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Volumn 43, Issue 4, 2004, Pages 511-514

Surprisingly Stable Helical Conformations in α/β-Peptides by Incorporation of cis-β-Aminocyclopropane Carboxylic Acids

Author keywords

peptides; amino acids; Foldamers; Helical structures; NMR spectroscopy

Indexed keywords

CARBOXYLIC ACIDS; CONFORMATIONS; STRUCTURE (COMPOSITION);

EID: 0842307523     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200352267     Document Type: Article
Times cited : (202)

References (33)
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    • 0347296029 scopus 로고    scopus 로고
    • 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.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 202
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    • 0027975871 scopus 로고
    • 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.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1054
    • Dado, G.P.1    Gellman, S.H.2
  • 28
    • 0024278597 scopus 로고
    • 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.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161
    • Dyson, H.J.1    Rance, M.2    Houghton, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 29
    • 0025904730 scopus 로고
    • 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.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519
    • Dyson, H.J.1    Wright, P.E.2
  • 30
    • 0030858227 scopus 로고    scopus 로고
    • 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.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8547
    • Andersen, H.A.1    Neidigh, J.W.2    Harris, S.M.3    Lee, G.M.4    Liu, Z.5    Tong, H.6
  • 33
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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.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 505


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.