-
1
-
-
0041852853
-
The role of dynamics in enzyme activity
-
DOI 10.1146/annurev.biophys.32.110601.142445
-
Daniel, R. M., Dunn, R. V., Finney, J. L., and Smith, J. C. (2003) The role of dynamics in enzyme activity. Annu. Rev. Biophys. Biomol. Struct. 32, 69-92. (Pubitemid 37056222)
-
(2003)
Annual Review of Biophysics and Biomolecular Structure
, vol.32
, pp. 69-92
-
-
Daniel, R.M.1
Dunn, R.V.2
Finney, J.L.3
Smith, J.C.4
-
2
-
-
27744499156
-
Intrinsic dynamics of an enzyme underlies catalysis
-
DOI 10.1038/nature04105, PII N04105
-
Eisenmesser, E. Z., Millet, O., Labeikovsky, W., Korzhnev, D. M., Wolf-Watz, M., Bosco, D. A., Skalicky, J. J., Kay, L. E., and Kern, D. (2005) Intrinsic dynamics of an enzyme underlies catalysis. Nature 438, 117-121. (Pubitemid 41599831)
-
(2005)
Nature
, vol.438
, Issue.7064
, pp. 117-121
-
-
Eisenmesser, E.Z.1
Millet, O.2
Labeikovsky, W.3
Korzhnev, D.M.4
Wolf-Watz, M.5
Bosco, D.A.6
Skalicky, J.J.7
Kay, L.E.8
Kern, D.9
-
3
-
-
33644556820
-
Enzyme dynamics along the reaction coordinate: Critical role of a conserved residue
-
Kovrigin, E. L., and Loria, J. P. (2006) Enzyme dynamics along the reaction coordinate: critical role of a conserved residue. Biochemistry 45, 2636-2647.
-
(2006)
Biochemistry
, vol.45
, pp. 2636-2647
-
-
Kovrigin, E.L.1
Loria, J.P.2
-
4
-
-
33748781457
-
The dynamic energy landscape of dihydrofolate reductase catalysis
-
DOI 10.1126/science.1130258
-
Boehr, D. D., McElheny, D., Dyson, H. J., and Wright, P. E. (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638-1642. (Pubitemid 44414038)
-
(2006)
Science
, vol.313
, Issue.5793
, pp. 1638-1642
-
-
Boehr, D.D.1
McElheny, D.2
Dyson, H.J.3
Wrightt, P.E.4
-
5
-
-
0024295023
-
Triosephosphate isomerase catalysis is diffusion controlled
-
Blacklow, S. C., Raines, R. T., Lim, W. A., Zamore, P. D., and Knowles, J. R. (1988) Triosephosphate isomerase catalysis is diffusion controlled. Biochemistry 27, 1158-1167.
-
(1988)
Biochemistry
, vol.27
, pp. 1158-1167
-
-
Blacklow, S.C.1
Raines, R.T.2
Lim, W.A.3
Zamore, P.D.4
Knowles, J.R.5
-
6
-
-
1442277682
-
Computational Modeling of the Catalytic Reaction in Triosephosphate Isomerase
-
DOI 10.1016/j.jmb.2003.11.016
-
Guallar, V., Jacobson, M., McDermott, A., and Friesner, R. A. (2004) Computational modeling of the catalytic reaction in triosephosphate isomerase. J. Mol. Biol. 337, 227-239. (Pubitemid 38270259)
-
(2004)
Journal of Molecular Biology
, vol.337
, Issue.1
, pp. 227-239
-
-
Guallar, V.1
Jacobson, M.2
McDermott, A.3
Friesner, R.A.4
-
7
-
-
0037422593
-
Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution
-
DOI 10.1073/pnas.0233793100
-
Jogl, G., Rozovsky, S., McDermott, A. E., and Tong, L. (2003) Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 100, 50-55. (Pubitemid 36078028)
-
(2003)
Proceedings of the National Academy of Sciences of the United States of America
, vol.100
, Issue.1
, pp. 50-55
-
-
Jogl, G.1
Rozovsky, S.2
McDermott, A.E.3
Tong, L.4
-
8
-
-
0025015392
-
Anatomy of a conformational change: Hinged 'lid' motion of the triosephosphate isomerase loop
-
Joseph, D., Petsko, G. A., and Karplus, M. (1990) Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science 249, 1425-1428. (Pubitemid 20341906)
-
(1990)
Science
, vol.249
, Issue.4975
, pp. 1425-1428
-
-
Joseph, D.1
Petsko, G.A.2
Karplus, M.3
-
9
-
-
0035967856
-
Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
-
DOI 10.1006/jmbi.2001.4673
-
Rozovsky, S., Jogl, G., Tong, L., and McDermott, A. E. (2001) Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310, 271-280. (Pubitemid 32619968)
-
(2001)
Journal of Molecular Biology
, vol.310
, Issue.1
, pp. 271-280
-
-
Rozovsky, S.1
Jogl, G.2
Tong, L.3
McDermott, A.E.4
-
10
-
-
0026779802
-
Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase
-
Sampson, N. S., and Knowles, J. R. (1992) Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. Biochemistry 31, 8482-8487.
-
(1992)
Biochemistry
, vol.31
, pp. 8482-8487
-
-
Sampson, N.S.1
Knowles, J.R.2
-
11
-
-
0038169722
-
Relaxation spectra of ribonuclease. I. The interaction of ribonuclease with cytidine 3′-phosphate
-
Cathou, R. E., and Hammes, G. G. (1965) Relaxation spectra of ribonuclease. I. The interaction of ribonuclease with cytidine 3′-phosphate. J. Am. Chem. Soc. 87, 3240-3245.
-
(1965)
J. Am. Chem. Soc.
, vol.87
, pp. 3240-3245
-
-
Cathou, R.E.1
Hammes, G.G.2
-
12
-
-
0013843341
-
Relaxation spectra of ribonuclease. III. Further investigation of the interaction of ribonuclease and cytidine 3′-phosphate
-
Cathou, R. E., and Hammes, G. G. (1965) Relaxation spectra of ribonuclease. III. Further investigation of the interaction of ribonuclease and cytidine 3′-phosphate. J. Am. Chem. Soc. 87, 4674-4680.
-
(1965)
J. Am. Chem. Soc.
, vol.87
, pp. 4674-4680
-
-
Cathou, R.E.1
Hammes, G.G.2
-
13
-
-
0037076522
-
Evidence for flexibility in the function of ribonuclease A
-
DOI 10.1021/bi025655m
-
Cole, R., and Loria, J. P. (2002) Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072-6081. (Pubitemid 34498913)
-
(2002)
Biochemistry
, vol.41
, Issue.19
, pp. 6072-6081
-
-
Cole, R.1
Loria, J.P.2
-
14
-
-
0028322323
-
The occupancy of two distinct conformations by active-site histidine-119 in crystals of ribonuclease is modulated by pH
-
DOI 10.1016/0014-5793(94)00664-4
-
de Mel, V. S., Doscher, M. S., Martin, P. D., and Edwards, B. F. (1994) The occupancy of two distinct conformations by active-site histidine-119 in crystals of ribonuclease is modulated by pH. FEBS Lett. 349, 155-160. (Pubitemid 24230241)
-
(1994)
FEBS Letters
, vol.349
, Issue.1
, pp. 155-160
-
-
Doscher, M.S.1
-
15
-
-
0032550648
-
Structure of the ribonuclease-uridine - Vanadate transition state analogue complex by Raman difference spectroscopy: Mechanistic implications
-
DOI 10.1021/ja972824v
-
Deng, H., Brugner, J. W., and Callender, R. (1998) Structure of the ribonuclease-uridine-vanadate transition state analogue complex by raman difference spectroscopy: mechanistic implications. J. Am. Chem. Soc. 120, 4717-4722. (Pubitemid 28282724)
-
(1998)
Journal of the American Chemical Society
, vol.120
, Issue.19
, pp. 4717-4722
-
-
Deng, H.1
Burgner II, J.W.2
Callender, R.H.3
-
16
-
-
0014007150
-
Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2′:3′-cyclic phosphate
-
Erman, J. E., and Hammes, G. G. (1966) Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2′:3′-cyclic phosphate. J. Am. Chem. Soc. 88, 5607-5614.
-
(1966)
J. Am. Chem. Soc.
, vol.88
, pp. 5607-5614
-
-
Erman, J.E.1
Hammes, G.G.2
-
17
-
-
0014007134
-
Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3′:5′-cytidine
-
Erman, J. E., and Hammes, G. G. (1966) Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3′: 5′-cytidine. J. Am. Chem. Soc. 88, 5614-5617.
-
(1966)
J. Am. Chem. Soc.
, vol.88
, pp. 5614-5617
-
-
Erman, J.E.1
Hammes, G.G.2
-
18
-
-
0013843367
-
Relaxation spectra of ribonuclease. II. Isomerization of ribonuclease at neutral pH values
-
French, T. C., and Hammes, G. G. (1965) Relaxation spectra of ribonuclease. II. Isomerization of ribonuclease at neutral pH values. J. Am. Chem. Soc. 87, 4669-4673.
-
(1965)
J. Am. Chem. Soc.
, vol.87
, pp. 4669-4673
-
-
French, T.C.1
Hammes, G.G.2
-
19
-
-
0015523041
-
Conformational states of bovine pancreatic ribonuclease A observed by normal and partially relaxed carbon 13 nuclear magnetic resonance
-
Glushko, V., Lawson, P. J., and Gurd, F. R. N. (1972) Conformational states of bovine pancreatic ribonuclease A observed by normal and partially relaxed carbon 13 nuclear magnetic resonance. J. Biol. Chem. 247, 3176-3185.
-
(1972)
J. Biol. Chem.
, vol.247
, pp. 3176-3185
-
-
Glushko, V.1
Lawson, P.J.2
Gurd, F.R.N.3
-
20
-
-
4243195831
-
Relaxation spectra of ribonuclease. VI. Interaction of ribonuclease with uridine 3′-monophosphate
-
Hammes, G. G., and Walz, F. G. (1969) Relaxation spectra of ribonuclease. VI. Interaction of ribonuclease with uridine 3′-monophosphate. J. Am. Chem. Soc. 91, 7179-7186.
-
(1969)
J. Am. Chem. Soc.
, vol.91
, pp. 7179-7186
-
-
Hammes, G.G.1
Walz, F.G.2
-
21
-
-
0021765928
-
Ribonuclease A: Carbon-13 nuclear magnetic resonance assignments, binding sites, and conformational flexibility
-
Howarth, O. W., and Lian, L. Y. (1984) Ribonuclease A: carbon-13 nuclear magnetic resonance assignments, binding sites, and conformational flexibility. Biochemistry 23, 3515-3521.
-
(1984)
Biochemistry
, vol.23
, pp. 3515-3521
-
-
Howarth, O.W.1
Lian, L.Y.2
-
23
-
-
0142210123
-
High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors
-
DOI 10.1110/ps.03196603
-
Leonidas, D. D., Chavali, G. B., Oikonomakos, N. G., Chrysina, E. D., Kosmopoulou, M. N., Vlassi, M., Frankling, C., and Acharya,K. R. (2003) High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors. Protein Sci. 12, 2559-2574. (Pubitemid 37310795)
-
(2003)
Protein Science
, vol.12
, Issue.11
, pp. 2559-2574
-
-
Leonidas, D.D.1
Chavali, G.B.2
Oikonomakos, N.G.3
Chrysina, E.D.4
Kosmopoulou, M.N.5
Vlassi, M.6
Frankling, C.7
Acahrya, K.R.8
-
24
-
-
0030917539
-
Crystal structures of ribonuclease a complexes with 5'- diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 Å resolution
-
DOI 10.1021/bi9700330
-
Leonidas, D. D., Shapiro, R., Irons, L. I., Russo, N., and Acharya, K. R. (1997) Crystal structures of ribonuclease A complexes with 5′- diphosphoadenosine 30-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 Å resolution. Biochemistry 36, 5578-5588. (Pubitemid 27200056)
-
(1997)
Biochemistry
, vol.36
, Issue.18
, pp. 5578-5588
-
-
Leonidas, D.D.1
Shapiro, R.2
Irons, L.I.3
Russo, N.4
Acharya, K.R.5
-
25
-
-
0016743108
-
Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. II. pH and inhibitor-induced conformational transitions affecting histidine-48 and one tyrosine residue of ribonuclease A
-
Markley, J. L. (1975) Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. II. pH and inhibitor-induced conformational transitions affecting histidine-48 and one tyrosine residue of ribonuclease A. Biochemistry 14, 3554-3561.
-
(1975)
Biochemistry
, vol.14
, pp. 3554-3561
-
-
Markley, J.L.1
-
26
-
-
0026606219
-
Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K
-
Tilton, R. F., Dewan, J. C., and Petsko, G. A. (1992) Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K. Biochemistry 31, 2469-2481.
-
(1992)
Biochemistry
, vol.31
, pp. 2469-2481
-
-
Tilton, R.F.1
Dewan, J.C.2
Petsko, G.A.3
-
27
-
-
33745380088
-
Characterization of the transition state of functional enzyme dynamics
-
DOI 10.1021/ja061435a
-
Kovrigin, E. L., and Loria, J. P. (2006) Characterization of the transition state of functional enzyme dynamics. J. Am. Chem. Soc. 128, 7724-7725. (Pubitemid 43945700)
-
(2006)
Journal of the American Chemical Society
, vol.128
, Issue.24
, pp. 7724-7725
-
-
Kovrigin, E.L.1
Loria, J.P.2
-
28
-
-
34547524047
-
The mechanism of rate-limiting motions in enzyme function
-
DOI 10.1073/pnas.0702551104
-
Watt, E. D., Shimada, H., Kovrigin, E. L., and Loria, J. P. (2007) The mechanism of rate-limiting motions in enzyme function. Proc. Natl. Acad. Sci. U.S.A. 104, 11981-11986. (Pubitemid 47185616)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.29
, pp. 11981-11986
-
-
Watt, E.D.1
Shimada, H.2
Kovrigin, E.L.3
Loria, J.P.4
-
29
-
-
21244440196
-
Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state
-
DOI 10.1021/ja0514949
-
Beach, H., Cole, R., Gill, M., and Loria, J. P. (2005) Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state. J. Am. Chem. Soc. 127, 9167-9176. (Pubitemid 40897609)
-
(2005)
Journal of the American Chemical Society
, vol.127
, Issue.25
, pp. 9167-9176
-
-
Beach, H.1
Cole, R.2
Gill, M.L.3
Loria, J.P.4
-
30
-
-
0038219675
-
Temperature dependence of the backbone dynamics of ribonuclease A in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′)pyrophosphate adenosine 3′-phosphate
-
DOI 10.1021/bi034027h
-
Kovrigin, E. L., Cole, R., and Loria, J. P. (2003) Temperature dependence of the backbone dynamics of ribonuclease A in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′) pyrophosphate adenosine 3′-phosphate. Biochemistry 42, 5279-5291. (Pubitemid 36560424)
-
(2003)
Biochemistry
, vol.42
, Issue.18
, pp. 5279-5291
-
-
Kovrigin, E.L.1
Cole, R.2
Loria, J.P.3
-
31
-
-
0032503565
-
Structure (1.3 Å) and charge states of ribonuclease A-uridine vanadate complex: Implications for the phosphate ester hydrolysis mechanism
-
Wladkowski, B. D., Svensson, L. A., Sjolin, L., Ladner, J. E., and Gilliland, G. L. (1998) Structure (1.3 Å) and charge states of ribonuclease A-uridine vanadate complex: implications for the phosphate ester hydrolysis mechanism. J. Am. Chem. Soc. 120, 5488-5498.
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 5488-5498
-
-
Wladkowski, B.D.1
Svensson, L.A.2
Sjolin, L.3
Ladner, J.E.4
Gilliland, G.L.5
-
32
-
-
0024291642
-
Structure of phosphate-free ribonuclease A refined at 1.26 Å
-
Wlodawer, A., Svensson, L. A., Sjolin, L., and Gilliland, G. L. (1988) Structure of phosphate-free ribonuclease A refined at 1.26 Å. Biochemistry 27, 2705-2717.
-
(1988)
Biochemistry
, vol.27
, pp. 2705-2717
-
-
Wlodawer, A.1
Svensson, L.A.2
Sjolin, L.3
Gilliland, G.L.4
-
33
-
-
0034725562
-
Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 angstrom resolution
-
Mallorqui-Fernandez, G., Pous, J., Peracaula, R., Aymami, J., Maeda, T., Tada, H., Yamada, H., Seno, M., de Llorens, R., Gomis-Ruth, F. X., and Coll, M. (2000) Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 angstrom resolution. J. Mol. Biol. 300, 1297-1307.
-
(2000)
J. Mol. Biol.
, vol.300
, pp. 1297-1307
-
-
Mallorqui-Fernandez, G.1
Pous, J.2
Peracaula, R.3
Aymami, J.4
Maeda, T.5
Tada, H.6
Yamada, H.7
Seno, M.8
De Llorens, R.9
Gomis-Ruth, F.X.10
Coll, M.11
-
34
-
-
0037044330
-
The crystal structure of eosinophil cationic protein in complex with 2′,5′-ADP at 2.0 Åresolution reveals the details of the ribonucleolytic active site
-
Mohan, C. G., Boix, E., Evans, H. R., Nikolovski, Z., Nogues, M. V., Cuchillo, C. M., and Acharya, K. R. (2002) The crystal structure of eosinophil cationic protein in complex with 2′,5′-ADP at 2.0 Åresolution reveals the details of the ribonucleolytic active site. Biochemistry 41, 12100-12106.
-
(2002)
Biochemistry
, vol.41
, pp. 12100-12106
-
-
Mohan, C.G.1
Boix, E.2
Evans, H.R.3
Nikolovski, Z.4
Nogues, M.V.5
Cuchillo, C.M.6
Acharya, K.R.7
-
35
-
-
0036137008
-
Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease a as revealed by crystallographic study of three Phe 120 mutants at 1.4 Å resolution
-
DOI 10.1110/ps.ps.31102
-
Chatani, E., Hayashi, R., Moriyama, H., and Ueki, T. (2002) Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 Å resolution. Protein Sci. 11, 72-81. (Pubitemid 34024759)
-
(2002)
Protein Science
, vol.11
, Issue.1
, pp. 72-81
-
-
Chatani, E.1
Hayashi, R.2
Moriyama, H.3
Ueki, T.4
-
36
-
-
33747829924
-
Expresso: Automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee
-
DOI 10.1093/nar/gkl092
-
Armougom, F., Moretti, S., Poirot, O., Audic, S., Dumas, P., Schaeli, B., Keduas, V., and Notredame, C. (2006) Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-coffee. Nucleic Acids Res. 34, W604-W608. (Pubitemid 44529841)
-
(2006)
Nucleic Acids Research
, vol.34
, Issue.WEB. SERV. ISS.
-
-
Armougom, F.1
Moretti, S.2
Poirot, O.3
Audic, S.4
Dumas, P.5
Schaeli, B.6
Keduas, V.7
Notredame, C.8
Notredame, C.9
-
37
-
-
0034725562
-
Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 Åresolution
-
Mallorqui-Fernandez, G., Pous, J., Peracaula, R., Aymami, J., Maeda, T., Tada, H., Yamada, H., Seno, M., de Llorens, R., Gomis-Ruth, F. X., and Coll, M. (2000) Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 Åresolution. J. Mol. Biol. 300, 1297-1307.
-
(2000)
J. Mol. Biol.
, vol.300
, pp. 1297-1307
-
-
Mallorqui-Fernandez, G.1
Pous, J.2
Peracaula, R.3
Aymami, J.4
Maeda, T.5
Tada, H.6
Yamada, H.7
Seno, M.8
De Llorens, R.9
Gomis-Ruth, F.X.10
Coll, M.11
-
38
-
-
0037066104
-
Atomic resolution (0.98 Å) structure of eosinophil-derived neurotoxin
-
DOI 10.1021/bi015911f
-
Swaminathan, G. J., Holloway, D. E., Veluraja, K., and Acharya, K. R. (2002) Atomic resolution (0.98 Å) structure of eosinophil-derived neurotoxin. Biochemistry 41, 3341-3352. (Pubitemid 34214032)
-
(2002)
Biochemistry
, vol.41
, Issue.10
, pp. 3341-3352
-
-
Swaminathan, G.J.1
Holloway, D.E.2
Veluraja, K.3
Acharya, K.R.4
-
39
-
-
0029032586
-
Engineering ribonuclease A: Production, purification and characterization of wild-type enzyme and mutants at Gln11
-
delCardayre, S. B., Ribo, M., Yokel, E. M., Quirk, D. J., Rutter, W. J., and Raines, R. T. (1995) Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 8, 261-273.
-
(1995)
Protein Eng.
, vol.8
, pp. 261-273
-
-
DelCardayre, S.B.1
Ribo, M.2
Yokel, E.M.3
Quirk, D.J.4
Rutter, W.J.5
Raines, R.T.6
-
40
-
-
49749180154
-
Some spectrophotometric and polarimetric experiments with ribonuclease
-
Sela, M., and Anfinsen, C. B. (1957) Some spectrophotometric and polarimetric experiments with ribonuclease. Biochim. Biophys. Acta 24, 229-235.
-
(1957)
Biochim. Biophys. Acta
, vol.24
, pp. 229-235
-
-
Sela, M.1
Anfinsen, C.B.2
-
41
-
-
85013746467
-
-
Elsevier Academic, San Diego, CA
-
Cavanagh, J., Fairbrother, W. J., Palmer, A. G., Rance, M., and Skelton, N. J. (2007) Protein NMR Spectroscopy: Principles and Practice, Elsevier Academic, San Diego, CA.
-
(2007)
Protein NMR Spectroscopy: Principles and Practice
-
-
Cavanagh, J.1
Fairbrother, W.J.2
Palmer, A.G.3
Rance, M.4
Skelton, N.J.5
-
42
-
-
44949282610
-
Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy
-
Cavanagh, J., Palmer, A. G., Wright, P. E., and Rance, M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy. J. Magn. Reson. 91, 429-436.
-
(1991)
J. Magn. Reson.
, vol.91
, pp. 429-436
-
-
Cavanagh, J.1
Palmer, A.G.2
Wright, P.E.3
Rance, M.4
-
43
-
-
44949289665
-
Sensitivity improvement in isotropic mixing (TOCSY) experiments
-
Cavanagh, J., and Rance, M. (1990) Sensitivity improvement in isotropic mixing (TOCSY) experiments. J. Magn. Reson. 88, 72-85.
-
(1990)
J. Magn. Reson.
, vol.88
, pp. 72-85
-
-
Cavanagh, J.1
Rance, M.2
-
44
-
-
0006925492
-
Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
-
Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 10663-10665
-
-
Kay, L.E.1
Keifer, P.2
Saarinen, T.3
-
45
-
-
44949276869
-
Sensitivity improvement in proton-detected two-dimensional heteronuclear correlationNMRspectroscopy
-
Palmer, A. G., Cavanagh, J., Wright, P. E., and Rance, M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlationNMRspectroscopy. J. Magn. Reson. 93, 151-170.
-
(1991)
J. Magn. Reson.
, vol.93
, pp. 151-170
-
-
Palmer, A.G.1
Cavanagh, J.2
Wright, P.E.3
Rance, M.4
-
46
-
-
0033577288
-
A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
-
DOI 10.1021/ja983961a
-
Loria, J. P., Rance, M., and Palmer, A. G. (1999) A Relaxation- compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121, 2331-2332. (Pubitemid 29152458)
-
(1999)
Journal of the American Chemical Society
, vol.121
, Issue.10
, pp. 2331-2332
-
-
Loria, J.P.1
Rance, M.2
Palmer III, A.G.3
-
47
-
-
0035819455
-
15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
-
DOI 10.1021/ja003447g
-
Mulder, F. A., Skrynnikov, N. R., Hon, B., Dahlquist, F. W., and Kay, L. E. (2001) Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J. Am. Chem. Soc. 123, 967-975. (Pubitemid 32151376)
-
(2001)
Journal of the American Chemical Society
, vol.123
, Issue.5
, pp. 967-975
-
-
Mulder, F.A.A.1
Skrynnikov, N.R.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
48
-
-
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. (1963) 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, 366-370.
-
(1963)
J. Chem. Phys.
, vol.39
, pp. 366-370
-
-
Luz, Z.1
Meiboom, S.2
-
49
-
-
0034728579
-
The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale
-
DOI 10.1021/ja993511y
-
Millet, O. M., Loria, J. P., Kroenke, C. D., Pons, M., and Palmer, A. G. (2000) The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 122, 2867-2877. (Pubitemid 30191047)
-
(2000)
Journal of the American Chemical Society
, vol.122
, Issue.12
, pp. 2867-2877
-
-
Millet, O.1
Loria, J.P.2
Kroenke, C.D.3
Pons, M.4
Palmer III, A.G.5
-
50
-
-
0033788347
-
Differential multiple-quantum relaxation arising from cross-correlated time-modulation of isotropic chemical shifts
-
Kloiber, K., and Konrat, R. (2000) Differential multiple-quantum relaxation arising from cross-correlated time-modulation of isotropic chemical shifts. J. Biomol. NMR 18, 33-42.
-
(2000)
J. Biomol. NMR
, vol.18
, pp. 33-42
-
-
Kloiber, K.1
Konrat, R.2
-
51
-
-
0028564999
-
The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules
-
Zegers, I., Maes, D., Dao-Thi, M. H., Poortmans, F., Palmer, R., and Wyns, L. (1994) The structures of RNase A complexed with 3′-CMP and d(CpA): active site conformation and conserved water molecules. Protein Sci. 3, 2322-2339.
-
(1994)
Protein Sci.
, vol.3
, pp. 2322-2339
-
-
Zegers, I.1
Maes, D.2
Dao-Thi, M.H.3
Poortmans, F.4
Palmer, R.5
Wyns, L.6
-
52
-
-
0029795040
-
The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR
-
DOI 10.1021/bi9611164
-
Grzesiek, S., Stahl, S. J., Wingfield, P. T., and Bax, A. (1996) The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry 35, 10256-10261. (Pubitemid 26277283)
-
(1996)
Biochemistry
, vol.35
, Issue.32
, pp. 10256-10261
-
-
Grzesiek, S.1
Stahl, S.J.2
Wingfield, P.T.3
Bax, A.4
-
53
-
-
0013843303
-
Equilibrium measurements of the binding of cytidine 3′-phosphate to ribonuclease
-
Hammes, G. G., and Schimmel, P. R. (1965) Equilibrium measurements of the binding of cytidine 3′-phosphate to ribonuclease. J. Am. Chem. Soc. 87, 4665-4669.
-
(1965)
J. Am. Chem. Soc.
, vol.87
, pp. 4665-4669
-
-
Hammes, G.G.1
Schimmel, P.R.2
-
54
-
-
0037378779
-
Catalysis by ribonuclease a is limited by the rate of substrate association
-
DOI 10.1021/bi026076k
-
Park, C., and Raines, R. T. (2003) Catalysis by ribonuclease A is limited by the rate of substrate association. Biochemistry 42, 3509-3518. (Pubitemid 36368645)
-
(2003)
Biochemistry
, vol.42
, Issue.12
, pp. 3509-3518
-
-
Park, C.1
Raines, R.T.2
-
55
-
-
0029595298
-
Limits to catalysis by ribonuclease A
-
DOI 10.1006/bioo.1995.1033
-
Thompson, J. E., Kutateladze, M. C., Venegas, F. D., Messmore, J. M., and Raines, R. T. (1995) Limits to catalysis by ribonuclease A. Bioorg. Chem. 23, 471-481. (Pubitemid 26027357)
-
(1995)
Bioorganic Chemistry
, vol.23
, Issue.4
, pp. 471-481
-
-
Thompson, J.E.1
Kutateladze, T.G.2
Schuster, M.C.3
Venegas, F.D.4
Messmore, J.M.5
Raines, R.T.6
-
56
-
-
0015207883
-
31PNMR study of the association of uridine-3′- monophosphate to ribonuclease A
-
31PNMR study of the association of uridine-3′-monophosphate to ribonuclease A. Biochem. Biophys. Res. Commun. 43, 142-148.
-
(1971)
Biochem. Biophys. Res. Commun.
, vol.43
, pp. 142-148
-
-
Lee, G.C.1
Chan, S.I.2
-
57
-
-
0001005285
-
Ribonuclease A
-
Raines, R. (1998) Ribonuclease A. Chem. Rev. 98, 1045-1065.
-
(1998)
Chem. Rev.
, vol.98
, pp. 1045-1065
-
-
Raines, R.1
-
58
-
-
0025777309
-
Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenase
-
Gerstein, M., and Chothia, C. (1991) Analysis of protein loop closure: two types of hinges produce one motion in lactate dehydrogenase. J. Mol. Biol. 220, 133-149. (Pubitemid 121004549)
-
(1991)
Journal of Molecular Biology
, vol.220
, Issue.1
, pp. 133-149
-
-
Gerstein, M.1
Chothia, C.2
-
59
-
-
84886621690
-
A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes
-
White, J. L., Hackert, M. L., Buehner, M., Adams, M. J., Ford, G. C., Lentz, P. J. Jr., Smiley, I. E., Steindel, S. J., and Rossmann, M. G. (1976) A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes. J. Mol. Biol. 102, 759-779.
-
(1976)
J. Mol. Biol.
, vol.102
, pp. 759-779
-
-
White, J.L.1
Hackert, M.L.2
Buehner, M.3
Adams, M.J.4
Ford, G.C.5
Lentz Jr., P.J.6
Smiley, I.E.7
Steindel, S.J.8
Rossmann, M.G.9
-
60
-
-
0025995908
-
A hybrid of bovine pancreatic ribonuclease and human angiogenin: An external loop as a module controlling substrate specificity?
-
Allemann, R. K., Presnell, S. R., and Benner, S. A. (1991) A hybrid of bovine pancreatic ribonuclease and human angiogenin: an external loop as a module controlling substrate specificity?. Protein Eng. 4, 831-835.
-
(1991)
Protein Eng.
, vol.4
, pp. 831-835
-
-
Allemann, R.K.1
Presnell, S.R.2
Benner, S.A.3
-
61
-
-
34250366262
-
Engineering the substrate specificity of Staphylococcus aureus sortase A: The beta6/beta7 loop from SrtB confers npqtn recognition to SrtA
-
DOI 10.1074/jbc.M610519200
-
Bentley, M. L., Gaweska, H., Kielec, J. M., and McCafferty, D. G. (2007) Engineering the substrate specificity of Staphylococcurs aureus sortase A - The beta 6/beta 7 loop from SrtB confers NPQTN recognition to SrtA. J. Biol. Chem. 282, 6571-6581. (Pubitemid 47100853)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.9
, pp. 6571-6581
-
-
Bentley, M.L.1
Gaweska, H.2
Kielec, J.M.3
McCafferty, D.G.4
-
63
-
-
0026520387
-
Converting trypsin to chymotrypsin: The role of surface loops
-
Hedstrom, L., Szilagyi, L., and Rutter, W. J. (1992) Converting trypsin to chymotrypsin: the role of surface loops. Science 255, 1249-1253.
-
(1992)
Science
, vol.255
, pp. 1249-1253
-
-
Hedstrom, L.1
Szilagyi, L.2
Rutter, W.J.3
-
64
-
-
23244458844
-
Specificity of trypsin and chymotrypsin: Loop-motion-controlled dynamic correlation as a determinant
-
DOI 10.1529/biophysj.104.057158
-
Ma, W., Tang, C., and Lai, L. (2005) Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant. Biophys. J. 89, 1183-1193. (Pubitemid 41099000)
-
(2005)
Biophysical Journal
, vol.89
, Issue.2
, pp. 1183-1193
-
-
Ma, W.1
Tang, C.2
Lai, L.3
-
65
-
-
34848905895
-
Conformational dynamics in loop swap mutants of homologous fibronectin type III domains
-
DOI 10.1529/biophysj.106.100578
-
Siggers, K., Soto, C., and Palmer, A. G.III (2007) Conformational dynamics in loop swap mutants of homologous fibronectin type III domains. Biophys. J. 93, 2447-2456. (Pubitemid 47511145)
-
(2007)
Biophysical Journal
, vol.93
, Issue.7
, pp. 2447-2456
-
-
Siggers, K.1
Soto, C.2
Palmer III, A.G.3
-
66
-
-
34247180580
-
Sequence-specific dynamics modulate recognition specificity in WW domains
-
DOI 10.1038/nsmb1207, PII NSMB1207
-
Peng, T., Zintsmaster, J. S., Namanja, A. T., and Peng, J. W. (2007) Sequence-specific dynamics modulate recognition specificity in WW domains. Nat. Struct. Mol. Biol. 14, 325-331. (Pubitemid 46608337)
-
(2007)
Nature Structural and Molecular Biology
, vol.14
, Issue.4
, pp. 325-331
-
-
Peng, T.1
Zintsmaster, J.S.2
Namanja, A.T.3
Peng, J.W.4
-
67
-
-
0031984752
-
Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
-
DOI 10.1038/nsb0198-55
-
Akke, M., Liu, J., Cavanagh, J., Erickson, H. P., and Palmer, A. G. (1998) Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat. Struct. Biol. 5, 55-59. (Pubitemid 28048977)
-
(1998)
Nature Structural Biology
, vol.5
, Issue.1
, pp. 55-59
-
-
Akke, M.1
Liu, J.2
Cavanagh, J.3
Erickson, H.P.4
Palmer III, A.G.5
-
68
-
-
34547524047
-
The mechanism of rate-limiting motions in enzyme function
-
DOI 10.1073/pnas.0702551104
-
Watt, E. D., Shimada, H., Kovrigin, E. L., and Loria, J. P. (2007) The mechanism of rate-limiting motions in enzyme function. Proc. Natl. Acad. Sci. U.S.A. 104, 11981-11986. (Pubitemid 47185616)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.29
, pp. 11981-11986
-
-
Watt, E.D.1
Shimada, H.2
Kovrigin, E.L.3
Loria, J.P.4
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