-
1
-
-
0040362704
-
Chemical basis for enzyme catalysis
-
Bruice T.C., Benkovic S.J. Chemical basis for enzyme catalysis. Biochemistry. 39:2000;6267-6274.
-
(2000)
Biochemistry
, vol.39
, pp. 6267-6274
-
-
Bruice, T.C.1
Benkovic, S.J.2
-
2
-
-
0001804089
-
Aspects of protein reaction dynamics: Deviations from simple behavior
-
Karplus M. Aspects of protein reaction dynamics: deviations from simple behavior. J Phys Chem B. 104:2000;11-27.
-
(2000)
J Phys Chem B
, vol.104
, pp. 11-27
-
-
Karplus, M.1
-
3
-
-
0035940264
-
Energetics and dynamics of enzymatic reactions
-
Villa J., Warshel A. Energetics and dynamics of enzymatic reactions. J Phys Chem B. 105:2001;7887-7907.
-
(2001)
J Phys Chem B
, vol.105
, pp. 7887-7907
-
-
Villa, J.1
Warshel, A.2
-
4
-
-
0033970020
-
Folding and binding cascades: Dynamic landscapes and population shifts
-
Kumar S., Ma B., Tsai C.-J., Sinha N., Nussinov R. Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci. 9:2000;10-19.
-
(2000)
Protein Sci
, vol.9
, pp. 10-19
-
-
Kumar, S.1
Ma, B.2
Tsai, C.-J.3
Sinha, N.4
Nussinov, R.5
-
6
-
-
0034919305
-
Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
-
An excellent and comprehensive review of the methods developed through 2000.
-
Palmer A.G., Kroenke C.D., Loria J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339:2001;204-238. An excellent and comprehensive review of the methods developed through 2000.
-
(2001)
Methods Enzymol
, vol.339
, pp. 204-238
-
-
Palmer, A.G.1
Kroenke, C.D.2
Loria, J.P.3
-
7
-
-
0034760077
-
Dynamic activation of protein function: A view emerging from NMR spectroscopy
-
Wand A.J. Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat Struct Biol. 8:2001;926-931.
-
(2001)
Nat Struct Biol
, vol.8
, pp. 926-931
-
-
Wand, A.J.1
-
8
-
-
0034033187
-
Long timescale simulations
-
Daggett V. Long timescale simulations. Curr Opin Struct Biol. 10:2000;160-164.
-
(2000)
Curr Opin Struct Biol
, vol.10
, pp. 160-164
-
-
Daggett, V.1
-
10
-
-
0032871220
-
Estimating the time scale of chemical exchange in proteins from measurements of transverse relaxation rates in solution
-
Ishima R., Torchia D.A. Estimating the time scale of chemical exchange in proteins from measurements of transverse relaxation rates in solution. J Biomol NMR. 14:1999;369-372.
-
(1999)
J Biomol NMR
, vol.14
, pp. 369-372
-
-
Ishima, R.1
Torchia, D.A.2
-
11
-
-
0034728579
-
The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
-
ex and Δω across all timescales. A single dimensionless parameter α is defined that uniquely determines the chemical shift timescale for the case of skewed populations. This information is vital for accurate extraction of dynamics parameters by fitting analytical expressions to relaxation data.
-
ex and Δω across all timescales. A single dimensionless parameter α is defined that uniquely determines the chemical shift timescale for the case of skewed populations. This information is vital for accurate extraction of dynamics parameters by fitting analytical expressions to relaxation data.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 2867-2877
-
-
Millet, O.1
Loria, J.P.2
Kroenke, C.D.3
Pons, M.4
Palmer, A.G.5
-
12
-
-
0034759979
-
Studying excited states of proteins by NMR spectroscopy
-
This paper describes the most careful and extensive characterization of conformational exchange published to date. Relaxation dispersion data obtained using relaxation-compensated CPMG experiments on multiple nuclei at multiple static magnetic field strengths and temperatures enabled a complete characterization of the rates, populations and activation barriers of this process. The study clearly demonstrates the great power of NMR relaxation measurements for investigating the dynamics of transitions that involve only very small populations of alternative conformations.
-
Mulder F.A.A., Mittermaier A., Hon B., Dahlquist F.W., Kay L.E. Studying excited states of proteins by NMR spectroscopy. Nat Struct Biol. 8:2001;932-935. This paper describes the most careful and extensive characterization of conformational exchange published to date. Relaxation dispersion data obtained using relaxation-compensated CPMG experiments on multiple nuclei at multiple static magnetic field strengths and temperatures enabled a complete characterization of the rates, populations and activation barriers of this process. The study clearly demonstrates the great power of NMR relaxation measurements for investigating the dynamics of transitions that involve only very small populations of alternative conformations.
-
(2001)
Nat Struct Biol
, vol.8
, pp. 932-935
-
-
Mulder, F.A.A.1
Mittermaier, A.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
13
-
-
0035930026
-
Slow dynamics in folded and unfolded states of an SH3 domain
-
An analytical expression is derived that accurately describes the exchange contributions to the relaxation rates measured by CPMG methods under conditions of slow exchange. The authors demonstrate the use of these methods for studying protein folding reactions under equilibrium conditions.
-
Tollinger M., Skrynnikov N.R., Mulder F.A.A., Forman-Kay J.D., Kay L.E. Slow dynamics in folded and unfolded states of an SH3 domain. J Am Chem Soc. 123:2001;11341-11352. An analytical expression is derived that accurately describes the exchange contributions to the relaxation rates measured by CPMG methods under conditions of slow exchange. The authors demonstrate the use of these methods for studying protein folding reactions under equilibrium conditions.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 11341-11352
-
-
Tollinger, M.1
Skrynnikov, N.R.2
Mulder, F.A.A.3
Forman-Kay, J.D.4
Kay, L.E.5
-
14
-
-
0036018262
-
1ρ relaxation outside the fast-exchange limit
-
The authors extend the analytical expression describing the dependence of the rotating-frame relaxation rate on the conformational exchange and spin-lock parameters. This work reveals that off-resonance spin-lock methods may be very advantageous for separating the chemical shift and population parameters using data obtained at a single magnetic field strength for systems outside the fast-exchange regime.
-
1ρ relaxation outside the fast-exchange limit. J Magn Reson. 154:2002;157-160. The authors extend the analytical expression describing the dependence of the rotating-frame relaxation rate on the conformational exchange and spin-lock parameters. This work reveals that off-resonance spin-lock methods may be very advantageous for separating the chemical shift and population parameters using data obtained at a single magnetic field strength for systems outside the fast-exchange regime.
-
(2002)
J Magn Reson
, vol.154
, pp. 157-160
-
-
Trott, O.1
Palmer, A.G.2
-
15
-
-
0033792053
-
Simulation of NMR pulse sequences during equilibrium and non-equilibrium chemical exchange
-
Helgstrand M., Härd T., Allard P. Simulation of NMR pulse sequences during equilibrium and non-equilibrium chemical exchange. J Biomol NMR. 18:2000;49-63.
-
(2000)
J Biomol NMR
, vol.18
, pp. 49-63
-
-
Helgstrand, M.1
Härd, T.2
Allard, P.3
-
16
-
-
0033577288
-
A relaxation-compensated Carr-Purcell-Meiboom-Gill for characterizing chemical exchange by NMR spectroscopy
-
Loria J.P., Rance M., Palmer A.G. A relaxation-compensated Carr-Purcell-Meiboom-Gill for characterizing chemical exchange by NMR spectroscopy. J Am Chem Soc. 121:1999;2331-2332.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 2331-2332
-
-
Loria, J.P.1
Rance, M.2
Palmer, A.G.3
-
17
-
-
0035695509
-
CPMG sequences with enhanced sensitivity to chemical exchange
-
Wang C.Y., Grey M.J., Palmer A.G. CPMG sequences with enhanced sensitivity to chemical exchange. J Biomol NMR. 21:2001;361-366.
-
(2001)
J Biomol NMR
, vol.21
, pp. 361-366
-
-
Wang, C.Y.1
Grey, M.J.2
Palmer, A.G.3
-
18
-
-
0030612833
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA. 94:1997;12366-12371.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 12366-12371
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wüthrich, K.4
-
19
-
-
0032719427
-
A TROSY CPMG sequence for characterizing chemical exchange in large proteins
-
Loria J.P., Rance M., Palmer A.G. A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J Biomol NMR. 15:1999;151-155.
-
(1999)
J Biomol NMR
, vol.15
, pp. 151-155
-
-
Loria, J.P.1
Rance, M.2
Palmer, A.G.3
-
20
-
-
0032842695
-
13C spin relaxation measurements in RNA: Sensitivity and resolution improvement using spin-state selective correlation experiments
-
13C spin relaxation measurements in RNA: Sensitivity and resolution improvement using spin-state selective correlation experiments. J Biomol NMR. 14:1999;241-252.
-
(1999)
J Biomol NMR
, vol.14
, pp. 241-252
-
-
Boisbouvier, J.1
Brutscher, B.2
Simorre, J.-P.3
Marion, D.4
-
21
-
-
0033003378
-
Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements
-
Mulder F.A.A., van Tilborg P.J.A., Kaptein R., Boelens R. Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. J Biomol NMR. 13:1999;275-288.
-
(1999)
J Biomol NMR
, vol.13
, pp. 275-288
-
-
Mulder, F.A.A.1
Van Tilborg, P.J.A.2
Kaptein, R.3
Boelens, R.4
-
22
-
-
0033121306
-
Separating the contributions to N-15 transverse relaxation in a fibronectin type III domain
-
Meekhof A.E., Freund S.M.V. Separating the contributions to N-15 transverse relaxation in a fibronectin type III domain. J Biomol NMR. 14:1999;13-22.
-
(1999)
J Biomol NMR
, vol.14
, pp. 13-22
-
-
Meekhof, A.E.1
Freund, S.M.V.2
-
23
-
-
0033572874
-
2 methyl isotopomers to detect slow conformational changes of protein side chains
-
2 methyl isotopomers to detect slow conformational changes of protein side chains. J Am Chem Soc. 121:1999;11589-11590.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 11589-11590
-
-
Ishima, R.1
Louis, J.M.2
Torchia, D.A.3
-
24
-
-
0035819455
-
15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
-
This paper is the first in a series (see also [25••,26••]) that uses a constant-time CPMG scheme with variable refocusing delays to enable characterization of exchange dynamics in sidechains. These studies take into careful consideration the several relaxation pathways that are active for these spin systems and include simulations of the evolution of the density matrix during the proposed pulse sequences.
-
15N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc. 123:2001;967-975. This paper is the first in a series (see also [25••,26••]) that uses a constant-time CPMG scheme with variable refocusing delays to enable characterization of exchange dynamics in sidechains. These studies take into careful consideration the several relaxation pathways that are active for these spin systems and include simulations of the evolution of the density matrix during the proposed pulse sequences.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 967-975
-
-
Mulder, F.A.A.1
Skrynnikov, N.R.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
25
-
-
0034809982
-
Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme
-
See annotation to [24••].
-
Skrynnikov N.R., Mulder F.A.A., Hon B., Dahlquist F.W., Kay L.E. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. J Am Chem Soc. 123:2001;4556-4566. See annotation to [24••].
-
(2001)
J Am Chem Soc
, vol.123
, pp. 4556-4566
-
-
Skrynnikov, N.R.1
Mulder, F.A.A.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
26
-
-
0037138654
-
Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme
-
See annotation to [24••].
-
Mulder F.A.A., Hon B., Mittermaier A., Dahlquist F.W., Kay L.E. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. J Am Chem Soc. 124:2001;1443-1451. See annotation to [24••].
-
(2001)
J Am Chem Soc
, vol.124
, pp. 1443-1451
-
-
Mulder, F.A.A.1
Hon, B.2
Mittermaier, A.3
Dahlquist, F.W.4
Kay, L.E.5
-
27
-
-
0037063506
-
An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates
-
Korzhnev D.M., Skrynnikov N.R., Millet O., Torchia D.A., Kay L.E. An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates. J Am Chem Soc. 124:2002;10743-10753.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 10743-10753
-
-
Korzhnev, D.M.1
Skrynnikov, N.R.2
Millet, O.3
Torchia, D.A.4
Kay, L.E.5
-
28
-
-
0032608454
-
A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated
-
Guenneugues M., Berthault P., Desvaux H. A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated. J Magn Reson. 136:1999;118-126.
-
(1999)
J Magn Reson
, vol.136
, pp. 118-126
-
-
Guenneugues, M.1
Berthault, P.2
Desvaux, H.3
-
29
-
-
0035078116
-
Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant
-
ex cluster in the structure.
-
ex cluster in the structure.
-
(2001)
Structure
, vol.9
, pp. 185-195
-
-
Evenäs, J.1
Malmendal, A.2
Akke, M.3
-
30
-
-
0000252605
-
Analysis of Carr-Purcell sequences with nonideal pulses
-
Simbrunner J., Stollberger R. Analysis of Carr-Purcell sequences with nonideal pulses. J Magn Reson. 109:1995;301-309.
-
(1995)
J Magn Reson
, vol.109
, pp. 301-309
-
-
Simbrunner, J.1
Stollberger, R.2
-
31
-
-
0000698894
-
Systematic errors associated with the CPMG pulse sequence and their effects on motional analysis of biomolecules
-
Ross A., Czisch M., King G.C. Systematic errors associated with the CPMG pulse sequence and their effects on motional analysis of biomolecules. J Magn Reson. 124:1997;355-365.
-
(1997)
J Magn Reson
, vol.124
, pp. 355-365
-
-
Ross, A.1
Czisch, M.2
King, G.C.3
-
34
-
-
0033788347
-
Differential multiple-quantum relaxation arising from cross-correlated time-modulation of isotropic chemical shifts
-
Kloiber K., Konrat R. Differential multiple-quantum relaxation arising from cross-correlated time-modulation of isotropic chemical shifts. J Biomol NMR. 18:2000;33-42.
-
(2000)
J Biomol NMR
, vol.18
, pp. 33-42
-
-
Kloiber, K.1
Konrat, R.2
-
35
-
-
0034821018
-
Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins
-
Früh D., Tolman J.R., Bodenhausen G., Zwahlen C. Cross-correlated chemical shift modulation: a signature of slow internal motions in proteins. J Am Chem Soc. 123:2001;4810-4816.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 4810-4816
-
-
Früh, D.1
Tolman, J.R.2
Bodenhausen, G.3
Zwahlen, C.4
-
36
-
-
0037120879
-
Reconstructing NMR spectra of 'invisible' excited states using HSQC and HMQC experiments
-
in press
-
Skrynnikov NR, Dahlquist FW, Kay LE: Reconstructing NMR spectra of 'invisible' excited states using HSQC and HMQC experiments. J Am Chem Soc 2002, in press.
-
(2002)
J Am Chem Soc
-
-
Skrynnikov, N.R.1
Dahlquist, F.W.2
Kay, L.E.3
-
37
-
-
0035937443
-
Two-state allosteric behaviour in a single-domain signaling protein
-
The authors compared the extent of exchange line broadening with coordinate differences and chemical shift perturbations for phosphorylated (active) and nonphosphorylated (inactive) states of the signaling protein NtrC, together with a nonphosphorylated but partially active mutant. The results indicate that the inactive state transiently populates conformations that are very similar to the active state. This provides a strong case for a scheme in which phosphorylation stabilizes a pre-existing but weakly populated conformation.
-
Volkman B.F., Lipson D., Wemmer D.E., Kern D. Two-state allosteric behaviour in a single-domain signaling protein. Science. 291:2001;2429-2433. The authors compared the extent of exchange line broadening with coordinate differences and chemical shift perturbations for phosphorylated (active) and nonphosphorylated (inactive) states of the signaling protein NtrC, together with a nonphosphorylated but partially active mutant. The results indicate that the inactive state transiently populates conformations that are very similar to the active state. This provides a strong case for a scheme in which phosphorylation stabilizes a pre-existing but weakly populated conformation.
-
(2001)
Science
, vol.291
, pp. 2429-2433
-
-
Volkman, B.F.1
Lipson, D.2
Wemmer, D.E.3
Kern, D.4
-
38
-
-
0040316915
-
Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation
-
van Tilborg P.J., Mulder F.A.A., de Backer M.M.E., Nair M., van Heerde E.C., Folkers G., van der Saag P.T., Karimi-Nejad Y., Boelens R., Kaptein R. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry. 38:1999;1951-1956.
-
(1999)
Biochemistry
, vol.38
, pp. 1951-1956
-
-
Van Tilborg, P.J.1
Mulder, F.A.A.2
De Backer, M.M.E.3
Nair, M.4
Van Heerde, E.C.5
Folkers, G.6
Van der Saag, P.T.7
Karimi-Nejad, Y.8
Boelens, R.9
Kaptein, R.10
-
39
-
-
0033544709
-
Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein
-
Mittermaier A., Varani L., Muhandiram D.R., Kay L.E., Varani G. Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein. J Mol Biol. 294:1999;967-979.
-
(1999)
J Mol Biol
, vol.294
, pp. 967-979
-
-
Mittermaier, A.1
Varani, L.2
Muhandiram, D.R.3
Kay, L.E.4
Varani, G.5
-
40
-
-
0033527588
-
Structural dynamics in the C-terminal domain of calmodulin at low calcium levels
-
Malmendal A., Evenäs J., Forsén S., Akke M. Structural dynamics in the C-terminal domain of calmodulin at low calcium levels. J Mol Biol. 293:1999;883-899.
-
(1999)
J Mol Biol
, vol.293
, pp. 883-899
-
-
Malmendal, A.1
Evenäs, J.2
Forsén, S.3
Akke, M.4
-
41
-
-
0033200247
-
Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function
-
Ishima R., Freedberg D.I., Wang Y.-X., Louis J.M., Torchia D.A. Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure. 7:1999;1047-1055.
-
(1999)
Structure
, vol.7
, pp. 1047-1055
-
-
Ishima, R.1
Freedberg, D.I.2
Wang, Y.-X.3
Louis, J.M.4
Torchia, D.A.5
-
42
-
-
0033566242
-
Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F
-
Feher V.A., Cavanagh J. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature. 400:1999;289-293.
-
(1999)
Nature
, vol.400
, pp. 289-293
-
-
Feher, V.A.1
Cavanagh, J.2
-
43
-
-
0034625316
-
Backbone dynamics of the C-terminal SH2 domain of the p85a subunit of phosphoinositide 3-kinase: Effect of phosphotyrosine-peptide binding and characterization of slow conformational exchange processes
-
Kristensen S.M., Siegal G., Sankar A., Driscoll P.C. Backbone dynamics of the C-terminal SH2 domain of the p85a subunit of phosphoinositide 3-kinase: effect of phosphotyrosine-peptide binding and characterization of slow conformational exchange processes. J Mol Biol. 299:2000;771-788.
-
(2000)
J Mol Biol
, vol.299
, pp. 771-788
-
-
Kristensen, S.M.1
Siegal, G.2
Sankar, A.3
Driscoll, P.C.4
-
44
-
-
0034647414
-
Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics
-
Lu J., Lin C.-L., Tang C., Ponder J.W., Kao J.L.F., Cistola D.P., Li E. Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics. J Mol Biol. 300:2000;619-632.
-
(2000)
J Mol Biol
, vol.300
, pp. 619-632
-
-
Lu, J.1
Lin, C.-L.2
Tang, C.3
Ponder, J.W.4
Kao, J.L.F.5
Cistola, D.P.6
Li, E.7
-
45
-
-
0033997901
-
The influence of DNA binding on the backbone dynamics of the yeast cell-cycle protein Mbp1
-
McIntosh P.B., Taylor I.A., Frenkiel T.A., Smerdon S.J., Lane A.N. The influence of DNA binding on the backbone dynamics of the yeast cell-cycle protein Mbp1. J Biomol NMR. 16:2000;183-196.
-
(2000)
J Biomol NMR
, vol.16
, pp. 183-196
-
-
McIntosh, P.B.1
Taylor, I.A.2
Frenkiel, T.A.3
Smerdon, S.J.4
Lane, A.N.5
-
46
-
-
0035967856
-
Solution-state NMR investigations of triose phosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
-
Rozovsky S., Jogl G., Tong L., McDermott A.E. Solution-state NMR investigations of triose phosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J Mol Biol. 310:2001;271-280.
-
(2001)
J Mol Biol
, vol.310
, pp. 271-280
-
-
Rozovsky, S.1
Jogl, G.2
Tong, L.3
McDermott, A.E.4
-
47
-
-
0035822676
-
Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA
-
Zhu L., Hu J., Lin D., Whitson R., Itakura K., Chen Y. Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA. Biochemistry. 40:2001;9142-9150.
-
(2001)
Biochemistry
, vol.40
, pp. 9142-9150
-
-
Zhu, L.1
Hu, J.2
Lin, D.3
Whitson, R.4
Itakura, K.5
Chen, Y.6
-
48
-
-
0035979729
-
Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF-1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA
-
Katahira M., Miyanoiri Y., Enokizono Y., Matsuda G., Nagata T., Ishikawa F., Uesugi S. Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF-1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA. J Mol Biol. 311:2001;973-988.
-
(2001)
J Mol Biol
, vol.311
, pp. 973-988
-
-
Katahira, M.1
Miyanoiri, Y.2
Enokizono, Y.3
Matsuda, G.4
Nagata, T.5
Ishikawa, F.6
Uesugi, S.7
-
49
-
-
0035823058
-
Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Landau peptide
-
Botuyan M.V., Mer G., Yi G.-S., Koth C.M., Case D.A., Edwards A.M., Chazin W.J., Arrowsmith C.H. Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Landau peptide. J Mol Biol. 312:2001;177-186.
-
(2001)
J Mol Biol
, vol.312
, pp. 177-186
-
-
Botuyan, M.V.1
Mer, G.2
Yi, G.-S.3
Koth, C.M.4
Case, D.A.5
Edwards, A.M.6
Chazin, W.J.7
Arrowsmith, C.H.8
-
50
-
-
0034664076
-
Active site dynamics in the lead-dependent ribozyme
-
Hoogstraten C.G., Wank J.R., Pardi A. Active site dynamics in the lead-dependent ribozyme. Biochemistry. 39:2000;9951-9958.
-
(2000)
Biochemistry
, vol.39
, pp. 9951-9958
-
-
Hoogstraten, C.G.1
Wank, J.R.2
Pardi, A.3
-
51
-
-
0035928796
-
Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
-
Osborne M.J., Schnell J., Benkovic S.J., Dyson H.J., Wright P.E. Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry. 40:2001;9846-9859.
-
(2001)
Biochemistry
, vol.40
, pp. 9846-9859
-
-
Osborne, M.J.1
Schnell, J.2
Benkovic, S.J.3
Dyson, H.J.4
Wright, P.E.5
-
52
-
-
0034945906
-
Functional dynamics in the active site of the ribonuclease binase
-
A nice example of how dynamics measurements can be complemented with analysis of residual dipolar couplings to obtain a more complete picture of the conformational fluctuations.
-
Wang L., Pang Y., Holder T., Brender J.R., Kurochkin A.V., Zuiderweg E.R.P. Functional dynamics in the active site of the ribonuclease binase. Proc Natl Acad Sci USA. 98:2001;7684-7689. A nice example of how dynamics measurements can be complemented with analysis of residual dipolar couplings to obtain a more complete picture of the conformational fluctuations.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 7684-7689
-
-
Wang, L.1
Pang, Y.2
Holder, T.3
Brender, J.R.4
Kurochkin, A.V.5
Zuiderweg, E.R.P.6
-
54
-
-
0037154884
-
Enzyme dynamics during catalysis
-
15N nuclei in cyclophilin A that are sensitive to substrate isomerization and/or binding. The binding constant and off-rate are found to agree with previous enzymological results. Numerical simulations of a minimal three-state system (cyclophilin A free, and bound to the substrate and product) indicate that the conformational exchange rate observed for the catalytically essential residue Arg55 corresponds well to the previously determined catalytic rate.
-
15N nuclei in cyclophilin A that are sensitive to substrate isomerization and/or binding. The binding constant and off-rate are found to agree with previous enzymological results. Numerical simulations of a minimal three-state system (cyclophilin A free, and bound to the substrate and product) indicate that the conformational exchange rate observed for the catalytically essential residue Arg55 corresponds well to the previously determined catalytic rate.
-
(2002)
Science
, vol.295
, pp. 1520-1523
-
-
Eisenmesser, E.Z.1
Bosco, D.A.2
Akke, M.3
Kern, D.4
-
55
-
-
0034680315
-
Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR
-
Mulder F.A.A., Hon B., Muhandiram D.R., Dahlquist F.W., Kay L.E. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39:2000;12614-12622.
-
(2000)
Biochemistry
, vol.39
, pp. 12614-12622
-
-
Mulder, F.A.A.1
Hon, B.2
Muhandiram, D.R.3
Dahlquist, F.W.4
Kay, L.E.5
-
57
-
-
0037051893
-
NMR measurement of the off rate from the first calcium-binding site of the synaptotagmin I C2A domain
-
Millet O., Bernado P., Garcia J., Rizo J., Pons M. NMR measurement of the off rate from the first calcium-binding site of the synaptotagmin I C2A domain. FEBS Lett. 516:2002;93-96.
-
(2002)
FEBS Lett
, vol.516
, pp. 93-96
-
-
Millet, O.1
Bernado, P.2
Garcia, J.3
Rizo, J.4
Pons, M.5
-
58
-
-
0031984752
-
Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
-
Akke M., Liu J., Cavanagh J., Erickson H.P., Palmer A.G. Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat Struct Biol. 5:1998;55-59.
-
(1998)
Nat Struct Biol
, vol.5
, pp. 55-59
-
-
Akke, M.1
Liu, J.2
Cavanagh, J.3
Erickson, H.P.4
Palmer, A.G.5
-
59
-
-
0032852490
-
NMR exchange broadening arising from specific low affinity protein self-association: Analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1
-
Pfuhl M., Chen H.A., Kristensen S.M., Driscoll P.C. NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1. J Biomol NMR. 14:1999;307-320.
-
(1999)
J Biomol NMR
, vol.14
, pp. 307-320
-
-
Pfuhl, M.1
Chen, H.A.2
Kristensen, S.M.3
Driscoll, P.C.4
-
60
-
-
0034730994
-
Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of αD-2 using C-13 NMR spin relaxation
-
Hill R.B., Bracken C., DeGrado W.F., Palmer A.G. Molecular motions and protein folding: Characterization of the backbone dynamics and folding equilibrium of αD-2 using C-13 NMR spin relaxation. J Am Chem Soc. 122:2000;11610-11619.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 11610-11619
-
-
Hill, R.B.1
Bracken, C.2
DeGrado, W.F.3
Palmer, A.G.4
-
61
-
-
0035819950
-
NMR study of monomer-dimer equilibrium of barstar in solution
-
Korchuganov D.S., Nolde S.B., Reibarkh M.Y., Orekhov V.Y., Schulga A.A., Ermolyuk Y.S., Kirpichnikov M.P., Arseniev A.S. NMR study of monomer-dimer equilibrium of barstar in solution. J Am Chem Soc. 123:2001;2068-2069.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 2068-2069
-
-
Korchuganov, D.S.1
Nolde, S.B.2
Reibarkh, M.Y.3
Orekhov, V.Y.4
Schulga, A.A.5
Ermolyuk, Y.S.6
Kirpichnikov, M.P.7
Arseniev, A.S.8
-
63
-
-
0035925113
-
Structural and dynamic analysis of residual dipolar coupling data for proteins
-
Tolman J.R., Al-Hashimi H.M., Kay L.E., Prestegard J.H. Structural and dynamic analysis of residual dipolar coupling data for proteins. J Am Chem Soc. 123:2001;1416-1424.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 1416-1424
-
-
Tolman, J.R.1
Al-Hashimi, H.M.2
Kay, L.E.3
Prestegard, J.H.4
-
64
-
-
0034820148
-
Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins
-
Meiler J., Prompers J.J., Peti W., Griesinger C., Brüschweiler R. Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins. J Am Chem Soc. 123:2001;6098-6107.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 6098-6107
-
-
Meiler, J.1
Prompers, J.J.2
Peti, W.3
Griesinger, C.4
Brüschweiler, R.5
-
65
-
-
0037157093
-
Model-free analysis of protein backbone motion from residual dipolar couplings
-
Peti W., Meiler J., Brüschweiler R., Griesinger C. Model-free analysis of protein backbone motion from residual dipolar couplings. J Am Chem Soc. 124:2002;5822-5833.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 5822-5833
-
-
Peti, W.1
Meiler, J.2
Brüschweiler, R.3
Griesinger, C.4
|