Kwak, K.2    Fayer, M.D.3
  • 50
    • 34848897271 scopus 로고    scopus 로고
    • Frequency-frequency correlation functions and apodization in 2D-IR vibrational echo spectroscopy, a new approach
    • Kwak, K., Park, S., Finkelstein, I. J., and Fayer, M. D. (2007) Frequency-frequency correlation functions and apodization in 2D-IR vibrational echo spectroscopy, a new approach J. Chem. Phys. 127, 124503
    • (2007) J. Chem. Phys. , vol.127 , pp. 124503
    • Kwak, K.1    Park, S.2    Finkelstein, I.J.3    Fayer, M.D.4
  • 51
    • 44449086941 scopus 로고    scopus 로고
    • Taking apart 2D-IR vibrational echo spectra: More information and elimination of distortions
    • Kwak, K., Rosenfeld, D. E., and Fayer, M. D. (2008) Taking apart 2D-IR vibrational echo spectra: More information and elimination of distortions J. Chem. Phys. 128, 204505
    • (2008) J. Chem. Phys. , vol.128 , pp. 204505
    • Kwak, K.1    Rosenfeld, D.E.2    Fayer, M.D.3
  • 53
    • 33645455485 scopus 로고    scopus 로고
    • Dynamics of proteins encapsulated in silica sol-gel glasses studied with IR vibrational echo spectroscopy
    • Massari, A. M., Finkelstein, I. J., and Fayer, M. D. (2006) Dynamics of proteins encapsulated in silica sol-gel glasses studied with IR vibrational echo spectroscopy J. Am. Chem. Soc. 128, 3990-3997
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3990-3997
    • Massari, A.M.1    Finkelstein, I.J.2    Fayer, M.D.3
  • 54
    • 37649012488 scopus 로고    scopus 로고
    • Disulfide bonds' influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy
    • Ishikawa, H., Kim, S., Kwak, K., Wakasugi, K., and Fayer, M. D. (2007) Disulfide bonds' influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy Proc. Natl. Acad. Sci. U.S.A. 104, 19309-19314
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19309-19314
    • Ishikawa, H.1    Kim, S.2    Kwak, K.3    Wakasugi, K.4    Fayer, M.D.5
  • 55
    • 0000890164 scopus 로고
    • Dynamic protein structures
    • Shimada, H. and Caughey, W. S. (1982) Dynamic protein structures J. Biol. Chem. 257, 1893-1900
    • (1982) J. Biol. Chem. , vol.257 , pp. 1893-1900
    • Shimada, H.1    Caughey, W.S.2
  • 56
    • 0024334934 scopus 로고
    • Resonance Raman investigations of site-directed mutants of myoglobin: Effects of distal histidine replacement
    • DOI 10.1021/bi00437a041
    • Morikis, D., Champion, P. M., Springer, B. A., and Sligar, S. G. (1989) Resonance Raman investigations of site-directed mutants of myoglobin: Effects of distal histidine replacement Biochemistry 28, 4791-4800 (Pubitemid 19151059)
    • (1989) Biochemistry , vol.28 , Issue.11 , pp. 4791-4800
    • Morikis, D.1    Champion, P.M.2    Springer, B.A.3    Sligar, S.G.4
  • 57
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T., Quillin, M. L., Phillips, G. N., Jr., and Olson, J. S. (1994) Structural determinants of the stretching frequency of CO bound to myoglobin Biochemistry 33, 1433-1446 (Pubitemid 24093691)
    • (1994) Biochemistry , vol.33 , Issue.6 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 58
    • 0000756711 scopus 로고
    • Multilevel vibrational dephasing and vibrational anharmonicity from infrared photon echo beats
    • Tokmakoff, A., Kwok, A. S., Urdahl, R. S., Francis, R. S., and Fayer, M. D. (1995) Multilevel vibrational dephasing and vibrational anharmonicity from infrared photon echo beats Chem. Phys. Lett. 234, 289-295
    • (1995) Chem. Phys. Lett. , vol.234 , pp. 289-295
    • Tokmakoff, A.1    Kwok, A.S.2    Urdahl, R.S.3    Francis, R.S.4    Fayer, M.D.5
  • 59
    • 0031161849 scopus 로고    scopus 로고
    • Vibrational anharmonicity and multilevel vibrational dephasing from vibrational echo beats
    • Rector, K. D., Kwok, A. S., Ferrante, C., Tokmakoff, A., Rella, C. W., and Fayer, M. D. (1997) Vibrational anharmonicity and multilevel vibrational dephasing from vibrational echo beats J. Chem. Phys. 106, 10027-10036 (Pubitemid 127626966)
    • (1997) Journal of Chemical Physics , vol.106 , Issue.24 , pp. 10027-10036
    • Rector, K.D.1    Kwok, A.S.2    Ferrante, C.3    Tokmakoff, A.4    Rella, C.W.5    Fayer, M.D.6
  • 60
    • 4243879778 scopus 로고    scopus 로고
    • Vibrational anharmonicities revealed by coherent two-dimensional infrared spectroscopy
    • DOI 10.1103/PhysRevLett.86.2154
    • Golonzka, O., Khalil, M., Demirdoven, N., and Tokmakoff, A. (2001) Vibrational anharmonicities revealed by coherent two-dimensional infrared spectroscopy Phys. Rev. Lett. 86, 2154-2157 (Pubitemid 32254784)
    • (2001) Physical Review Letters , vol.86 , Issue.10 , pp. 2154-2157
    • Golonzka, O.1    Khalil, M.2    Demirdoven, N.3    Tokmakoff, A.4
  • 61
    • 48249120004 scopus 로고    scopus 로고
    • Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin
    • Ruscio, J. Z., Kumar, D., Shukla, M., Prisant, M. G., Murali, T. M., and Onufriev, A. V. (2008) Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin Proc. Natl. Acad. Sci. U.S.A. 105, 9204-9209
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9204-9209
    • Ruscio, J.Z.1    Kumar, D.2    Shukla, M.3    Prisant, M.G.4    Murali, T.M.5    Onufriev, A.V.6
  • 62
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • DOI 10.1038/nature05959, PII NATURE05959
    • Frederick, K. K., Marlow, M. S., Valentine, K. G., and Wand, A. J. (2007) Conformational entropy in molecular recognition by proteins Nature 448, 325-329 (Pubitemid 47080342)
    • (2007) Nature , vol.448 , Issue.7151 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 63
    • 0034868445 scopus 로고    scopus 로고
    • NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
    • DOI 10.1021/ar000079c
    • Stone, M. J. (2001) NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding Acc. Chem. Res. 34, 379-388 (Pubitemid 32816459)
    • (2001) Accounts of Chemical Research , vol.34 , Issue.5 , pp. 379-388
    • Stone, M.J.1
  • 64
    • 34047267978 scopus 로고    scopus 로고
    • Ultrafast catalytic processes in enzymes
    • Zhong, D. P. (2007) Ultrafast catalytic processes in enzymes Curr. Opin. Chem. Biol. 11, 174-181
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 174-181
    • Zhong, D.P.1
  • 65
    • 33646524282 scopus 로고    scopus 로고
    • Coupling between protein and reaction dynamics in enzymatic processes: Application of grote-hynes theory to catechol o-methyltransferase
    • Roca, M., Moliner, V., Tunon, I., and Hynes, J. T. (2006) Coupling between protein and reaction dynamics in enzymatic processes: Application of grote-hynes theory to catechol o-methyltransferase J. Am. Chem. Soc. 128, 6186-6193
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6186-6193
    • Roca, M.1    Moliner, V.2    Tunon, I.3    Hynes, J.T.4
  • 66
    • 4344700570 scopus 로고    scopus 로고
    • The structural dynamics of myoglobin
    • DOI 10.1016/j.jsb.2004.04.008, PII S1047847704001017
    • Brunori, M., Bourgeois, D., and Vallone, B. (2004) The structural dynamics of myoglobin J. Struct. Biol. 147, 223-234 (Pubitemid 39140731)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 223-234
    • Brunori, M.1    Bourgeois, D.2    Vallone, B.3
  • 67
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • DOI 10.1074/jbc.271.30.17593
    • Olson, J. S. and Phillips, G. N. (1996) Kinetic pathways and barriers for ligand binding to myoglobin J. Biol. Chem. 271, 17593-17596 (Pubitemid 26250722)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17593-17596
    • Olson, J.S.1    Phillips Jr., G.N.2
  • 68
    • 0011006084 scopus 로고    scopus 로고
    • Attachment of histidine tags to recombinant tumor necrosis factor-α drastically changes its properties
    • Fonda, I., Kenig, M., Gaberc-Porekar, V., Pristovaek, P., and Menart, V. (2002) Attachment of histidine tags to recombinant tumor necrosis factor-α drastically changes its properties Sci. World J. 2, 1312-1325
    • (2002) Sci. World J. , vol.2 , pp. 1312-1325
    • Fonda, I.1    Kenig, M.2    Gaberc-Porekar, V.3    Pristovaek, P.4    Menart, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.