메뉴 건너뛰기




Volumn , Issue 27, 2007, Pages 2814-2816

Bend-ribbon forming γ-peptides

Author keywords

[No Author keywords available]

Indexed keywords

C PEPTIDE; HYDROGEN;

EID: 34447132259     PISSN: 13597345     EISSN: None     Source Type: Journal    
DOI: 10.1039/b706528k     Document Type: Article
Times cited : (31)

References (33)
  • 24
    • 34447128359 scopus 로고    scopus 로고
    • A series of oligomers (dimer, trimer, tetramer, pentamer) up to the hexamer level was prepared for the heterochiral series
    • A series of oligomers (dimer, trimer, tetramer, pentamer) up to the hexamer level was prepared for the heterochiral series
  • 30
    • 34447114677 scopus 로고    scopus 로고
    • 1H NMR spectrum of hexamer 7 is complicated by resonance overlap and unambiguous assignment of every resonance was not possible. However, a pentameric derivative was completely assigned and demonstrated an analogous pattern to tetramer 4
    • Residues are labelled alphabetically from the N- to the C-terminus, with protons within each residue being numbered from the highest ranking carbon according to IUPAC recommendations
  • 32
    • 34447129804 scopus 로고    scopus 로고
    • i+1 hydrogen bonds would produce the same pattern of shielded and deshielded amide protons but would require a hydrogen bond to the C-terminal ester (and is inconsistent with the patterns of NOE enhancements observed)
    • i+1 hydrogen bonds would produce the same pattern of shielded and deshielded amide protons but would require a hydrogen bond to the C-terminal ester (and is inconsistent with the patterns of NOE enhancements observed)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.