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Volumn 147, Issue 3, 2004, Pages 235-246

Picosecond time-resolved X-ray crystallography: Probing protein function in real time

Author keywords

Laue; Myoglobin; Picosecond; Protein dynamics; Protein function; Time resolved X ray crystallography

Indexed keywords

MYOGLOBIN;

EID: 4344574384     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.06.009     Document Type: Article
Times cited : (155)

References (44)
  • 3
    • 0038892271 scopus 로고    scopus 로고
    • LSCALEâ€"the new normalization, scaling and absorption correction program in the Daresbury Laue software suite
    • S. Arzt LSCALEâ€"the new normalization, scaling and absorption correction program in the Daresbury Laue software suite J. Appl. Cryst. 33 1999 554 562
    • (1999) J. Appl. Cryst. , vol.33 , pp. 554-562
    • Arzt, S.1
  • 6
    • 0033869343 scopus 로고    scopus 로고
    • Towards automated Laue data processing: Application to the choice of optimal X-ray spectrum
    • D. Bourgeois, U. Wagner, and M. Wulff Towards automated Laue data processing: application to the choice of optimal X-ray spectrum Acta Cryst. D 2000 973 985
    • (2000) Acta Cryst. D , pp. 973-985
    • Bourgeois, D.1    Wagner2    Wulff, M.U.3
  • 7
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • Wiley New York
    • C.L. Brooks III, M. Karplus, and B.M. Pettitt Proteins: a theoretical perspective of dynamics, structure and thermodynamics Advances in Chemical Physics vol. 71 1988 Wiley New York
    • (1988) Advances in Chemical Physics , vol.71
    • Brooks III, C.L.1    Karplus2    Pettitt, B.M.M.3
  • 10
    • 0001405524 scopus 로고
    • LAUEGEN, an X-windows-based program for the processing of Laue X-ray diffraction data
    • J.W. Campbell LAUEGEN, an X-windows-based program for the processing of Laue X-ray diffraction data J. Appl. Cryst 18 1995 228 236
    • (1995) J. Appl. Cryst , vol.18 , pp. 228-236
    • Campbell, J.W.1
  • 12
    • 0027953943 scopus 로고
    • Nitric oxide recombination to double mutants of myoglobin: Role of ligand diffusion in a fluctuating heme pocket
    • M.L. Carlson, R. Regan, R. Elber, H. Li, G.N. Phillips Jr., J.S. Olson, and Q.H. Gibson Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket Biochemistry 33 1994 10597 10606
    • (1994) Biochemistry , vol.33 , pp. 10597-10606
    • Carlson, M.L.1    Regan, R.2    Elber, R.3    Li, H.4    Phillips Jr., G.N.5    Olson6    Gibson, Q.H.J.S.7
  • 14
    • 0037052504 scopus 로고    scopus 로고
    • Physics. The ultimate bright idea
    • A. Cho Physics. The ultimate bright idea Science 296 2002 1008 1010
    • (2002) Science , vol.296 , pp. 1008-1010
    • Cho, A.1
  • 15
    • 0034708201 scopus 로고    scopus 로고
    • Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin
    • K. Chu, J. Vojtchovsky, B.H. McMahon, R.M. Sweet, J. Berendzen, and I. Schlichting Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin Nature 403 2000 921 923
    • (2000) Nature , vol.403 , pp. 921-923
    • Chu, K.1    Vojtchovsky, J.2    McMahon, B.H.3    Sweet, R.M.4    Berendzen5    Schlichting, I.J.6
  • 16
    • 0025600834 scopus 로고
    • Enhanced sampling in molecular dynamics: Use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin
    • R. Elber, and M. Karplus Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin J. Am. Chem. Soc. 112 1990 9161 9175
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9161-9175
    • Elber1    Karplus, M.R.2
  • 17
    • 0001530911 scopus 로고
    • Photosensitivity of haem compounds
    • Q.H. Gibson, and S. Ainsworth Photosensitivity of haem compounds Nature 180 1957 1416 1417
    • (1957) Nature , vol.180 , pp. 1416-1417
    • Gibson1    Ainsworth, S.Q.H.2
  • 18
    • 0026526264 scopus 로고
    • Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants
    • Q.H. Gibson, R. Regan, R. Elber, J.S. Olson, and T.E. Carver Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants J. Biol. Chem. 267 1992 22022 22034
    • (1992) J. Biol. Chem. , vol.267 , pp. 22022-22034
    • Gibson, Q.H.1    Regan, R.2    Elber, R.3    Olson4    Carver, T.E.J.S.5
  • 19
    • 0001368645 scopus 로고    scopus 로고
    • Femtosecond Heterodyne-Detected Four-Wave-Mixing Studies of Deterministic Protein Motions. 2. Protein Response
    • G.D. Goodno, A. Astinov, and R.J.D. Miller Femtosecond Heterodyne-Detected Four-Wave-Mixing Studies of Deterministic Protein Motions. 2. Protein Response J. Phys. Chem. A 103 1999 10630 10643
    • (1999) J. Phys. Chem. a , vol.103 , pp. 10630-10643
    • Goodno, G.D.1    Astinov2    Miller, R.J.D.A.3
  • 20
    • 0021111948 scopus 로고
    • Geminate recombination of carbon monoxide to myoglobin
    • E.R. Henry, J.H. Sommer, J. Hofrichter, and W.A. Eaton Geminate recombination of carbon monoxide to myoglobin J. Mol. Biol. 166 1983 443 451
    • (1983) J. Mol. Biol. , vol.166 , pp. 443-451
    • Henry, E.R.1    Sommer, J.H.2    Hofrichter3    Eaton, W.A.J.4
  • 22
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • G.S. Kachalova, A.N. Popov, and H.D. Bartunik A steric mechanism for inhibition of CO binding to heme proteins Science 284 1999 473 476
    • (1999) Science , vol.284 , pp. 473-476
    • Kachalova, G.S.1    Popov2    Bartunik, H.D.A.N.3
  • 23
    • 36449006186 scopus 로고
    • Midinfrared vibrational-spectrum of CO after photodissociation from heme evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin
    • M.H. Lim, T.A. Jackson, and P.A. Anfinrud Midinfrared vibrational-spectrum of CO after photodissociation from heme evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin J. Chem. Phys. 102 1995 4355 4366
    • (1995) J. Chem. Phys. , vol.102 , pp. 4355-4366
    • Lim, M.H.1    Jackson2    Anfinrud, P.A.T.A.3
  • 25
    • 0035354587 scopus 로고    scopus 로고
    • Time-resolved biochemical crystallography: A mechanistic perspective
    • K. Moffat Time-resolved biochemical crystallography: a mechanistic perspective Chem. Rev. 101 2001 1569 1581
    • (2001) Chem. Rev. , vol.101 , pp. 1569-1581
    • Moffat, K.1
  • 27
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • J.S. Olson, and G.N. Phillips Jr. Kinetic pathways and barriers for ligand binding to myoglobin J. Biol. Chem. 271 1996 17596
    • (1996) J. Biol. Chem. , vol.271 , pp. 17596
    • Phillips G.N., Jr.1    Olson, J.S.2
  • 28
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • A. Ostermann, R. Waschipky, F.G. Parak, and G.U. Nienhaus Ligand binding and conformational motions in myoglobin Nature 404 2000 205 208
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak3    Nienhaus, G.U.F.G.4
  • 30
    • 0027368854 scopus 로고
    • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • M.L. Quillin, R.M. Arduini, J.S. Olson, and G.N. Phillips Jr. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin J. Mol. Biol. 234 1993 140 155
    • (1993) J. Mol. Biol. , vol.234 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Phillips G.N., Jr.3    Olson, J.S.4
  • 31
    • 0028941660 scopus 로고
    • Structural and functional effects of apolar mutations of the distal valine in myoglobin
    • M.L. Quillin Structural and functional effects of apolar mutations of the distal valine in myoglobin J. Mol. Biol. 245 1995 416 436
    • (1995) J. Mol. Biol. , vol.245 , pp. 416-436
    • Quillin, M.L.1
  • 32
    • 0022878103 scopus 로고
    • Simulation of carboxymyoglobin photodissociation
    • M. Sassaroli, and D.L. Rousseau Simulation of carboxymyoglobin photodissociation J. Biol. Chem. 261 1986 16292 16294
    • (1986) J. Biol. Chem. , vol.261 , pp. 16292-16294
    • Sassaroli1    Rousseau, D.L.M.2
  • 34
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: Ligand binding to myoglobin
    • I. Schlichting, and K. Chu Trapping intermediates in the crystal: ligand binding to myoglobin Curr. Opin. Struct. Biol. 10 2000 744 752
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 744-752
    • Schlichting1    Chu, K.I.2
  • 37
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
    • V. Srajer Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction Biochemistry 40 2001 13802 13815
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1
  • 38
    • 10544231457 scopus 로고    scopus 로고
    • Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time-resolved crystallography
    • V. Srajer Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography Science 274 1996 1726 1729
    • (1996) Science , vol.274 , pp. 1726-1729
    • Srajer, V.1
  • 39
    • 0028519126 scopus 로고
    • Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
    • T.Y. Teng, V. Srajer, and K. Moffat Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K Nat. Struct. Biol. 1 1994 701 705
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 701-705
    • Teng, T.Y.1    Srajer2    Moffat, K.V.3
  • 40
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 a
    • R.F. Tilton Jr., I.D. Kuntz Jr., and G.A. Petsko Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A Biochemistry 23 1984 2849 2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton Jr., R.F.1    Kuntz Jr., I.D.2    Petsko, G.A.3
  • 41
    • 0031051369 scopus 로고    scopus 로고
    • A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin
    • D. Vitkup, G.A. Petsko, and M. Karplus A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin Nat. Struct. Biol. 4 1997 202 208
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 202-208
    • Vitkup, D.1    Petsko2    Karplus, M.G.A.3
  • 42
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • J. Vojtechovsky, K. Chu, J. Berendzen, R.M. Sweet, and I. Schlichting Crystal structures of myoglobin-ligand complexes at near-atomic resolution Biophys. J. 77 1999 2153 2174
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet4    Schlichting, I.R.M.5
  • 44
    • 0037157156 scopus 로고    scopus 로고
    • Measurements of the photodissociation quantum yields of MbNO and MbO(2) and the vibrational relaxation of the six-coordinate heme species
    • X. Ye, A. Demidov, and P.M. Champion Measurements of the photodissociation quantum yields of MbNO and MbO(2) and the vibrational relaxation of the six-coordinate heme species J. Am. Chem. Soc. 124 2002 5914 5924
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5914-5924
    • Ye, X.1    Demidov2    Champion, P.M.A.3


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