-
2
-
-
33748781457
-
The dynamic energy landscape of dihydrofolate reductase catalysis
-
DOI 10.1126/science.1130258
-
Boehr, D. D., McElheny, D., Dyson, H. J. & Wright, P. E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638-1642 (2006). (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
-
3
-
-
36849048228
-
Intrinsic motions along an enzymatic reaction trajectory
-
DOI 10.1038/nature06410, PII NATURE06410
-
Henzler-Wildman, K. A. et al. Intrinsic motions along an enzymatic reaction trajectory. Nature 450, 838-844 (2007). (Pubitemid 350231334)
-
(2007)
Nature
, vol.450
, Issue.7171
, pp. 838-844
-
-
Henzler-Wildman, K.A.1
Thai, V.2
Lei, M.3
Ott, M.4
Wolf-Watz, M.5
Fenn, T.6
Pozharski, E.7
Wilson, M.A.8
Petsko, G.A.9
Karplus, M.10
Hubner, C.G.11
Kern, D.12
-
4
-
-
0026509036
-
A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene
-
Eriksson, A. E., Baase, W. A., Wozniak, J. A. & Matthews, B. W. A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature 355, 371-373 (1992).
-
(1992)
Nature
, vol.355
, pp. 371-373
-
-
Eriksson, A.E.1
Baase, W.A.2
Wozniak, J.A.3
Matthews, B.W.4
-
5
-
-
0034759979
-
Studying excited states of proteins by NMR spectroscopy
-
DOI 10.1038/nsb1101-932
-
Mulder, F. A.A., Mittermaier, A.,Hon, B.,Dahlquist, F. W.&Kay, L. E. Studyingexcited states of protein by NMR spectroscopy. Nature Struct. Biol. 8, 932-935 (2001). (Pubitemid 33032360)
-
(2001)
Nature Structural Biology
, vol.8
, Issue.11
, pp. 932-935
-
-
Mulder, F.A.A.1
Mittermaier, A.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
6
-
-
0034919305
-
Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
-
DOI 10.1016/S0076-6879(01)39315-1
-
Palmer, A. G., Kroenke, C. D. & Loria, J. P. NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339, 204-238 (2001). (Pubitemid 32666562)
-
(2001)
Methods in Enzymology
, vol.339
, pp. 204-238
-
-
Palmer III, A.G.1
Kroenke, C.D.2
Loria, J.P.3
-
7
-
-
42449146665
-
Consistent blind protein structure generation from NMR chemical shift data
-
DOI 10.1073/pnas.0800256105
-
Shen, Y. et al. Consistent blind protein structure generation from NMR chemical shift data. Proc. Natl Acad. Sci. USA 105, 4685-4690 (2008). (Pubitemid 351753807)
-
(2008)
Proceedings of the National Academy of Sciences of the United States of America
, vol.105
, Issue.12
, pp. 4685-4690
-
-
Shen, Y.1
Lange, O.2
Delaglio, F.3
Rossi, P.4
Aramini, J.M.5
Liu, G.6
Eletsky, A.7
Wu, Y.8
Singarapu, K.K.9
Lemak, A.10
Ignatchenko, A.11
Arrowsmith, C.H.12
Szyperski, T.13
Montelione, G.T.14
Baker, D.15
Bax, A.16
-
8
-
-
77950234229
-
Lessons fromthe lysozyme of phage T4
-
Baase, W. A., Liu, L., Tronrud, D. E. & Matthews, B. W. Lessons fromthe lysozyme of phage T4. Protein Sci. 19, 631-641 (2010).
-
(2010)
Protein Sci.
, vol.19
, pp. 631-641
-
-
Baase, W.A.1
Liu, L.2
Tronrud, D.E.3
Matthews, B.W.4
-
9
-
-
0026567907
-
Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
-
Eriksson, A. E. et al. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255, 178-183 (1992).
-
(1992)
Science
, vol.255
, pp. 178-183
-
-
Eriksson, A.E.1
-
10
-
-
42449102160
-
Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: An application to protein folding
-
Korzhnev, D. M. & Kay, L. E. Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Acc. Chem. Res. 41, 442-451 (2008).
-
(2008)
Acc. Chem. Res.
, vol.41
, pp. 442-451
-
-
Korzhnev, D.M.1
Kay, L.E.2
-
11
-
-
46949093335
-
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
-
Hansen, D. F., Vallurupalli, P. & Kay, L. E. Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states. J. Biomol. NMR 41, 113-120 (2008).
-
(2008)
J. Biomol. NMR
, vol.41
, pp. 113-120
-
-
Hansen, D.F.1
Vallurupalli, P.2
Kay, L.E.3
-
12
-
-
34547455182
-
Protein structure determination from NMR chemical shifts
-
DOI 10.1073/pnas.0610313104
-
Cavalli, A., Salvatella, X., Dobson, C. M. & Vendruscolo, M. Protein structure determination from NMR chemical shifts. Proc. Natl Acad. Sci. USA 104, 9615-9620 (2007). (Pubitemid 47175315)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.23
, pp. 9615-9620
-
-
Cavalli, A.1
Salvatella, X.2
Dobson, C.M.3
Vendruscolo, M.4
-
13
-
-
50149085281
-
Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
-
Vallurupalli, P., Hansen, D. F. & Kay, L. E. Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy. Proc. Natl Acad. Sci. USA 105, 11766-11771 (2008).
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 11766-11771
-
-
Vallurupalli, P.1
Hansen, D.F.2
Kay, L.E.3
-
14
-
-
77956501272
-
A transient and low-populated protein-folding intermediate at atomic resolution
-
Korzhnev, D. M., Religa, T. L., Banachewicz, W., Fersht, A. R. & Kay, L. E. A transient and low-populated protein-folding intermediate at atomic resolution. Science 329, 1312-1316 (2010).
-
(2010)
Science
, vol.329
, pp. 1312-1316
-
-
Korzhnev, D.M.1
Religa, T.L.2
Banachewicz, W.3
Fersht, A.R.4
Kay, L.E.5
-
15
-
-
27544456339
-
A simple method to predict protein flexibility using secondary chemical shifts
-
DOI 10.1021/ja054842f
-
Berjanskii, M. V.&Wishart, D. S. A simplemethod to predict protein flexibility using secondary chemical shifts. J. Am. Chem. Soc. 127, 14970-14971 (2005). (Pubitemid 41547332)
-
(2005)
Journal of the American Chemical Society
, vol.127
, Issue.43
, pp. 14970-14971
-
-
Berjanskii, M.V.1
Wishart, D.S.2
-
16
-
-
34548861782
-
Protein-protein docking with backbone flexibility
-
DOI 10.1016/j.jmb.2007.07.050, PII S0022283607010030
-
Wang, C., Bradley, P. & Baker, D. Protein-protein docking with backbone flexibility. J. Mol. Biol. 373, 503-519 (2007). (Pubitemid 47445567)
-
(2007)
Journal of Molecular Biology
, vol.373
, Issue.2
, pp. 503-519
-
-
Wang, C.1
Bradley, P.2
Baker, D.3
-
18
-
-
33845182844
-
2D chemical-exchange NMR-spectroscopy by proton detected heteronuclear correlation
-
Montelione, G. T. & Wagner, G. 2D chemical-exchange NMR-spectroscopy by proton detected heteronuclear correlation. J. Am. Chem. Soc. 111, 3096-3098 (1989).
-
(1989)
J. Am. Chem. Soc.
, vol.111
, pp. 3096-3098
-
-
Montelione, G.T.1
Wagner, G.2
-
19
-
-
0028503463
-
A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
-
Farrow, N. A., Zhang, O., Forman-Kay, J. D. & Kay, L. E. A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium. J. Biomol. NMR 4, 727-734 (1994).
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 727-734
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
20
-
-
0029882583
-
Access of ligands to cavities within the core of a protein is rapid
-
DOI 10.1038/nsb0696-516
-
Feher, V. A., Baldwin, E. P. & Dahlquist, F. W. Access of ligands to cavities within the core of a protein is rapid. Nature Struct. Biol. 3, 516-521 (1996). (Pubitemid 26174700)
-
(1996)
Nature Structural Biology
, vol.3
, Issue.6
, pp. 516-521
-
-
Feher, V.A.1
Baldwin, E.P.2
Dahlquist, F.W.3
-
21
-
-
77950497745
-
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
-
Religa, T. L., Sprangers, R. & Kay, L. E. Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science 328, 98-102 (2010).
-
(2010)
Science
, vol.328
, pp. 98-102
-
-
Religa, T.L.1
Sprangers, R.2
Kay, L.E.3
-
22
-
-
0030981418
-
1 angles of aromatic residues in proteins from three-bond J(C'Cγ) and J(NCγ) couplings
-
DOI 10.1021/ja963625z, PII S0002786396036256
-
Hu, J. S., Grzesiek, S. & Bax, A. Two-dimensionalNMR methods for determining x1 angles of aromatic residues in proteins from three-bond JC'Cc and JNCc couplings. J. Am. Chem. Soc. 119, 1803-1804 (1997). (Pubitemid 27145534)
-
(1997)
Journal of the American Chemical Society
, vol.119
, Issue.7
, pp. 1803-1804
-
-
Hu, J.-S.1
Grzesiek, S.2
Bax, A.3
-
23
-
-
0026955827
-
Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme
-
Nicholson, H., Tronrud, D. E., Becktel, W. J. & Matthews, B. W. Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. Biopolymers 32, 1431-1441 (1992).
-
(1992)
Biopolymers
, vol.32
, pp. 1431-1441
-
-
Nicholson, H.1
Tronrud, D.E.2
Becktel, W.J.3
Matthews, B.W.4
-
24
-
-
64849101493
-
Protein dynamism and evolvability
-
Tokuriki, N. & Tawfik, D. S. Protein dynamism and evolvability. Science 324, 203-207 (2009).
-
(2009)
Science
, vol.324
, pp. 203-207
-
-
Tokuriki, N.1
Tawfik, D.S.2
-
25
-
-
0017272554
-
Enzymerecruitment in evolutionofnewfunction
-
Jensen, R. A. Enzymerecruitment in evolutionofnewfunction. Annu. Rev. Microbiol. 30, 409-425 (1976).
-
(1976)
Annu. Rev. Microbiol.
, vol.30
, pp. 409-425
-
-
Jensen, R.A.1
-
26
-
-
33845865301
-
Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA
-
DOI 10.1126/science.1133116
-
Walden, W. E. et al. Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. Science 314, 1903-1908 (2006). (Pubitemid 46026108)
-
(2006)
Science
, vol.314
, Issue.5807
, pp. 1903-1908
-
-
Walden, W.E.1
Selezneva, A.I.2
Dupuy, J.3
Volbeda, A.4
Fontecilla-Camps, J.C.5
Theil, E.C.6
Volz, K.7
-
27
-
-
35548976322
-
Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
-
DOI 10.1038/nature06232, PII NATURE06232
-
Tang, C., Schwieters, C. D. & Clore, G. M. Open-to-closed transition in apo maltosebinding protein observed by paramagneticNMR. Nature 449, 1078-1082 (2007). (Pubitemid 350014601)
-
(2007)
Nature
, vol.449
, Issue.7165
, pp. 1078-1082
-
-
Tang, C.1
Schwieters, C.D.2
Clore, G.M.3
-
28
-
-
58149091254
-
Halogenated benzenesboundwithin a nonpolar cavity in T4 lysozymeprovide examples of i SandI Se halogen-bonding
-
Liu, L. J.,Baase, W.A.&Matthews, B.W.Halogenated benzenesboundwithin a nonpolar cavity in T4 lysozymeprovide examples of I SandI Se halogen-bonding. J. Mol. Biol. 385, 595-605 (2009).
-
(2009)
J. Mol. Biol.
, vol.385
, pp. 595-605
-
-
Liu, L.J.1
Baase, W.A.2
Matthews, B.W.3
-
29
-
-
68349093958
-
TALOS1: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
-
Shen, Y., Delaglio, F., Cornilescu, G. & Bax, A. TALOS1: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223 (2009).
-
(2009)
J. Biomol. NMR
, vol.44
, pp. 213-223
-
-
Shen, Y.1
Delaglio, F.2
Cornilescu, G.3
Bax, A.4
-
30
-
-
9244237643
-
Using chemical exchange to assign non-covalent protein complexes in slow exchange with the free state: Enhanced resolution and efficient signal editing
-
DOI 10.1023/B:JNMR.0000048857.44219.c3
-
Rodríguez, J. C., Jennings, P. A. & Melacini, G. Using chemical exchange to assign non-covalent protein complexes in slow exchange with the free state: enhanced resolution and efficient signal editing. J. Biomol. NMR 30, 155-161 (2004). (Pubitemid 39549732)
-
(2004)
Journal of Biomolecular NMR
, vol.30
, Issue.2
, pp. 155-161
-
-
Rodriguez, J.C.1
Jennings, P.A.2
Melacini, G.3
-
31
-
-
75549088827
-
Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy
-
Lundström, P., Vallurupalli, P., Hansen, D. F. & Kay, L. E. Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy. Nature Protocols 4, 1641-1648 (2009).
-
(2009)
Nature Protocols
, vol.4
, pp. 1641-1648
-
-
Lundström, P.1
Vallurupalli, P.2
Hansen, D.F.3
Kay, L.E.4
-
32
-
-
69249209773
-
CPMGrelaxationdispersion NMR experiments measuring glycine 1Ha and 13Ca chemical shifts in the 'invisible' excited states of proteins
-
Vallurupalli, P.,Hansen, D. F., Lundstrom, P.&Kay, L. E.CPMGrelaxationdispersion NMR experiments measuring glycine 1Ha and 13Ca chemical shifts in the 'invisible' excited states of proteins. J. Biomol. NMR 45, 45-55 (2009).
-
(2009)
J. Biomol. NMR
, vol.45
, pp. 45-55
-
-
Vallurupalli, P.1
Hansen, D.F.2
Lundstrom, P.3
Kay, L.E.4
-
33
-
-
0347722841
-
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
-
PII S0079656598000259
-
Sattler, M., Schleucher, J. & Griesinger, C. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34, 93-158 (1999). (Pubitemid 129595216)
-
(1999)
Progress in Nuclear Magnetic Resonance Spectroscopy
, vol.34
, Issue.2
, pp. 93-158
-
-
Sattler, M.1
Schleucher, J.2
Griesinger, C.3
-
34
-
-
3242880292
-
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
-
DOI 10.1038/nature02655
-
Korzhnev, D. M. et al. Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature 430, 586-590 (2004). (Pubitemid 38998635)
-
(2004)
Nature
, vol.430
, Issue.6999
, 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
-
35
-
-
36749058463
-
Measurement of bond vector orientations in invisible excited states of proteins
-
DOI 10.1073/pnas.0708296104
-
Vallurupalli, P., Hansen, D. F., Stollar, E., Meirovitch, E. & Kay, L. E. Measurement of bond vector orientations in invisible excited states of proteins. Proc. Natl Acad. Sci. USA 104, 18473-18477 (2007). (Pubitemid 350210721)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.47
, pp. 18473-18477
-
-
Vallurupalli, P.1
Hansen, D.F.2
Stollar, E.3
Meirovitch, E.4
Kay, L.E.5
-
36
-
-
39749156063
-
Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: How well can we do?
-
DOI 10.1021/ja078337p
-
Hansen, D. F., Vallurupalli, P., Lundstrom, P., Neudecker, P. & Kay, L. E. Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? J. Am. Chem. Soc. 130, 2667-2675 (2008). (Pubitemid 351304782)
-
(2008)
Journal of the American Chemical Society
, vol.130
, Issue.8
, pp. 2667-2675
-
-
Hansen, D.F.1
Vallurupalli, P.2
Lundstrom, P.3
Neudecker, P.4
Kay, L.E.5
-
37
-
-
0037120879
-
Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments
-
DOI 10.1021/ja0207089
-
Skrynnikov, N. R., Dahlquist, F. W. & Kay, L. E. Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. J. Am. Chem. Soc. 124, 12352-12360 (2002). (Pubitemid 35154900)
-
(2002)
Journal of the American Chemical Society
, vol.124
, Issue.41
, pp. 12352-12360
-
-
Skrynnikov, N.R.1
Dahlquist, F.W.2
Kay, L.E.3
-
38
-
-
77954689925
-
A simple method for measuring signs of 1HN chemical shift differences between ground and excited protein states
-
Bouvignies, G. et al. A simple method for measuring signs of 1HN chemical shift differences between ground and excited protein states. J. Biomol. NMR 47, 135-141 (2010).
-
(2010)
J. Biomol. NMR
, vol.47
, pp. 135-141
-
-
Bouvignies, G.1
-
39
-
-
1242336825
-
Double- and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins
-
Orekhov, V. Y., Korzhnev, D. M. & Kay, L. E. Double-and zero-quantum NMR relaxation dispersion experiments sampling millisecond time scale dynamics in proteins. J. Am. Chem. Soc. 126, 1886-1891 (2004). (Pubitemid 38222773)
-
(2004)
Journal of the American Chemical Society
, vol.126
, Issue.6
, pp. 1886-1891
-
-
Orekhov, V.Yu.1
Korzhnev, D.M.2
Kay, L.E.3
-
40
-
-
0030764469
-
13C three- bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?
-
DOI 10.1021/ja970067v
-
Hu, J. S. & Bax, A. Determination of Q and x1 angles in proteins from13C-13C threebond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J. Am. Chem. Soc. 119, 6360-6368 (1997). (Pubitemid 27364249)
-
(1997)
Journal of the American Chemical Society
, vol.119
, Issue.27
, pp. 6360-6368
-
-
Hu, J.-S.1
Bax, A.2
-
41
-
-
0029400480
-
NMRpipe-amultidimensional spectral processing systembased on Unix pipes
-
Delaglio, F. et al.NMRpipe-amultidimensional spectral processing systembased on Unix pipes. J. Biomol. NMR 6, 277-293 (1995).
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
-
42
-
-
0004757060
-
-
University of California, San Francisco
-
Goddard, T. D. & Kneller, D. G. SPARKY 3 (University of California, San Francisco, 2006).
-
(2006)
SPARKY
, vol.3
-
-
Goddard, T.D.1
Kneller, D.G.2
-
43
-
-
19444382397
-
The CCPN data model for NMR spectroscopy: Development of a software pipeline
-
DOI 10.1002/prot.20449
-
Vranken, W. F. et al. The CCPN datamodel forNMR spectroscopy: development of a software pipeline. Proteins Struct. Funct. Bioinform. 59, 687-696 (2005). (Pubitemid 40695845)
-
(2005)
Proteins: Structure, Function and Genetics
, vol.59
, Issue.4
, pp. 687-696
-
-
Vranken, W.F.1
Boucher, W.2
Stevens, T.J.3
Fogh, R.H.4
Pajon, A.5
Llinas, M.6
Ulrich, E.L.7
Markley, J.L.8
Ionides, J.9
Laue, E.D.10
-
44
-
-
0034680315
-
Flexibility and ligand exchange in a buried cavitymutant of T4 lysozymestudied bymultinuclear NMR
-
Mulder, F. A., Hon, B., Muhandiram, D. R., Dahlquist, F. W.& Kay, L. E. Flexibility and ligand exchange in a buried cavitymutant of T4 lysozymestudied bymultinuclear NMR. Biochemistry 39, 12614-12622 (2000).
-
(2000)
Biochemistry
, vol.39
, pp. 12614-12622
-
-
Mulder, F.A.1
Hon, B.2
Muhandiram, D.R.3
Dahlquist, F.W.4
Kay, L.E.5
-
45
-
-
0010957050
-
Reaction rates by nuclearmagnetic resonance
-
McConnell, H. M. Reaction rates by nuclearmagnetic resonance. J. Chem. Phys. 28, 430-431 (1958).
-
(1958)
J. Chem. Phys.
, vol.28
, pp. 430-431
-
-
McConnell, H.M.1
-
46
-
-
28044440088
-
Quantitative NMR spectroscopy of supramolecular complexes: Dynamic side pores in ClpP are important for product release
-
DOI 10.1073/pnas.0507370102
-
Sprangers, R., Gribun, A., Hwang, P. M., Houry, W. A. & Kay, L. E. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proc. Natl Acad. Sci. USA 102, 16678-16683 (2005). (Pubitemid 41688836)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.46
, pp. 16678-16683
-
-
Sprangers, R.1
Gribun, A.2
Hwang, P.M.3
Houry, W.A.4
Kay, L.E.5
-
47
-
-
0004161838
-
-
Cambridge Univ. Press
-
Press, W. H., Flannery, B. P., Teukolsky, S. A.& Vetterling, W. T. Numerical Recipes in C. The Art of Scientific Computing 2nd edn (Cambridge Univ. Press, 1992).
-
(1992)
Numerical Recipes in C. the Art of Scientific Computing 2nd Edn
-
-
Press, W.H.1
Flannery, B.P.2
Teukolsky, S.A.3
Vetterling, W.T.4
-
48
-
-
79952426683
-
SciNet: Lessons learned from building a power-efficient top-20 system and data centre
-
Loken, C. et al. SciNet: Lessons learned from building a power-efficient top-20 system and data centre. J. Phys. Conf. Ser. 256, 012026 (2010).
-
(2010)
J. Phys. Conf. Ser.
, vol.256
, pp. 012026
-
-
Loken, C.1
-
50
-
-
4444221565
-
UCSF Chimera - A visualization system for exploratory research and analysis
-
Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
-
(2004)
J. Comput. Chem.
, vol.25
, pp. 1605-1612
-
-
Pettersen, E.F.1
-
51
-
-
79551470095
-
Role of conformational sampling in computing mutation-induced changes in protein structure and stability
-
Kellogg, E. H., Leaver-Fay, A. & Baker, D. Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins 79, 830-838 (2011).
-
(2011)
Proteins
, vol.79
, pp. 830-838
-
-
Kellogg, E.H.1
Leaver-Fay, A.2
Baker, D.3
|