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Volumn 50, Issue 26, 2011, Pages 5843-5846

Characteristic structural parameters for the γ-peptide 14-helix: Importance of subunit preorganization

Author keywords

foldamers; helical structures; NMR spectroscopy; nuclear Overhauser effect; peptides

Indexed keywords

AMINO ACID RESIDUES; CHARACTERISTIC PARAMETER; CRYSTALLOGRAPHIC DATA; FOLDAMERS; HELICAL STRUCTURES; HOMOLOGOUS PEPTIDE; NUCLEAR OVERHAUSER EFFECTS; PREORGANIZATION; STRUCTURAL PARAMETER; SUBSTITUTION PATTERNS;

EID: 79959216979     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201101301     Document Type: Article
Times cited : (49)

References (64)
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    • For discussion of the β-peptide 14-, 12-, 10/12- and 10-helices, see Ref. [2a]. For the 14/16-helix, see
    • For discussion of the β-peptide 14-, 12-, 10/12- and 10-helices, see Ref. [2a]. For the 14/16-helix, see:, M. I. Mándity, E. Wéber, T. A. Martinek, G. Olajos, G. K. Tõth, E. Vass, F. Fülöp, Angew. Chem. 2009, 121, 2205-2209
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    • Mándity, M.I.1    Wéber, E.2    Martinek, T.A.3    Olajos, G.4    Tõth, G.K.5    Vass, E.6    Fülöp, F.7
  • 12
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    • For recent developments with 12-helical β-peptides, see
    • Angew. Chem. Int. Ed. 2009, 48, 2171-2175. For recent developments with 12-helical β-peptides, see
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  • 14
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    • Angew. Chem. Int. Ed. 2010, 49, 8232-8236
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    • Extensive crystallographic characterization has recently been reported for urea-based oligomers that adopt a helical conformation that is quasi-isostructural with the γ-peptide 14-helix
    • Extensive crystallographic characterization has recently been reported for urea-based oligomers that adopt a helical conformation that is quasi-isostructural with the γ-peptide 14-helix:, L. Fischer, P. Claudon, N. Pendem, E. Miclet, C. Didierjean, E. Ennifar, G. Guichard, Angew. Chem. 2010, 122, 1085-1088
    • (2010) Angew. Chem. , vol.122 , pp. 1085-1088
    • Fischer, L.1    Claudon, P.2    Pendem, N.3    Miclet, E.4    Didierjean, C.5    Ennifar, E.6    Guichard, G.7
  • 41
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    • Despite the structural similarity of the oligourea and γ-peptide helices, however, the backbone difference can lead to profound functional differences
    • Angew. Chem. Int. Ed. 2010, 49, 1067-1070. Despite the structural similarity of the oligourea and γ-peptide helices, however, the backbone difference can lead to profound functional differences
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 1067-1070
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    • See the Supporting Information for details
    • See the Supporting Information for details.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.