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18544386112
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Selected examples: a) B. Gong, H. Q. Zeng, J. Zhu, L. H. Yua, Y. H. Han, S. Z. Cheng, M. Furukawa, R. D. Parra, A. Y. Kovalevsky, J. L. Mills, E. Skrzypczak-Jankun, S. Martinovic, R. D. Smith, C. Zheng, T. Szyperski, X. C. Zeng, Proc. Natl. Acad. Sci. USA 2002, 99, 11583;
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b) B. R. Huck, J. D. Fisk, S. H. Gellman, Org. Lett. 2000, 2, 2607;
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c) Y. Hamuro, S. J. Geib, A. D. Hamilton, J. Am. Chem. Soc. 1996, 118, 7529;
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e) M. Hagihara, N. J. Anthony, T. J. Stout, J. Clardy, S. L. Schreiber, J. Am. Chem. Soc. 1992, 104, 6568.
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Recent examples: a) E. A. Porter, B. Weisblum, S. H. Gellman, J. Am. Chem. Soc. 2002, 124, 7324;
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Porter, E.A.1
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b) U. Arnold, M. P. Hinderaker, B. L. Nilsson, B. R. Huck, S. H. Gellman, R. T. Raines, J. Am. Chem. Soc. 2002, 124, 8522;
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Arnold, U.1
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c) T. L. Raguse, E. A. Porter, B. Weisblum, S. H. Gellman, J. Am. Chem. Soc. 2002,124, 12774;
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Raguse, T.L.1
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0009537812
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f) E. A. Porter, X. Wang, H.-S. Lee, B. Weisblum, S. H. Gellman, Nature 2000, 404, 565;
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Nature
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Porter, E.A.1
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g) M. Werder, H. Hausre, S. Abele, D. Seebach, Helv. Chim. Acta 1999, 82, 1774;
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Werder, M.1
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h) Y. Hamuro, J. P. Schneider, W. F. DeGrado, J. Am. Chem. Soc. 1999, 121, 12200.
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a) V. Pavone, A. Lombardi, X. Yang, C. Pedone, B. D. Blasio, Biopolymers 1990, 30, 189;
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b) V. Pavone, A. Lombardi, G. D'Auria, M. Saviano, F. Nastri, L. Paolillo, B. D. Blasio, C. Pedone, Biopolymers 1992, 32, 173;
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Pavone, V.1
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D'Auria, G.3
Saviano, M.4
Nastri, F.5
Paolillo, L.6
Blasio, B.D.7
Pedone, C.8
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0026230383
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c) B. D. Blasio, A. Lombardi, X. Yang, C. Pedone, V. Pavone, Biopolymers 1991, 31, 1181;
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Blasio, B.D.1
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d) V. Pavone, A. Lombardi, C. A. Maggi, L. Quartara, C. Pedone, J. Pept. Sci. 1995, 1, 236;
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Pavone, V.1
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e) A. Lombardi, M. Saviano, F. Nastri, O. Maglio, M. Mazzeo, C. Isernia, L. Paolillo, V. Pavone, Biopolymers 1996, 38, 693.
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Lombardi, A.1
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Isernia, C.6
Paolillo, L.7
Pavone, V.8
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23
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0842342405
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N. Koglin, C. Zorn, R. Beumer, C. Cabrele, C. Bubert, N. Sewald, O. Reiser, A. G. Beck-Sickinger, Angew. Chem. 2003, 115, 212; Angew. Chem. Int. Ed. 2003, 42, 202.
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Angew. Chem.
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Koglin, N.1
Zorn, C.2
Beumer, R.3
Cabrele, C.4
Bubert, C.5
Sewald, N.6
Reiser, O.7
Beck-Sickinger, A.G.8
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24
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0347296029
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N. Koglin, C. Zorn, R. Beumer, C. Cabrele, C. Bubert, N. Sewald, O. Reiser, A. G. Beck-Sickinger, Angew. Chem. 2003, 115, 212; Angew. Chem. Int. Ed. 2003, 42, 202.
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Angew. Chem. Int. Ed.
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25
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0035479435
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Synthesis and special peptide coupling techniques for 8 and ent-8 have been reported: a) C. Zorn, F. Gnad, S. Salmen, T. Herpin, O. Reiser, Tetrahedron Lett. 2001, 42, 7049;
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Tetrahedron Lett.
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Zorn, C.1
Gnad, F.2
Salmen, S.3
Herpin, T.4
Reiser, O.5
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26
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0034731625
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b) R. Beumer, C. Bubert, C. Cabrele, O. Vielhauer, M. Pietzsch, O. Reiser, J. Org. Chem. 2000, 65, 8960.
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Beumer, R.1
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Vielhauer, O.4
Pietzsch, M.5
Reiser, O.6
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27
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0027975871
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2Me, N-Ac instead of N-Boc) in solution indeed indicate the presence of complete intramolecular hydrogen bonding between CO and NH in cis position. In contrast, the analogous β-alanine derivative does not show any hydrogen bonding, cf. G. P. Dado, S. H. Gellman, J. Am. Chem. Soc. 1994, 116, 1054.
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J. Am. Chem. Soc.
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Dado, G.P.1
Gellman, S.H.2
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28
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0024278597
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Dyson and Wright have established criteria by which partially folded shorter peptides can be identified: H. J. Dyson, M. Rance, R. A. Houghton, R. A. Lerner, P. E. Wright, J. Mol. Biol. 1988, 201, 161; H. J. Dyson, P. E. Wright, Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 519. NOEs between sequential amide protons indicate significant φ,ψ population in the helical part of the Ramachandran plot but medium-range (mainly i,i+2 and i,i+ 3) connectivities are required to unambiguously prove the presence of a helix and thereby distinguish it from interconverting, tumlike structures. Small temperature dependencies of the amide proton chemical shift have also been used as an indication that the amide proton is involved in a hydrogen bond, but it has been argued recently that low-temperature coefficients indicate folding upon temperature lowering instead: H. A. Andersen, J. W. Neidigh, S. M. Harris, G. M. Lee, Z. Liu, H. Tong, J. Am. Chem. Soc. 1997, 119, 8547.
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J. Mol. Biol.
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Dyson, H.J.1
Rance, M.2
Houghton, R.A.3
Lerner, R.A.4
Wright, P.E.5
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29
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0025904730
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Dyson and Wright have established criteria by which partially folded shorter peptides can be identified: H. J. Dyson, M. Rance, R. A. Houghton, R. A. Lerner, P. E. Wright, J. Mol. Biol. 1988, 201, 161; H. J. Dyson, P. E. Wright, Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 519. NOEs between sequential amide protons indicate significant φ,ψ population in the helical part of the Ramachandran plot but medium-range (mainly i,i+2 and i,i+ 3) connectivities are required to unambiguously prove the presence of a helix and thereby distinguish it from interconverting, tumlike structures. Small temperature dependencies of the amide proton chemical shift have also been used as an indication that the amide proton is involved in a hydrogen bond, but it has been argued recently that low-temperature coefficients indicate folding upon temperature lowering instead: H. A. Andersen, J. W. Neidigh, S. M. Harris, G. M. Lee, Z. Liu, H. Tong, J. Am. Chem. Soc. 1997, 119, 8547.
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Annu. Rev. Biophys. Biophys. Chem.
, vol.20
, pp. 519
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Dyson, H.J.1
Wright, P.E.2
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30
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0030858227
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Dyson and Wright have established criteria by which partially folded shorter peptides can be identified: H. J. Dyson, M. Rance, R. A. Houghton, R. A. Lerner, P. E. Wright, J. Mol. Biol. 1988, 201, 161; H. J. Dyson, P. E. Wright, Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 519. NOEs between sequential amide protons indicate significant φ,ψ population in the helical part of the Ramachandran plot but medium-range (mainly i,i+2 and i,i+ 3) connectivities are required to unambiguously prove the presence of a helix and thereby distinguish it from interconverting, tumlike structures. Small temperature dependencies of the amide proton chemical shift have also been used as an indication that the amide proton is involved in a hydrogen bond, but it has been argued recently that low-temperature coefficients indicate folding upon temperature lowering instead: H. A. Andersen, J. W. Neidigh, S. M. Harris, G. M. Lee, Z. Liu, H. Tong, J. Am. Chem. Soc. 1997, 119, 8547.
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J. Am. Chem. Soc.
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Andersen, H.A.1
Neidigh, J.W.2
Harris, S.M.3
Lee, G.M.4
Liu, Z.5
Tong, H.6
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D. A. Case, D. A. Pearlman, J. W. Caldwell, T. E. Cheatham III, J. Wang, W. S. Ross, C. Simmerling, T. Darden, K. M. Merz, R. V. Stanton, A. Cheng, J. J. Vincent, M. Crowley, V. Tsui, H. Gohlke, R. Radmer, Y. Duan, J. Pitera, I. Massova, G. L. Seibel, U. C. Singh, P. Weiner, P. A. Kollman, AMBER 7, University of California, San Francisco, 2002.
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(2002)
AMBER 7
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Case, D.A.1
Pearlman, D.A.2
Caldwell, J.W.3
Cheatham III, T.E.4
Wang, J.5
Ross, W.S.6
Simmerling, C.7
Darden, T.8
Merz, K.M.9
Stanton, R.V.10
Cheng, A.11
Vincent, J.J.12
Crowley, M.13
Tsui, V.14
Gohlke, H.15
Radmer, R.16
Duan, Y.17
Pitera, J.18
Massova, I.19
Seibel, G.L.20
Singh, U.C.21
Weiner, P.22
Kollman, P.A.23
more..
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See also: A. Hayen, M. A. Schmitt, F. N. Ngassa, K. A. Thomasson, S. H. Gellman, Angew. Chem. 2004, 116, 511; Angew. Chem. Int. Ed. 2004, 43, 505.
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Angew. Chem.
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, pp. 511
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Hayen, A.1
Schmitt, M.A.2
Ngassa, F.N.3
Thomasson, K.A.4
Gellman, S.H.5
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See also: A. Hayen, M. A. Schmitt, F. N. Ngassa, K. A. Thomasson, S. H. Gellman, Angew. Chem. 2004, 116, 511; Angew. Chem. Int. Ed. 2004, 43, 505.
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(2004)
Angew. Chem. Int. Ed.
, vol.43
, pp. 505
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