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Volumn 7, Issue 9, 1999, Pages 2021-2026

CH/π interaction in the conformation of peptides. A database study

Author keywords

CH interaction; Conformation; CSD; Database; Peptide

Indexed keywords

ARTICLE; CRYSTAL STRUCTURE; MOLECULAR INTERACTION; PEPTIDE ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0032836467     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(99)00123-6     Document Type: Article
Times cited : (88)

References (72)
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    • See ref 1, Chapter 5
    • See ref 1, Chapter 5.
  • 9
    • 20544433165 scopus 로고
    • 2-carbon:
    • 2-carbon: Bondi, A. J. Phys. Chem. 1964, 68, 441-451.
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-451
    • Bondi, A.1
  • 10
    • 37049068703 scopus 로고
    • Discrimination of the CH/π interaction from the attractive part of the van der Waals force is difficult. The CH/π interaction includes the dispersion force, however, contribution from the delocalization mechanism is also important The van der Waals force (hence the van der Waals distance) is an ambiguous concept representing a blend of a variety of non-specific interactions. For discussions regarding the nature of the CH/π interaction, see refs 1 and 7
    • Discrimination of the CH/π interaction from the attractive part of the van der Waals force is difficult. The CH/π interaction includes the dispersion force, however, contribution from the delocalization mechanism is also important (Takagi, T.; Tanaka, A.; Matsuo, S.; Maezaki, H.; Tani, M.; Fujiwara, H.; Sasaki, Y. J. Chem. Soc., Perkin Trans. 2 1987, 1015-1018). The van der Waals force (hence the van der Waals distance) is an ambiguous concept representing a blend of a variety of non-specific interactions. For discussions regarding the nature of the CH/π interaction, see refs 1 and 7.
    • (1987) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1015-1018
    • Takagi, T.1    Tanaka, A.2    Matsuo, S.3    Maezaki, H.4    Tani, M.5    Fujiwara, H.6    Sasaki, Y.7
  • 11
    • 0344800257 scopus 로고    scopus 로고
    • Only entries with hydrogen coordinates were collected
    • Only entries with hydrogen coordinates were collected.
  • 12
    • 0344800258 scopus 로고    scopus 로고
    • The C-H bond distance was corrected to a standard value of 1.083 Å in the CSD software
    • The C-H bond distance was corrected to a standard value of 1.083 Å in the CSD software.
  • 13
    • 0345663261 scopus 로고    scopus 로고
    • The dotted lines in Figures 3-9 were drawn by use of our CHPI program after optimizing the hydrogen coordinates
    • The dotted lines in Figures 3-9 were drawn by use of our CHPI program after optimizing the hydrogen coordinates.
  • 54
    • 0344800225 scopus 로고    scopus 로고
    • Refs 28 and 29 (bitterness)
    • Refs 28 and 29 (bitterness).
  • 57
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    • Ref. 34 (antisickling)
    • Ref. 34 (antisickling).
  • 59
    • 0344368441 scopus 로고    scopus 로고
    • Refs 48-51 (enzyme inhibitory activity)
    • Refs 48-51 (enzyme inhibitory activity).
  • 63
    • 0345663195 scopus 로고    scopus 로고
    • Ref 1, pp 178-181; Tables 11.1 and 11.2
    • Ref 1, pp 178-181; Tables 11.1 and 11.2.
  • 64
    • 0344800221 scopus 로고    scopus 로고
    • Ref. 61, Tables 1 and 2
    • Ref. 61, Tables 1 and 2.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.