-
1
-
-
0030504664
-
Feasibility and realization of single-pulse Laue diffraction on macromolecular crystals at ESRF
-
Bourgeois D, Ursby T, Wulff M, Pradervand C, Legrand A, Schildkamp W, Laboure S, Srajer S, Teng TY, Roth M, Moffat K. Feasibility and realization of single-pulse Laue diffraction on macromolecular crystals at ESRF. J Synchrotron Radiat. 3:1996;65-74.
-
(1996)
J Synchrotron Radiat
, vol.3
, pp. 65-74
-
-
Bourgeois, D.1
Ursby, T.2
Wulff, M.3
Pradervand, C.4
Legrand, A.5
Schildkamp, W.6
Laboure, S.7
Srajer, S.8
Teng, T.Y.9
Roth, M.10
Moffat, K.11
-
2
-
-
10544231457
-
Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time-resolved crystallography
-
Srajer V, Teng T, Ursby T, Pradervand C, Ren Z, Adachi S, Schildkamp W, Bourgeois D, Wulff M, Moffat K. 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
Teng, T.2
Ursby, T.3
Pradervand, C.4
Ren, Z.5
Adachi, S.6
Schildkamp, W.7
Bourgeois, D.8
Wulff, M.9
Moffat, K.10
-
4
-
-
76149099201
-
Biophysical applications of vibrational spectroscopy
-
New York: John Wiley & Sons
-
Diem M. Biophysical applications of vibrational spectroscopy. Introduction to Modern Vibrational Spectroscopy. 1993;204-235 John Wiley & Sons, New York.
-
(1993)
Introduction to Modern Vibrational Spectroscopy
, pp. 204-235
-
-
Diem, M.1
-
5
-
-
0028307232
-
Infrared methods for study of hemoglobin reactions and structures
-
Dong A, Caughey WS. Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 232:1994;139-175.
-
(1994)
Methods Enzymol
, vol.232
, pp. 139-175
-
-
Dong, A.1
Caughey, W.S.2
-
6
-
-
0027207780
-
Theory of photoselection by intense light pulses
-
Ansari A, Szabo A. Theory of photoselection by intense light pulses. Biophys J. 64:1993;838-851.
-
(1993)
Biophys J
, vol.64
, pp. 838-851
-
-
Ansari, A.1
Szabo, A.2
-
7
-
-
0027159782
-
Photoselection in polarized photolysis experiments on heme proteins
-
Ansari A, Jones CM, Henry ER, Hofrichter J, Eaton WA. Photoselection in polarized photolysis experiments on heme proteins. Biophys J. 64:1993;852-868.
-
(1993)
Biophys J
, vol.64
, pp. 852-868
-
-
Ansari, A.1
Jones, C.M.2
Henry, E.R.3
Hofrichter, J.4
Eaton, W.A.5
-
8
-
-
0029647452
-
Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O
-
Lim M, Jackson TA, Anfinrud PA. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O. Science. 269:1995;962-966.
-
(1995)
Science
, vol.269
, pp. 962-966
-
-
Lim, M.1
Jackson, T.A.2
Anfinrud, P.A.3
-
9
-
-
0342407584
-
The dynamics of conformational relaxation and ligand motion in myoglobin
-
Cambridge, MA: Harvard University
-
Lim M. The dynamics of conformational relaxation and ligand motion in myoglobin. PhD Thesis. 1995;Harvard University, Cambridge, MA.
-
(1995)
PhD Thesis
-
-
Lim, M.1
-
10
-
-
0031054657
-
Ultrafast dynamics of ligand rotation and trapping in photolyzed carbonmonoxy myoglobin
-
Time-resolved IR spectra of CO dissociated from the heme of Mb are recorded with ≈ 200 fs time resolution. The spectra reveal two CO trajectories in which the ligand rotates ≈ 90° and becomes trapped within a nearby ligand-docking site. Subsequent evolution of the CO spectrum reveals the dynamics of protein rearrangement about the translocated ligand. of outstanding interest
-
Lim M, Jackson TA, Anfinrud PA. Ultrafast dynamics of ligand rotation and trapping in photolyzed carbonmonoxy myoglobin. Nat Struct Biol. 4:1997;209-214 Time-resolved IR spectra of CO dissociated from the heme of Mb are recorded with ≈ 200 fs time resolution. The spectra reveal two CO trajectories in which the ligand rotates ≈ 90° and becomes trapped within a nearby ligand-docking site. Subsequent evolution of the CO spectrum reveals the dynamics of protein rearrangement about the translocated ligand. of outstanding interest.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 209-214
-
-
Lim, M.1
Jackson, T.A.2
Anfinrud, P.A.3
-
11
-
-
0025128786
-
Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopy
-
Rothberg L, Jedju TM, Austin RH. Ligand dynamics in the photodissociation of carboxyhemoglobin by subpicosecond transient infrared spectroscopy. Biophys J. 57:1990;369-373.
-
(1990)
Biophys J
, vol.57
, pp. 369-373
-
-
Rothberg, L.1
Jedju, T.M.2
Austin, R.H.3
-
12
-
-
0027222548
-
Determination of Fe-CO geometry in the subunits of carbonmonoxy hemoglobin M Boston using femtosecond infrared spectroscopy
-
Lian T, Locke B, Kitagawa T, Nagai M, Hochstrasser RM. Determination of Fe-CO geometry in the subunits of carbonmonoxy hemoglobin M Boston using femtosecond infrared spectroscopy. Biochemistry. 32:1993;5809-5814.
-
(1993)
Biochemistry
, vol.32
, pp. 5809-5814
-
-
Lian, T.1
Locke, B.2
Kitagawa, T.3
Nagai, M.4
Hochstrasser, R.M.5
-
13
-
-
0024040123
-
Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy
-
Moore JN, Hansen PA, Hochstrasser RM. Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy. Proc Natl Acad Sci USA. 85:1988;5062-5066.
-
(1988)
Proc Natl Acad Sci USA
, vol.85
, pp. 5062-5066
-
-
Moore, J.N.1
Hansen, P.A.2
Hochstrasser, R.M.3
-
14
-
-
0018109333
-
Infrared spectroscopy of ligands, gases, and other groups in aqueous solutions and tissues
-
Maxwell JC, Caughey WS. Infrared spectroscopy of ligands, gases, and other groups in aqueous solutions and tissues. Methods Enzymol. 54:1978;302-323.
-
(1978)
Methods Enzymol
, vol.54
, pp. 302-323
-
-
Maxwell, J.C.1
Caughey, W.S.2
-
15
-
-
33751156797
-
Protein dynamics in the bacteriorhodopsin photocycle: A nanosecond step-scan FTIR investigation of the KL to L transition
-
-1) reveal both fast and slow kinetic events in the bacteriorhodopsin KL to L transition. A comparison with results on hydrated films shows that when water activity is low, the fast kinetic process is blocked and a different L structure is produced. of special interest
-
-1) reveal both fast and slow kinetic events in the bacteriorhodopsin KL to L transition. A comparison with results on hydrated films shows that when water activity is low, the fast kinetic process is blocked and a different L structure is produced. of special interest.
-
(1996)
J Phys Chem
, vol.100
, pp. 16026-16033
-
-
Hage, W.1
Kim, M.2
Frei, H.3
Mathies, R.A.4
-
16
-
-
0027288334
-
Picosecond infrared studies of the dynamics of the photosynthetic reaction center
-
Maiti S, Cowen BR, Diller R, Iannone M, Moser CC, Dutton PL, Hochstrasser RM. Picosecond infrared studies of the dynamics of the photosynthetic reaction center. Proc Natl Acad Sci USA. 90:1993;5247-5251.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 5247-5251
-
-
Maiti, S.1
Cowen, B.R.2
Diller, R.3
Iannone, M.4
Moser, C.C.5
Dutton, P.L.6
Hochstrasser, R.M.7
-
17
-
-
0001221695
-
Transient binding of photodissociated CO to CuB+ of eukaryotic cytochrome oxidase at ambient temperature. Direct evidence from time-resolved infrared spectroscopy
-
Dyer RB, Einasdottir O, Killough PM, Lopez-Garriga JJ, Woodruff WH. Transient binding of photodissociated CO to CuB+ of eukaryotic cytochrome oxidase at ambient temperature. Direct evidence from time-resolved infrared spectroscopy. J Am Chem Soc. 111:1989;7657-7659.
-
(1989)
J Am Chem Soc
, vol.111
, pp. 7657-7659
-
-
Dyer, R.B.1
Einasdottir, O.2
Killough, P.M.3
Lopez-Garriga, J.J.4
Woodruff, W.H.5
-
18
-
-
0026648198
-
Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: Dynamics of binding and interaction upon QA and QB reduction
-
Hienerwadel R, Thibodeau D, Lenz F, Nabedryk E, Breton J, Kreutz W, Mantele W. Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics of binding and interaction upon QA and QB reduction. Biochemistry. 31:1992;5799-5808.
-
(1992)
Biochemistry
, vol.31
, pp. 5799-5808
-
-
Hienerwadel, R.1
Thibodeau, D.2
Lenz, F.3
Nabedryk, E.4
Breton, J.5
Kreutz, W.6
Mantele, W.7
-
19
-
-
0029818947
-
Nanosecond step-scan FTIR spectroscopy of hemoglobin: Ligand recombination and protein conformational changes
-
Conformational changes of hemoglobin upon ligand dissociation and recombination are probed using step-scan FTIR with 20 ns time resolution. Although most of the difference bands are developed within the first 50 ns, some arise with a time constant of 0.4 μs, reflecting a tertiary motion that is coincident with a quaternary motion detected by others. Two relaxation rates are observed, suggesting that either tertiary structural changes both precede and follow recombination, or there are different recombination rates for the α and β chains in the dimer. of special interest
-
Hu X, Frei H, Spiro TG. Nanosecond step-scan FTIR spectroscopy of hemoglobin: ligand recombination and protein conformational changes. Biochemistry. 35:1996;13001-13005 Conformational changes of hemoglobin upon ligand dissociation and recombination are probed using step-scan FTIR with 20 ns time resolution. Although most of the difference bands are developed within the first 50 ns, some arise with a time constant of 0.4 μs, reflecting a tertiary motion that is coincident with a quaternary motion detected by others. Two relaxation rates are observed, suggesting that either tertiary structural changes both precede and follow recombination, or there are different recombination rates for the α and β chains in the dimer. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 13001-13005
-
-
Hu, X.1
Frei, H.2
Spiro, T.G.3
-
20
-
-
0000005909
-
Time-resolved step-scan FTIR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations
-
Weidlich O, Siebert F. Time-resolved step-scan FTIR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations. Appl Spectroscr. 43:1993;1394-1400.
-
(1993)
Appl Spectroscr
, vol.43
, pp. 1394-1400
-
-
Weidlich, O.1
Siebert, F.2
-
21
-
-
0027478957
-
Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin
-
Sasaki J, Maeda A, Kato C, Hamaguchi H. Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin. Biochemistry. 32:1993;867-871.
-
(1993)
Biochemistry
, vol.32
, pp. 867-871
-
-
Sasaki, J.1
Maeda, A.2
Kato, C.3
Hamaguchi, H.4
-
22
-
-
0028944068
-
Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle
-
Sasaki J, Yuzawa T, Kandori H, Maeda A, Hamaguchi H. Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle. Biophys J. 68:1995;2073-2080.
-
(1995)
Biophys J
, vol.68
, pp. 2073-2080
-
-
Sasaki, J.1
Yuzawa, T.2
Kandori, H.3
Maeda, A.4
Hamaguchi, H.5
-
23
-
-
0000916745
-
Femtosecond IR spectroscopy: Methods and applications to protein dynamics
-
Anfinrud PA, Lim M, Jackson TA. Femtosecond IR spectroscopy: methods and applications to protein dynamics. Proc SPIE-Int Soc Opt Eng. 2138:1994;107-115.
-
(1994)
Proc SPIE-Int Soc Opt Eng
, vol.2138
, pp. 107-115
-
-
Anfinrud, P.A.1
Lim, M.2
Jackson, T.A.3
-
24
-
-
0027927167
-
Dual-beam subpicosecond broadband infrared spectrometer
-
Dougherty TP, Heilweil EJ. Dual-beam subpicosecond broadband infrared spectrometer. Optics Lett. 19:1994;129-131.
-
(1994)
Optics Lett
, vol.19
, pp. 129-131
-
-
Dougherty, T.P.1
Heilweil, E.J.2
-
25
-
-
0026390950
-
Applications of infrared free electron lasers: Basic research on the dynamics of molecular systems
-
Dlott DD, Fayer MD. Applications of infrared free electron lasers: basic research on the dynamics of molecular systems. IEEE J Quantum Electron. 27:1991;2697.
-
(1991)
IEEE J Quantum Electron
, vol.27
, pp. 2697
-
-
Dlott, D.D.1
Fayer, M.D.2
-
26
-
-
84865562884
-
Picosecond and femtosecond infrared spectroscopy with cw diode lasers
-
Anfinrud P, Han C, Hansen PA, Moore JN, Hochstrasser RM. Picosecond and femtosecond infrared spectroscopy with cw diode lasers. Spring Ser Chem Phys. 48:1988;442-446.
-
(1988)
Spring Ser Chem Phys
, vol.48
, pp. 442-446
-
-
Anfinrud, P.1
Han, C.2
Hansen, P.A.3
Moore, J.N.4
Hochstrasser, R.M.5
-
28
-
-
0026631357
-
Picosecond dynamics of bacteriorhodopsin, probed by time-resolved infrared spectroscopy
-
Diller R, Iannone M, Cowen BR, Maiti S, Bogomolni RA, Hochstrasser RM. Picosecond dynamics of bacteriorhodopsin, probed by time-resolved infrared spectroscopy. Biochemistry. 31:1992;5567-5572.
-
(1992)
Biochemistry
, vol.31
, pp. 5567-5572
-
-
Diller, R.1
Iannone, M.2
Cowen, B.R.3
Maiti, S.4
Bogomolni, R.A.5
Hochstrasser, R.M.6
-
29
-
-
0027948980
-
Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides
-
Maiti S, Walker GC, Cowen BR, Pippenger R, Moser CC, Dutton PL, Hochstrasser RM. Femtosecond coherent transient infrared spectroscopy of reaction centers from Rhodobacter sphaeroides. Proc Natl Acad Sci USA. 91:1994;10360-10364.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10360-10364
-
-
Maiti, S.1
Walker, G.C.2
Cowen, B.R.3
Pippenger, R.4
Moser, C.C.5
Dutton, P.L.6
Hochstrasser, R.M.7
-
30
-
-
0027187772
-
Ultrafast infrared spectroscopy of protein dynamics
-
Hochstrasser RM, Diller R, Maiti S, Lian T, Locke B, Moser C, Dutton PL, Cowen BR, Walker GC. Ultrafast infrared spectroscopy of protein dynamics. Spring Ser Chem Phys. 55:1993;517-521.
-
(1993)
Spring Ser Chem Phys
, vol.55
, pp. 517-521
-
-
Hochstrasser, R.M.1
Diller, R.2
Maiti, S.3
Lian, T.4
Locke, B.5
Moser, C.6
Dutton, P.L.7
Cowen, B.R.8
Walker, G.C.9
-
31
-
-
0030046906
-
Fast events in protein folding: Helix melting and formation in a small peptide
-
Unfolding of a 21-residue α-helical peptide (suc-Fs 21-peptide) is initiated using an 18° C T-jump with 20 ns resolution; refolding is not observed on the submillisecond timescale. The frequency and width of the amide I band are used to probe the kinetics of helix melting. Helix/coil interconversion is shown to occur on a timescale three orders of magnitude more rapid than that of intramolecular tertiary contact formation. of special interest
-
Williams S, Causgrove TP, Gilmanshin R, Fang KS, Callender RH, Woodruff WH, Dyer RB. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. 35:1996;691-697 Unfolding of a 21-residue α-helical peptide (suc-Fs 21-peptide) is initiated using an 18° C T-jump with 20 ns resolution; refolding is not observed on the submillisecond timescale. The frequency and width of the amide I band are used to probe the kinetics of helix melting. Helix/coil interconversion is shown to occur on a timescale three orders of magnitude more rapid than that of intramolecular tertiary contact formation. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 691-697
-
-
Williams, S.1
Causgrove, T.P.2
Gilmanshin, R.3
Fang, K.S.4
Callender, R.H.5
Woodruff, W.H.6
Dyer, R.B.7
-
32
-
-
0028967120
-
Protonation of Glu L212 following QB-formation in the photosynthetic reaction center of Rhodobacter sphaeroides: Evidence from time-resolved infrared spectroscopy
-
Hienerwadel R, Grzybek S, Fogel C, Kreutz W, Okamura MY, Paddock ML, Breton J, Nabedryk E, Mantele W. Protonation of Glu L212 following QB-formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy. Biochemistry. 34:1995;2832-2843.
-
(1995)
Biochemistry
, vol.34
, pp. 2832-2843
-
-
Hienerwadel, R.1
Grzybek, S.2
Fogel, C.3
Kreutz, W.4
Okamura, M.Y.5
Paddock, M.L.6
Breton, J.7
Nabedryk, E.8
Mantele, W.9
-
33
-
-
0002327112
-
Femtosecond time-resolved infrared laser study of the J-K transition of bacteriorhodopsin
-
Diller R, Maiti S, Walker GC, Cowen BR, Pippenger R, Bogomolni RA, Hochstrasser RM. Femtosecond time-resolved infrared laser study of the J-K transition of bacteriorhodopsin. Chem Phys Lett. 241:1995;109-115.
-
(1995)
Chem Phys Lett
, vol.241
, pp. 109-115
-
-
Diller, R.1
Maiti, S.2
Walker, G.C.3
Cowen, B.R.4
Pippenger, R.5
Bogomolni, R.A.6
Hochstrasser, R.M.7
-
34
-
-
0027363262
-
Photodissociation and recombination of carbonmonoxy cytochrome oxidase: Dynamics from picoseconds to kiloseconds
-
Einarsdottir O, Dyer RB, Lemon DD, Killough PM, Hubig SM, Atherton SJ, Lopez-Garriga JJ, Palmer G, Woodruff WH. Photodissociation and recombination of carbonmonoxy cytochrome oxidase: dynamics from picoseconds to kiloseconds. Biochemistry. 32:1993;12013-12024.
-
(1993)
Biochemistry
, vol.32
, pp. 12013-12024
-
-
Einarsdottir, O.1
Dyer, R.B.2
Lemon, D.D.3
Killough, P.M.4
Hubig, S.M.5
Atherton, S.J.6
Lopez-Garriga, J.J.7
Palmer, G.8
Woodruff, W.H.9
-
36
-
-
36449006186
-
Mid-IR vibrational spectrum of CO after photodissociation from heme: Evidence for a ligand docking site in the heme pocket of hemoglobin and myoglobin
-
Lim M, Jackson TA, Anfinrud PA. Mid-IR 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.1
Jackson, T.A.2
Anfinrud, P.A.3
-
37
-
-
0030882198
-
Modulating carbon monoxide binding affinity and kinetics in myoglobin: The roles of the distal histidine and the heme pocket docking site
-
in press
-
Lim M, Jackson TA, Anfinrud PA. Modulating carbon monoxide binding affinity and kinetics in myoglobin: the roles of the distal histidine and the heme pocket docking site. J Biol Inorg Chem. 1997;. in press.
-
(1997)
J Biol Inorg Chem
-
-
Lim, M.1
Jackson, T.A.2
Anfinrud, P.A.3
-
38
-
-
0027362481
-
Protein response to photodissociation of CO from carbonmonoxymyoglobin probed by time-resolved infrared spectroscopy of the amide I band
-
Causgrove TP, Dyer RB. Protein response to photodissociation of CO from carbonmonoxymyoglobin probed by time-resolved infrared spectroscopy of the amide I band. Biochemistry. 32:1993;11985-11991.
-
(1993)
Biochemistry
, vol.32
, pp. 11985-11991
-
-
Causgrove, T.P.1
Dyer, R.B.2
-
39
-
-
0030079898
-
Picosecond structural dynamics of myoglobin following photolysis of carbon monoxide
-
Causgrove TP, Dyer RB. Picosecond structural dynamics of myoglobin following photolysis of carbon monoxide. J Phys Chem. 100:1996;3273-3277.
-
(1996)
J Phys Chem
, vol.100
, pp. 3273-3277
-
-
Causgrove, T.P.1
Dyer, R.B.2
|