-
1
-
-
5144233105
-
MLEV-17 based two-dimensional homonuclear magnetism transfer spectroscopy
-
Bax A., Davis D. G. MLEV-17 based two-dimensional homonuclear magnetism transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
-
(1985)
J. Magn. Reson.
, vol.65
, pp. 355-360
-
-
Bax, A.1
Davis, D.G.2
-
2
-
-
0000349003
-
Evidence for a short linear peptide that folds into native stable β-hairpin in aqueous solution
-
Blanco F. J., Jiménez M. A., Rico M., Santoro J., Herranz J., Nieto J. L. Evidence for a short linear peptide that folds into native stable β-hairpin in aqueous solution. J. Am. Chem. Soc. 115:1993;5887-5888.
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 5887-5888
-
-
Blanco, F.J.1
Jiménez, M.A.2
Rico, M.3
Santoro, J.4
Herranz, J.5
Nieto, J.L.6
-
3
-
-
0011491177
-
Structure determination of a tetrassacharide: Transient nuclear Overhauser effect in the rotating frame
-
Bothner-By A. A., Stephens R. L., Lee J. M., Warren C. D., Jeanloz R. W. Structure determination of a tetrassacharide: transient nuclear Overhauser effect in the rotating frame. J. Am. Chem. Soc. 106:1984;811-813.
-
(1984)
J. Am. Chem. Soc.
, vol.106
, pp. 811-813
-
-
Bothner-By, A.A.1
Stephens, R.L.2
Lee, J.M.3
Warren, C.D.4
Jeanloz, R.W.5
-
4
-
-
0025119481
-
Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance
-
Bradley E. K., Thomason J. F., Cohen F. E., Kosen P. A., Kuntz I. D. Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. J. Mol. Biol. 215:1990;607-622.
-
(1990)
J. Mol. Biol.
, vol.215
, pp. 607-622
-
-
Bradley, E.K.1
Thomason, J.F.2
Cohen, F.E.3
Kosen, P.A.4
Kuntz, I.D.5
-
5
-
-
0027265713
-
The role of turns in the structure of an α-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 α-helical protein. Nature. 363:1993;355-358.
-
(1993)
Nature
, vol.363
, 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
-
6
-
-
0028284549
-
Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare mutations that prevent the folding of Rop
-
Castagnoli L., Vetriani C., Cesareni C. Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare mutations that prevent the folding of Rop. J. Mol. Biol. 234:1994;378-387.
-
(1994)
J. Mol. Biol.
, vol.234
, pp. 378-387
-
-
Castagnoli, L.1
Vetriani, C.2
Cesareni, C.3
-
8
-
-
0015914783
-
Conformation of twisted β-pleated sheets in proteins
-
Chothia C. Conformation of twisted β-pleated sheets in proteins. J. Mol. Biol. 75:1973;295-302.
-
(1973)
J. Mol. Biol.
, vol.75
, pp. 295-302
-
-
Chothia, C.1
-
9
-
-
0028857729
-
Interactions responsible for the β-hairpin conformational population formed by a designed linear peptide
-
de Alba E., Blanco F. J., Jiménez M. A., Rico M., Nieto J. L. Interactions responsible for the β-hairpin conformational population formed by a designed linear peptide. Eur. J. Biochem. 233:1995;283-292.
-
(1995)
Eur. J. Biochem.
, vol.233
, pp. 283-292
-
-
De Alba, E.1
Blanco, F.J.2
Jiménez, M.A.3
Rico, M.4
Nieto, J.L.5
-
10
-
-
0030334822
-
Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution
-
de Alba E., Jiménez M. A., Rico M., Nieto J. L. Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution. Folding design. 1:1996;122-144.
-
(1996)
Folding Design
, vol.1
, pp. 122-144
-
-
De Alba, E.1
Jiménez, M.A.2
Rico, M.3
Nieto, J.L.4
-
11
-
-
1842403587
-
Turn residue sequence determines β-hairpin conformation in designed peptides
-
de Alba E., Jiménez M. A., Rico M. Turn residue sequence determines β-hairpin conformation in designed peptides. J. Am. Chem. Soc. 119:1997;175-183.
-
(1997)
J. Am. Chem. Soc.
, vol.119
, pp. 175-183
-
-
De Alba, E.1
Jiménez, M.A.2
Rico, M.3
-
13
-
-
0024448151
-
Calculation of protein extinction coefficients from amino acid sequence data
-
Gill S. C., Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
-
(1989)
Anal. Biochem.
, vol.182
, pp. 319-326
-
-
Gill, S.C.1
Hippel, P.H.2
-
14
-
-
0026089657
-
Improved efficency of protein structure calculations from NMR using the program DIANA with redundant dihedral angle constraints
-
Güntert P., Braun W., Wüthrich K. Improved efficency of protein structure calculations from NMR using the program DIANA with redundant dihedral angle constraints. J. Mol. Biol. 217:1991;517-530.
-
(1991)
J. Mol. Biol.
, vol.217
, pp. 517-530
-
-
Güntert, P.1
Braun, W.2
Wüthrich, K.3
-
15
-
-
0030992473
-
Insights of β-hairpin stabilty in aqueous solution from peptides with enforced type I′ and type II′ β-turns
-
Haque T. S., Gellman S. H. Insights of β-hairpin stabilty in aqueous solution from peptides with enforced type I′ and type II′ β-turns. J. Am. Chem. Soc. 119:1997;2303-2304.
-
(1997)
J. Am. Chem. Soc.
, vol.119
, pp. 2303-2304
-
-
Haque, T.S.1
Gellman, S.H.2
-
17
-
-
0028566270
-
A revised set of potentials for β-turn formation in proteins
-
Hutchinson E. G., Thornton J. M. A revised set of potentials for β-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
-
18
-
-
0024556397
-
Transfer of a β-turn structure to a new protein context
-
Hynes T. R., Kautz R. A., Goodman M. A., Gill J. F., Fox R. O. Transfer of a β-turn structure to a new protein context. Nature. 339:1989;73-76.
-
(1989)
Nature
, vol.339
, pp. 73-76
-
-
Hynes, T.R.1
Kautz, R.A.2
Goodman, M.A.3
Gill, J.F.4
Fox, R.O.5
-
19
-
-
0028174179
-
Engineering alternative β-turn types in staphylococcal nuclease
-
Hynes T. R., Hodel A., Fox R. O. Engineering alternative β-turn types in staphylococcal nuclease. Biochemistry. 33:1994;5021-5030.
-
(1994)
Biochemistry
, vol.33
, pp. 5021-5030
-
-
Hynes, T.R.1
Hodel, A.2
Fox, R.O.3
-
20
-
-
0028174643
-
Quantitative determination of helical propensities from trifluoroethanol titration curves
-
Jasanoff, Fersht A. R. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry. 1:1994;2129-2135.
-
(1994)
Biochemistry
, vol.1
, pp. 2129-2135
-
-
Jasanoff1
Fersht, A.R.2
-
22
-
-
0020997912
-
Dictionary of protein secondary structure: Patterns recognition of hydrogen-bonded and geometrical features
-
Kabsch W., Sander C. Dictionary of protein secondary structure: patterns recognition of hydrogen-bonded and geometrical features. Biopolymers. 27:1983;2577-2637.
-
(1983)
Biopolymers
, vol.27
, pp. 2577-2637
-
-
Kabsch, W.1
Sander, C.2
-
23
-
-
0000655560
-
A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments
-
Kadkhodaei M., Hwang T. L., Tang J., Shaka A. J. A simple windowless mixing sequence to suppress cross relaxation in TOCSY experiments. J. Magn. Reson. ser. A. 104:1993;105-107.
-
(1993)
J. Magn. Reson. Ser. a
, vol.104
, pp. 105-107
-
-
Kadkhodaei, M.1
Hwang, T.L.2
Tang, J.3
Shaka, A.J.4
-
24
-
-
33745356391
-
Contact electron-spin coupling of nuclear magnetic moments
-
Karplus M. Contact electron-spin coupling of nuclear magnetic moments. J. Phys. Chem. 30:1995;11-15.
-
(1995)
J. Phys. Chem.
, vol.30
, pp. 11-15
-
-
Karplus, M.1
-
25
-
-
0031048642
-
Intestinal fatty acid binding protein: A specific residue in one turn appears to stabilize the native structure and be responsible for slow folding
-
Kim K., Ramanathan R., Frieden C. Intestinal fatty acid binding protein: a specific residue in one turn appears to stabilize the native structure and be responsible for slow folding. Protein Sci. 6:1997;364-372.
-
(1997)
Protein Sci.
, vol.6
, pp. 364-372
-
-
Kim, K.1
Ramanathan, R.2
Frieden, C.3
-
26
-
-
0019327003
-
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
-
Kumar A., Ernst R. A., Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
-
(1980)
Biochem. Biophys. Res. Commun.
, vol.95
, pp. 1-6
-
-
Kumar, A.1
Ernst, R.A.2
Wüthrich, K.3
-
27
-
-
33847801579
-
Charge relay at the peptide bond: A protein magnetic resonance study of solvation effects on the amide electron density distribution
-
Llinás M., Klein M. P. Charge relay at the peptide bond: a protein magnetic resonance study of solvation effects on the amide electron density distribution. J. Am. Chem. Soc. 97:1975;4731-4737.
-
(1975)
J. Am. Chem. Soc.
, vol.97
, pp. 4731-4737
-
-
Llinás, M.1
Klein, M.P.2
-
28
-
-
0031588693
-
Folding kinetics of CheY mutants with enhanced native α-helix propensities
-
López-Hernández E., Cronet P., Serrano L., Munoz V. Folding kinetics of CheY mutants with enhanced native α-helix propensities. J. Mol. Biol. 266:1997;610-620.
-
(1997)
J. Mol. Biol.
, vol.266
, pp. 610-620
-
-
López-Hernández, E.1
Cronet, P.2
Serrano, L.3
Munoz, V.4
-
29
-
-
0029207339
-
"random coil" 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
-
Merutka G., Dyson H. J., Wright P. E. "Random coil" 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR. 5:1995;14-24.
-
(1995)
J. Biomol. NMR
, vol.5
, pp. 14-24
-
-
Merutka, G.1
Dyson, H.J.2
Wright, P.E.3
-
30
-
-
0028176595
-
Measurement of the β-sheet propensities of amino acids
-
Minor D. L. Jr, Kim P. S. Measurement of the β-sheet propensities of amino acids. Nature. 367:1994a;660-663.
-
(1994)
Nature
, vol.367
, pp. 660-663
-
-
Minor D.L., Jr.1
Kim, P.S.2
-
31
-
-
0027998757
-
Context is a major determinant of β-sheet propensity
-
Minor D. L. Jr, Kim P. S. Context is a major determinant of β-sheet propensity. Nature. 371:1994b;264-267.
-
(1994)
Nature
, vol.371
, pp. 264-267
-
-
Minor D.L., Jr.1
Kim, P.S.2
-
32
-
-
0028568650
-
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: Comparison with experimental scales
-
Munoz V., Serrano L. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales. Proteins: Struct. Funct. Genet. 20:1994;301-311.
-
(1994)
Proteins: Struct. Funct. Genet.
, vol.20
, pp. 301-311
-
-
Munoz, V.1
Serrano, L.2
-
33
-
-
0029155035
-
Helix design, prediction and stability
-
Munoz V., Serrano L. Helix design, prediction and stability. Curr. Opin. Biotechnol. 6:1995;382-386.
-
(1995)
Curr. Opin. Biotechnol.
, vol.6
, pp. 382-386
-
-
Munoz, V.1
Serrano, L.2
-
35
-
-
0022804939
-
Stabilization of the ribonuclease S-peptide α-helix by tri fluoroethanol
-
Nelson J. W., Kallenbach N. R. Stabilization of the ribonuclease S-peptide α-helix by tri fluoroethanol. Proteins: Struct. Funct. Genet. 1:1986;211-217.
-
(1986)
Proteins: Struct. Funct. Genet.
, vol.1
, pp. 211-217
-
-
Nelson, J.W.1
Kallenbach, N.R.2
-
36
-
-
0031022599
-
β-Turn propensities as paradigms for the analysis of structural motifs to engineer protein stability
-
Ohage E. C., Grami W., Walter M. M., Steinbacher S., Steipe B. β-Turn propensities as paradigms for the analysis of structural motifs to engineer protein stability. Protein Sci. 6:1997;233-241.
-
(1997)
Protein Sci.
, vol.6
, pp. 233-241
-
-
Ohage, E.C.1
Grami, W.2
Walter, M.M.3
Steinbacher, S.4
Steipe, B.5
-
37
-
-
0005963761
-
Multiple quantum filters for elucidating NMR coupling networks
-
Piantini U., Sørensen O. W., Ernst R. R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104:1982;6800-6801.
-
(1982)
J. Am. Chem. Soc.
, vol.104
, pp. 6800-6801
-
-
Piantini, U.1
Sørensen, O.W.2
Ernst, R.R.3
-
41
-
-
0028865129
-
A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-soluble non-native β-hairpin
-
Searle M. S., Williams D. H., Packman L. C. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-soluble non-native β-hairpin. Nature Struct. Biol. 2:1995;999-1006.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 999-1006
-
-
Searle, M.S.1
Williams, D.H.2
Packman, L.C.3
-
42
-
-
0028790273
-
Comparison between the φ distribution of the amino acids in the protein database and NMR data indicates that amino acids have various φ propensities in the random coil conformation
-
Serrano. L. Comparison between the φ distribution of the amino acids in the protein database and NMR data indicates that amino acids have various φ propensities in the random coil conformation. J. Mol. Biol. 254:1995;322-333.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 322-333
-
-
Serrano., L.1
-
43
-
-
0021844602
-
β-Hairpin families in globular proteins
-
Sibanda B. L., Thornton J. M. β-Hairpin families in globular proteins. Nature. 316:1985;170-174.
-
(1985)
Nature
, vol.316
, pp. 170-174
-
-
Sibanda, B.L.1
Thornton, J.M.2
-
44
-
-
0025341310
-
Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins
-
Sippl M. J. Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. J. Mol. Biol. 213:1990;859-883.
-
(1990)
J. Mol. Biol.
, vol.213
, pp. 859-883
-
-
Sippl, M.J.1
-
45
-
-
0029000696
-
Knowledge-based potentials for proteins
-
Sippl M. J. Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 2:1995;1229-1235.
-
(1995)
Curr. Opin. Struct. Biol.
, vol.2
, pp. 1229-1235
-
-
Sippl, M.J.1
-
46
-
-
0028792105
-
Guidelines for protein design: The energetics of β-sheet side-chain interactions
-
Smith C. K., Regan L. Guidelines for protein design: the energetics of β-sheet side-chain interactions. Science. 270:1995;980-982.
-
(1995)
Science
, vol.270
, pp. 980-982
-
-
Smith, C.K.1
Regan, L.2
-
47
-
-
0029978353
-
Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
-
Smith L. J., Bolin K. A., Schwalbe H., MacArthur M. W., Thornton J. M., Dobson C. M. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255:1996;494-506.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 494-506
-
-
Smith, L.J.1
Bolin, K.A.2
Schwalbe, H.3
MacArthur, M.W.4
Thornton, J.M.5
Dobson, C.M.6
-
48
-
-
0002584387
-
A convenient and accurate method for the measurement of the values of spin-spin coupling constants
-
Stonehouse J., Keeler J. A convenient and accurate method for the measurement of the values of spin-spin coupling constants. J. Magn. Reson. A112:1995;43-57.
-
(1995)
J. Magn. Reson.
, vol.112
, pp. 43-57
-
-
Stonehouse, J.1
Keeler, J.2
-
49
-
-
0030567375
-
Economy in protein design: Evolution of a metal-independent ββα motif based on zinc finger domains
-
Struthers M. D., Cheng R. P., Imperiali B. Economy in protein design: evolution of a metal-independent ββα motif based on zinc finger domains. J. Am. Chem. Soc. 118:1996;3073-3081.
-
(1996)
J. Am. Chem. Soc.
, vol.118
, pp. 3073-3081
-
-
Struthers, M.D.1
Cheng, R.P.2
Imperiali, B.3
-
50
-
-
0029147823
-
Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures
-
Swindells M. B., MacArthur M. W., Thornton J. M. Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures. Nature Struct. Biol. 2:1995;596-603.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 596-603
-
-
Swindells, M.B.1
MacArthur, M.W.2
Thornton, J.M.3
-
51
-
-
0014364651
-
Protein denaturation
-
Tanford C. Protein denaturation. Advan. Protein Chem. 23:1968;121-282.
-
(1968)
Advan. Protein Chem.
, vol.23
, pp. 121-282
-
-
Tanford, C.1
-
52
-
-
0030334742
-
Stabilization of proteins by rational design of a α-helix stability using helix-coil transition theory
-
Villegas V., Viguera A. R., Avilés F. X., Serrano L. Stabilization of proteins by rational design of a α-helix stability using helix-coil transition theory. Folding design. 1:1996;29-32.
-
(1996)
Folding Design
, vol.1
, pp. 29-32
-
-
Villegas, V.1
Viguera, A.R.2
Avilés, F.X.3
Serrano, L.4
-
53
-
-
0029034436
-
Side-chain interactions between sulfur conatining amino acids and phenylalanine in α-helices
-
Viguera A. R., Serrano L. Side-chain interactions between sulfur conatining amino acids and phenylalanine in α-helices. Biochemistry. 34:1995;8771-8779.
-
(1995)
Biochemistry
, vol.34
, pp. 8771-8779
-
-
Viguera, A.R.1
Serrano, L.2
-
54
-
-
0028932770
-
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
-
Viguera A. R., Blanco F. J., Serrano L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247:1995;670-681.
-
(1995)
J. Mol. Biol.
, vol.247
, pp. 670-681
-
-
Viguera, A.R.1
Blanco, F.J.2
Serrano, L.3
-
55
-
-
0030623698
-
Favourable native-like helical local interactions can accelerate protein folding
-
Viguera A. R., Villegas V., Aviles F. X., Serrano L. Favourable native-like helical local interactions can accelerate protein folding. Folding Design. 2:1996;23-33.
-
(1996)
Folding Design
, vol.2
, pp. 23-33
-
-
Viguera, A.R.1
Villegas, V.2
Aviles, F.X.3
Serrano, L.4
-
56
-
-
0025398721
-
WHATIF: A molecular modelling and drug design program
-
Vriend G. WHATIF: a molecular modelling and drug design program. J. Mol. Biol. 8:1990;52-56.
-
(1990)
J. Mol. Biol.
, vol.8
, pp. 52-56
-
-
Vriend, G.1
-
57
-
-
0025328818
-
Secondary structure dependent chemical shifts in proteins
-
Williamson M. P. Secondary structure dependent chemical shifts in proteins. Biopolymers. 29:1990;1423-1431.
-
(1990)
Biopolymers
, vol.29
, pp. 1423-1431
-
-
Williamson, M.P.1
-
58
-
-
0029058159
-
An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
-
Wouters M. A., Curmi P. M. G. An analysis of side chain interactions and pair correlations within antiparallel β-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins: Struct. Funct. Genet. 22:1995;119-131.
-
(1995)
Proteins: Struct. Funct. Genet.
, vol.22
, pp. 119-131
-
-
Wouters, M.A.1
Curmi, P.M.G.2
|