-
1
-
-
21244440196
-
Conservation of μs-ms enzyme motions in the apo- and substrate-mimicked state
-
Beach H., Cole R., Gill M., and Loria J.P. Conservation of μs-ms enzyme motions in the apo- and substrate-mimicked state. J. Am. Chem. Soc. 127 (2005) 9167-9176
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 9167-9176
-
-
Beach, H.1
Cole, R.2
Gill, M.3
Loria, J.P.4
-
2
-
-
0041866694
-
Mapping chemical exchange in proteins with MW >50 kD
-
Wang C., Rance M., and Palmer A.G. Mapping chemical exchange in proteins with MW >50 kD. J. Am. Chem. Soc. 125 (2003) 8968-8969
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 8968-8969
-
-
Wang, C.1
Rance, M.2
Palmer, A.G.3
-
4
-
-
0037076522
-
Evidence for flexibility in the function of ribonuclease A
-
Cole R., and Loria J.P. Evidence for flexibility in the function of ribonuclease A. Biochemistry 41 (2002) 6072-6081
-
(2002)
Biochemistry
, vol.41
, pp. 6072-6081
-
-
Cole, R.1
Loria, J.P.2
-
5
-
-
0034945906
-
Functional dynamics in the active site of the ribonuclease binase
-
Wang L., Pang Y., Holder T., Brender J.R., Kurochkin A.V., and Zuiderweg E.R. Functional dynamics in the active site of the ribonuclease binase. Proc. Natl. Acad. Sci. USA 98 (2001) 7684-7689
-
(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.6
-
6
-
-
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., and 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
-
7
-
-
0032517325
-
Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in predeuterated proteins: application to HIV-1 protease
-
Ishima R., Wingfield P.T., Stahl S.J., Kaufman J.D., and Torchia D.A. Using amide 1H and 15N transverse relaxation to detect millisecond time-scale motions in predeuterated proteins: application to HIV-1 protease. J. Am. Chem. Soc. 120 (1998) 10534-10542
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 10534-10542
-
-
Ishima, R.1
Wingfield, P.T.2
Stahl, S.J.3
Kaufman, J.D.4
Torchia, D.A.5
-
8
-
-
0035930026
-
Slow dynamics in folded and unfolded states of an SH3 domain
-
Tollinger M., Skrynnikov N.R., Mulder F.A., Forman-Kay J.D., and Kay L.E. Slow dynamics in folded and unfolded states of an SH3 domain. J. Am. Chem. Soc. 123 (2001) 11341-11352
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 11341-11352
-
-
Tollinger, M.1
Skrynnikov, N.R.2
Mulder, F.A.3
Forman-Kay, J.D.4
Kay, L.E.5
-
9
-
-
0034730994
-
Molecular motions and protein folding: characterization of the backbone dynamics and folding equilibrium of alpha D-2 using C-13 NMR spin relaxation
-
Hill R.B., Bracken C., DeGrado W.F., and Palmer A.G. Molecular motions and protein folding: characterization of the backbone dynamics and folding equilibrium of alpha D-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
-
10
-
-
3242880292
-
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
-
Korzhnev D.M., Salvatella X., Vendruscolo M., Di Nardo A.A., Davidson A.R., Dobson C.M., and Kay L.E. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature 430 (2004) 586-590
-
(2004)
Nature
, vol.430
, pp. 586-590
-
-
Korzhnev, D.M.1
Salvatella, X.2
Vendruscolo, M.3
Di Nardo, A.A.4
Davidson, A.R.5
Dobson, C.M.6
Kay, L.E.7
-
11
-
-
0033607727
-
Characterization of millisecond time-scale dynamics in the molten globule state of alpha-lactalbumin by NMR
-
Kim S., Bracken C., and Baum J. Characterization of millisecond time-scale dynamics in the molten globule state of alpha-lactalbumin by NMR. J. Mol. Biol. 294 (1999) 551-560
-
(1999)
J. Mol. Biol.
, vol.294
, pp. 551-560
-
-
Kim, S.1
Bracken, C.2
Baum, J.3
-
12
-
-
0036815758
-
NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis
-
Akke M. NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis. Curr. Opin. Struct. Biol. 12 (2002) 642-647
-
(2002)
Curr. Opin. Struct. Biol.
, vol.12
, pp. 642-647
-
-
Akke, M.1
-
13
-
-
0141791271
-
Direct observation of protein-ligand interaction kinetics
-
Mittag T., Schaffhausen B., and Gunther U.L. Direct observation of protein-ligand interaction kinetics. Biochemistry 42 (2003) 11128-11136
-
(2003)
Biochemistry
, vol.42
, pp. 11128-11136
-
-
Mittag, T.1
Schaffhausen, B.2
Gunther, U.L.3
-
14
-
-
4644273901
-
-
Downing A.K. (Ed), Humana Press, Totowa
-
Kempf J.G., and Loria J.P. In: Downing A.K. (Ed). Protein NMR Techniques (2004), Humana Press, Totowa 185-231
-
(2004)
Protein NMR Techniques
, pp. 185-231
-
-
Kempf, J.G.1
Loria, J.P.2
-
15
-
-
16244365477
-
Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems
-
Palmer A.G., Grey M.J., and Wang C. Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems. Methods Enzymol. 394 (2005) 430-465
-
(2005)
Methods Enzymol.
, vol.394
, pp. 430-465
-
-
Palmer, A.G.1
Grey, M.J.2
Wang, C.3
-
16
-
-
33644580506
-
Nuclear transfer effects in nuclear magnetic resonance pulse experiments
-
Woessner D.E. Nuclear transfer effects in nuclear magnetic resonance pulse experiments. J. Chem. Phys. 35 (1961) 41-48
-
(1961)
J. Chem. Phys.
, vol.35
, pp. 41-48
-
-
Woessner, D.E.1
-
17
-
-
33645951116
-
Some steady state and spin echo NMR studies at varied temperatures
-
Reeves L.W., and Wells E.J. Some steady state and spin echo NMR studies at varied temperatures. Disc. Faraday Soc. 34 (1962) 177-184
-
(1962)
Disc. Faraday Soc.
, vol.34
, pp. 177-184
-
-
Reeves, L.W.1
Wells, E.J.2
-
18
-
-
36849127400
-
Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution-order of the reaction with respect to solvent
-
Luz Z., and Meiboom S. Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution-order of the reaction with respect to solvent. J. Chem. Phys. 39 (1963) 366-370
-
(1963)
J. Chem. Phys.
, vol.39
, pp. 366-370
-
-
Luz, Z.1
Meiboom, S.2
-
19
-
-
0014023143
-
Nuclear magnetic resonance methods for determining chemical-exchange rates
-
Allerhand A., Gutowsky H.S., Jonas J., and Meinzer R.A. Nuclear magnetic resonance methods for determining chemical-exchange rates. J. Am. Chem. Soc. 88 (1966) 3185-3193
-
(1966)
J. Am. Chem. Soc.
, vol.88
, pp. 3185-3193
-
-
Allerhand, A.1
Gutowsky, H.S.2
Jonas, J.3
Meinzer, R.A.4
-
20
-
-
0000555643
-
Spin-echo studies of chemical exchange. II. Closed formulas for two sites
-
Allerhand A., and Gutowsky H.S. Spin-echo studies of chemical exchange. II. Closed formulas for two sites. J. Chem. Phys. 42 (1965) 1587-1599
-
(1965)
J. Chem. Phys.
, vol.42
, pp. 1587-1599
-
-
Allerhand, A.1
Gutowsky, H.S.2
-
23
-
-
0001766423
-
2 relaxation-the multisite case
-
2 relaxation-the multisite case. J. Magn. Reson. 30 (1978) 111-128
-
(1978)
J. Magn. Reson.
, vol.30
, pp. 111-128
-
-
Jen, J.1
-
24
-
-
0345306309
-
Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling
-
Grey M.J., Wang C., and Palmer III A.G. Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling. J. Am. Chem. Soc. 125 (2003) 14324-14335
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 14324-14335
-
-
Grey, M.J.1
Wang, C.2
Palmer III, A.G.3
-
25
-
-
0032871220
-
Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution
-
Ishima R., and Torchia D.A. Estimating the time scale of chemical exchange of 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
-
26
-
-
0034728579
-
The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
-
Millet O.M., Loria J.P., Kroenke C.D., Pons M., and Palmer A.G. The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 122 (2000) 2867-2877
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 2867-2877
-
-
Millet, O.M.1
Loria, J.P.2
Kroenke, C.D.3
Pons, M.4
Palmer, A.G.5
-
27
-
-
0034759979
-
Studying excited states of proteins by NMR spectroscopy
-
Mulder F.A., Mittermaier A., Hon B., Dahlquist F.W., and Kay L.E. Studying excited states of proteins by NMR spectroscopy. Nat. Struct. Biol. 8 (2001) 932-935
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 932-935
-
-
Mulder, F.A.1
Mittermaier, A.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
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