-
1
-
-
0000913086
-
A fast algorithm for rendering space-filling molecule pictures
-
Bacon D. J., Anderson W. F. A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6:1988;219-220.
-
(1988)
J. Mol. Graph.
, vol.6
, pp. 219-220
-
-
Bacon, D.J.1
Anderson, W.F.2
-
2
-
-
0027265713
-
The role of turns in the structure of an alpha-helical protein
-
Brunet A. P., Huang E. S., Huffine M. E., Loeb J. E., Weltman R. J., Hecht M. H. The role of turns in the structure of an alpha-helical protein. Nature. 364:1993;355-358.
-
(1993)
Nature
, vol.364
, pp. 355-358
-
-
Brunet, A.P.1
Huang, E.S.2
Huffine, M.E.3
Loeb, J.E.4
Weltman, R.J.5
Hecht, M.H.6
-
3
-
-
0031005061
-
The energy landscape of a fast-folding protein mapped by Ala→Gly substitutions
-
Burton R. E., Huang G. S., Daugherty M. A., Calderone T. L., Oas T. G. The energy landscape of a fast-folding protein mapped by Ala→Gly substitutions. Nature Struct. Biol. 4:1997;305-310.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 305-310
-
-
Burton, R.E.1
Huang, G.S.2
Daugherty, M.A.3
Calderone, T.L.4
Oas, T.G.5
-
4
-
-
0030334648
-
An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
-
Clarke J., Fersht A. R. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold. Des. 1:1996;243-254.
-
(1996)
Fold. Des.
, vol.1
, pp. 243-254
-
-
Clarke, J.1
Fersht, A.R.2
-
5
-
-
0029900846
-
The magnitude of the backbone conformational entropy change in protein folding
-
D'Aquino J. A., G'omez J., Hilser V. J., Lee K. H., Amzel L. M., Freire E. The magnitude of the backbone conformational entropy change in protein folding. Proteins: Struct. Funct. Genet. 25:1996;143-156.
-
(1996)
Proteins: Struct. Funct. Genet.
, vol.25
, pp. 143-156
-
-
D'Aquino, J.A.1
G'omez, J.2
Hilser, V.J.3
Lee, K.H.4
Amzel, L.M.5
Freire, E.6
-
7
-
-
0028856785
-
Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
-
Fersht A. R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873.
-
(1995)
Proc. Natl Acad. Sci. USA
, vol.92
, pp. 10869-10873
-
-
Fersht, A.R.1
-
8
-
-
0031043161
-
Nucleation mechanisms in protein folding
-
Fersht A. R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7:1997;3-9.
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 3-9
-
-
Fersht, A.R.1
-
10
-
-
0029004982
-
A phage display system for studying the sequence determinants of protein folding
-
Gu H., Yi Q., Bray S. T., Riddle D. S., Shiau A. K., Baker D. A phage display system for studying the sequence determinants of protein folding. Protein Sci. 4:1995;1108-1117.
-
(1995)
Protein Sci.
, vol.4
, pp. 1108-1117
-
-
Gu, H.1
Yi, Q.2
Bray, S.T.3
Riddle, D.S.4
Shiau, A.K.5
Baker, D.6
-
11
-
-
0028566270
-
A revised set of potentials for beta-turn formation in proteins
-
Hutchinson E. G., Thornton J. M. A revised set of potentials for beta-turn formation in proteins. Protein Sci. 3:1994;2207-2216.
-
(1994)
Protein Sci.
, vol.3
, pp. 2207-2216
-
-
Hutchinson, E.G.1
Thornton, J.M.2
-
12
-
-
0028868995
-
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
-
Itzhaki L. S., Otzen D. E., Fersht A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254:1995;260-288.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 260-288
-
-
Itzhaki, L.S.1
Otzen, D.E.2
Fersht, A.R.3
-
13
-
-
0027384577
-
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
-
Jackson S. E., Morocci M., elMasry N. F., Johnson C. M., Fersht A. R. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry. 32:1993;11259-11269.
-
(1993)
Biochemistry
, vol.32
, pp. 11259-11269
-
-
Jackson, S.E.1
Morocci, M.2
ElMasry, N.F.3
Johnson, C.M.4
Fersht, A.R.5
-
14
-
-
0026244229
-
MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
-
Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
-
(1991)
J. Appl. Crystallog.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
15
-
-
0031588693
-
Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities
-
L'opez Hern'andez E., Cronet P., Serrano L., Munoz V. Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities. J. Mol. Biol. 266:1997;610-620.
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 610-620
-
-
L'opez Hern'andez, E.1
Cronet, P.2
Serrano, L.3
Munoz, V.4
-
16
-
-
0024358426
-
Mapping the transition state and pathway of protein folding by protein engineering
-
Matouschek K., Kellis J. T., Serrano L., Fersht A. R. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340. 1989;122-126.
-
(1989)
Nature 340
, pp. 122-126
-
-
Matouschek, K.1
Kellis, J.T.2
Serrano, L.3
Fersht, A.R.4
-
17
-
-
0028057108
-
Raster3D version 2.0. A program for photorealistic molecular graphics
-
Merritt E. A., Murphy M. E. P. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog, sect. D. 50:1994;869-873.
-
(1994)
Acta Crystallog, Sect. D
, vol.50
, pp. 869-873
-
-
Merritt, E.A.1
Murphy, M.E.P.2
-
18
-
-
0028485627
-
Protein stability effects of a complete set of alanine substitutions in Arc repressor
-
Milla M. E., Brown B. M., Sauer R. T. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature Struct. Biol. 1:1994;518-523.
-
(1994)
Nature Struct. Biol.
, vol.1
, pp. 518-523
-
-
Milla, M.E.1
Brown, B.M.2
Sauer, R.T.3
-
19
-
-
0029090925
-
Redesigning the topology of a four-helix-bundle protein: Monomeric Rop
-
Predki P. F., Regan L. Redesigning the topology of a four-helix-bundle protein: monomeric Rop. Biochemistry. 34:1995;9834-9839.
-
(1995)
Biochemistry
, vol.34
, pp. 9834-9839
-
-
Predki, P.F.1
Regan, L.2
-
21
-
-
0040589805
-
Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: Secondary structure propensities are not conserved in proteins with the same fold
-
Ram'irez Alvarado M., Serrano L., Blanco F. J. Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. Protein Sci. 6:1997;162-174.
-
(1997)
Protein Sci.
, vol.6
, pp. 162-174
-
-
Ram'irez Alvarado, M.1
Serrano, L.2
Blanco, F.J.3
-
22
-
-
0026345258
-
Random mutagenesis of protein sequences using oligonucleotide cassettes
-
Reidhaar Olson J. F., Bowie J. U., Breyer R. M., Hu J. C., Knight K. L., Lim W. A., Mossing M. C., Parsell D. A., Shoemaker K. R., Sauer R. T. Random mutagenesis of protein sequences using oligonucleotide cassettes. Methods enzymol. 208:1991;564-586.
-
(1991)
Methods Enzymol.
, vol.208
, pp. 564-586
-
-
Reidhaar Olson, J.F.1
Bowie, J.U.2
Breyer, R.M.3
Hu, J.C.4
Knight, K.L.5
Lim, W.A.6
Mossing, M.C.7
Parsell, D.A.8
Shoemaker, K.R.9
Sauer, R.T.10
-
23
-
-
0030900533
-
Kinetics of folding of the IgG binding domain of peptostreptococcal protein L
-
Scalley M. L., Yi Q., Gu H., McCormack A., Yates J. R. 3., Baker D. Kinetics of folding of the IgG binding domain of peptostreptococcal protein L. Biochemistry. 36:1997;3373-3382.
-
(1997)
Biochemistry
, vol.36
, pp. 3373-3382
-
-
Scalley, M.L.1
Yi, Q.2
Gu, H.3
McCormack, A.4
Yates J.R. III5
Baker, D.6
-
24
-
-
78651171134
-
On the kinetics of the helix-coil transition of polypeptides in solution
-
Schwartz G. On the kinetics of the helix-coil transition of polypeptides in solution. J. Mol. Biol. 11:1965;65-77.
-
(1965)
J. Mol. Biol.
, vol.11
, pp. 65-77
-
-
Schwartz, G.1
-
25
-
-
0026579572
-
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
-
Serrano L., Matouschek A., Fersht A. R. The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224:1992;805-818.
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 805-818
-
-
Serrano, L.1
Matouschek, A.2
Fersht, A.R.3
-
26
-
-
0029670994
-
Conserved residues and the mechanism of protein folding
-
Shakhnovich E., Abkevich V., Ptitsyn O. Conserved residues and the mechanism of protein folding. Nature. 379:1996;96-98.
-
(1996)
Nature
, vol.379
, pp. 96-98
-
-
Shakhnovich, E.1
Abkevich, V.2
Ptitsyn, O.3
-
27
-
-
0031585984
-
Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
-
Simons K., Kooperberg D., Huang E., Baker D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268:1997;209-225.
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 209-225
-
-
Simons, K.1
Kooperberg, D.2
Huang, E.3
Baker, D.4
-
28
-
-
0029990293
-
The role of helix formation in the folding of a fully alpha-helical coiled coil
-
Sosnick T. R., Jackson S., Wilk R. R., Englander S. W., DeGrado W. F. The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins: Struct. Funct. Genet. 24:1996;427-432.
-
(1996)
Proteins: Struct. Funct. Genet.
, vol.24
, pp. 427-432
-
-
Sosnick, T.R.1
Jackson, S.2
Wilk, R.R.3
Englander, S.W.4
DeGrado, W.F.5
-
29
-
-
0030604696
-
Local interactions dominate folding in a simple protein model
-
Unger R., Moult J. Local interactions dominate folding in a simple protein model. J. Mol. Biol. 259:1996;988-994.
-
(1996)
J. Mol. Biol.
, vol.259
, pp. 988-994
-
-
Unger, R.1
Moult, J.2
-
30
-
-
0027155337
-
Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L
-
Wikstrom M., Sjobring U., Kastern W., Bjorck L., Drakenberg T., Forsen S. Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L. Biochemistry. 32:1993;3381-3386.
-
(1993)
Biochemistry
, vol.32
, pp. 3381-3386
-
-
Wikstrom, M.1
Sjobring, U.2
Kastern, W.3
Bjorck, L.4
Drakenberg, T.5
Forsen, S.6
-
31
-
-
0029035614
-
Mapping of immunoglobulin light chain-binding site of protein L
-
Wikstrom M., Sjobring U., Drakenberg T., Forsen S., Bjorck L. Mapping of immunoglobulin light chain-binding site of protein L. J. Mol. Biol. 250:1995;128-133.
-
(1995)
J. Mol. Biol.
, vol.250
, pp. 128-133
-
-
Wikstrom, M.1
Sjobring, U.2
Drakenberg, T.3
Forsen, S.4
Bjorck, L.5
-
32
-
-
0030026589
-
Backbone dynamics of a domain of protein L which binds to immunoglobulin light chains
-
Wikstrom M., Forsen S., Drakenberg T. Backbone dynamics of a domain of protein L which binds to immunoglobulin light chains. Eur. J. Biochem. 235:1996;543-548.
-
(1996)
Eur. J. Biochem.
, vol.235
, pp. 543-548
-
-
Wikstrom, M.1
Forsen, S.2
Drakenberg, T.3
-
33
-
-
0029877554
-
Sequence replacements in the central beta-turn of plastocyanin
-
Ybe J. A., Hecht M. H. Sequence replacements in the central beta-turn of plastocyanin. Protein Sci. 5:1996;814-824.
-
(1996)
Protein Sci.
, vol.5
, pp. 814-824
-
-
Ybe, J.A.1
Hecht, M.H.2
-
34
-
-
0029897657
-
Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR
-
Yi Q., Baker D. Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR. Protein Sci. 5:1996;1060-1066.
-
(1996)
Protein Sci.
, vol.5
, pp. 1060-1066
-
-
Yi, Q.1
Baker, D.2
-
35
-
-
0030631570
-
Characterization of the free energy spectrum of Peptostreptococcal protein L
-
Yi Q., Scalley M. L., Simons K., Gladwin S., Baker D. Characterization of the free energy spectrum of Peptostreptococcal protein L. Fold. Des. 2:1997;271-280.
-
(1997)
Fold. Des.
, vol.2
, pp. 271-280
-
-
Yi, Q.1
Scalley, M.L.2
Simons, K.3
Gladwin, S.4
Baker, D.5
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