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PS-PEG-trityl chloride resin was prepared from PS-PEG-trityl alcohol resin (Novabiochem NovaSyn TGT alcohol resin) by treatment with acetyl chloride, as described in the Novabiochem catalog
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PS-PEG-trityl chloride resin was prepared from PS-PEG-trityl alcohol resin (Novabiochem NovaSyn TGT alcohol resin) by treatment with acetyl chloride, as described in the Novabiochem catalog.
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2O solution.
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α values (average of 0.05 ppm) than those of peptide 6 (Figure 3). This slight downfield shifting of the peptide 3a monomer suggests a somewhat greater population of β-strand conformer.
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α values (average of 0.05 ppm) than those of peptide 6 (Figure 3). This slight downfield shifting of the peptide 3a monomer suggests a somewhat greater population of β-strand conformer.
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34247845026
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NOEs among side chains that might arise from further self-association of the dimers cannot be distinguished from those resulting from folding and dimerization
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NOEs among side chains that might arise from further self-association of the dimers cannot be distinguished from those resulting from folding and dimerization.
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Exchange between the monomer and the oligomer occurs relatively slowly, on the time scale of the PFG NMR experiment, and has little effect on the diffusion coefficients observed for either species
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Exchange between the monomer and the oligomer occurs relatively slowly, on the time scale of the PFG NMR experiment, and has little effect on the diffusion coefficients observed for either species.
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, vol.61
, pp. 103-124
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Teller, D.C.1
Swanson, E.2
DeHaen, C.3
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85
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0003836410
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Beckman Instruments, Inc, Palo Alto, CA
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(b) McRorie, D. K.; Voelker, P. J. Self-Associating Systems in the Analytical Ultracentrifugation; Beckman Instruments, Inc.: Palo Alto, CA, 1993.
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(1993)
Self-Associating Systems in the Analytical Ultracentrifugation
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McRorie, D.K.1
Voelker, P.J.2
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86
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33748565349
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(c) Howlett, G. J.; Minton, A. P.; Rivas, G. Curr. Opin. Chem. Biol. 2006, 10, 430-436.
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(2006)
Curr. Opin. Chem. Biol
, vol.10
, pp. 430-436
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Howlett, G.J.1
Minton, A.P.2
Rivas, G.3
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87
-
-
34247899590
-
-
2O solution without NaCl. This result indicates that the oligomerization states do not change upon adding NaCl.
-
2O solution without NaCl. This result indicates that the oligomerization states do not change upon adding NaCl.
-
-
-
-
90
-
-
34247892864
-
-
3/g according to ref 36b.
-
3/g according to ref 36b.
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-
-
-
91
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33744816438
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Scott, D. J, Harding, S. E, Rowe, A. J, Eds, Royal Society of Chemistry: U.K
-
(a) Demeler, B. In Modern Analytical Ultracentrifugation: Techniques and Methods; Scott, D. J., Harding, S. E., Rowe, A. J., Eds.; Royal Society of Chemistry: U.K., 2005; pp 210-229.
-
(2005)
Modern Analytical Ultracentrifugation: Techniques and Methods
, pp. 210-229
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-
Demeler, B.1
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92
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34247846781
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-
(b) http://www.ultrascan.uthscsa.edu.
-
-
-
-
94
-
-
24144485161
-
-
Finite element analysis of the data from the 39 μM experiment suggests that this peak corresponds to the monomer. For a description of finite element analysis, see: (a) Cao, W.; Demeler, B. Biophys. J. 2005, 89, 1589-1602.
-
Finite element analysis of the data from the 39 μM experiment suggests that this peak corresponds to the monomer. For a description of finite element analysis, see: (a) Cao, W.; Demeler, B. Biophys. J. 2005, 89, 1589-1602.
-
-
-
-
96
-
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0019756004
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Johnson, M. L.; Correia, J. J.; Yphantis, D. A.; Halvorson, H. R. Biophys. J. 1981, 36, 575-588.
-
(1981)
Biophys. J
, vol.36
, pp. 575-588
-
-
Johnson, M.L.1
Correia, J.J.2
Yphantis, D.A.3
Halvorson, H.R.4
-
97
-
-
34247871912
-
-
The UV-absorbance data from the 15 μM samples (g and h) are scaled to fringes and appear relatively shallow because they are plotted on the same scale as the data from the 1.5 and 9 mM experiments.
-
The UV-absorbance data from the 15 μM samples (g and h) are scaled to fringes and appear relatively shallow because they are plotted on the same scale as the data from the 1.5 and 9 mM experiments.
-
-
-
-
98
-
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14944368141
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-
Foss, T. R.; Kelker, M. S.; Wiseman, R. L.; Wilson, I. A.; Kelly, J. W. J. Mol. Biol. 2005, 347, 841-854.
-
(2005)
J. Mol. Biol
, vol.347
, pp. 841-854
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Foss, T.R.1
Kelker, M.S.2
Wiseman, R.L.3
Wilson, I.A.4
Kelly, J.W.5
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99
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0028132243
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-
Hagihara, Y.; Oobatake, M.; Goto, Y. Protein Sci. 1994, 3, 1418-1429.
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(1994)
Protein Sci
, vol.3
, pp. 1418-1429
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-
Hagihara, Y.1
Oobatake, M.2
Goto, Y.3
-
100
-
-
34247866991
-
-
The ionization state of the GIu residue in peptides 3b and 3h is not certain, because the studies were done without buffer. Attempts to control the pH with phosphate buffer resulted in precipitation of these peptides.
-
The ionization state of the GIu residue in peptides 3b and 3h is not certain, because the studies were done without buffer. Attempts to control the pH with phosphate buffer resulted in precipitation of these peptides.
-
-
-
-
101
-
-
34247886499
-
-
2/s, respectively, which are about the same as those values for the monomer and tetramer of peptide 3a. The ratio of these values (0.57) is consistent with tetramer formation.
-
2/s, respectively, which are about the same as those values for the monomer and tetramer of peptide 3a. The ratio of these values (0.57) is consistent with tetramer formation.
-
-
-
-
102
-
-
34247890609
-
-
2/s, which is about the same as that of the tetramer of peptide 3a at the same temperature.
-
2/s, which is about the same as that of the tetramer of peptide 3a at the same temperature.
-
-
-
-
103
-
-
34247862788
-
-
The diffusion coefficients of the oligomers of peptides 3j and 3k are about 0.80-0.85 times that of the tetramer of peptide 3a. The smaller diffusion coefficients of these peptides suggest that peptides 3j and 3k form higher oligomers, such as hexamers or octamers, rather than tetramers. ROESY experiments show that the oligomers of these peptides comprise edge-to-edge dimers. The higher oligomers may be thought of as small micelles in which the hydrophobic faces of the β-sheet dimers form a hydrophobic core.
-
The diffusion coefficients of the oligomers of peptides 3j and 3k are about 0.80-0.85 times that of the tetramer of peptide 3a. The smaller diffusion coefficients of these peptides suggest that peptides 3j and 3k form higher oligomers, such as hexamers or octamers, rather than tetramers. ROESY experiments show that the oligomers of these peptides comprise edge-to-edge dimers. The higher oligomers may be thought of as small micelles in which the hydrophobic faces of the β-sheet dimers form a hydrophobic core.
-
-
-
-
104
-
-
34247878253
-
-
We have observed similar improvements in the folding of the 42-membered-ring macrocyclic peptides 2 upon placing Phe across from the aromatic ring of Hao. For details, see ref 18
-
We have observed similar improvements in the folding of the 42-membered-ring macrocyclic peptides 2 upon placing Phe across from the aromatic ring of Hao. For details, see ref 18.
-
-
-
-
106
-
-
34247873548
-
-
2O solution of peptide 3m from 1.0 mM to 16.0 mM results in similar downfield shifting.
-
2O solution of peptide 3m from 1.0 mM to 16.0 mM results in similar downfield shifting.
-
-
-
-
107
-
-
0030932886
-
-
For a notable exception, see: a
-
For a notable exception, see: (a) Li, H.; Dunn, J. J.; Luft, B. J.; Lawson, C. L. Proc Natl. Acad. Sci. U.S.A. 1997, 94, 3584-3589.
-
(1997)
Proc Natl. Acad. Sci. U.S.A
, vol.94
, pp. 3584-3589
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Li, H.1
Dunn, J.J.2
Luft, B.J.3
Lawson, C.L.4
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108
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0034719388
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(b) Koide, S.; Huang, X.; Link, K.; Koide, A.; Bu, Z.; Engelman, D. M. Nature 2000, 403, 456-460.
-
(2000)
Nature
, vol.403
, pp. 456-460
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-
Koide, S.1
Huang, X.2
Link, K.3
Koide, A.4
Bu, Z.5
Engelman, D.M.6
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