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Volumn 100, Issue 36, 1996, Pages 14995-15004

Determination of the three-dimensional structure of a new crystalline form of N-acetyl-Pro-Gly-Phe as revealed by 13C REDOR, X-ray diffraction, and molecular dynamics calculation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33748501698     PISSN: 00223654     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp960179t     Document Type: Article
Times cited : (59)

References (59)
  • 26
    • 33748490922 scopus 로고    scopus 로고
    • note
    • 15N distances by this treatment as a three-spin system were found to be 3.46 and 4.12 Å, respectively. These data are obviously within the claimed level of error as ±0.05 Å evaluated by the present two-spin system.
  • 43
    • 85087582863 scopus 로고    scopus 로고
    • note
    • 27,31,32 This is not the case, however, when the two peaks crossed over at certain Ψ angles.
  • 44
    • 33748500901 scopus 로고    scopus 로고
    • note
    • This does not necessarily mean that the accurate REDOR parameters are available with a longer π pulse such as 50 μs even if the condition of 10% of the rotor cycle is satisfied. This is because utilization of a longer π pulse may cause an additional error caused by insufficient excitation range for the entire spin system.
  • 45
    • 33748513341 scopus 로고    scopus 로고
    • note
    • 2 value for the carbonyl carbon was 27.4 ms under the present spectrometer condition.
  • 53
    • 33748482052 scopus 로고    scopus 로고
    • note
    • 36
  • 54
    • 33748492829 scopus 로고    scopus 로고
    • note
    • 2).
  • 57
    • 33748514244 scopus 로고    scopus 로고
    • The broadened shoulder peak was unequivocally assigned to the Cγ carbon in view of the present X-ray diffraction and MD simulation data
    • The broadened shoulder peak was unequivocally assigned to the Cγ carbon in view of the present X-ray diffraction and MD simulation data.
  • 58
    • 33748498538 scopus 로고    scopus 로고
    • note
    • 43 Therefore, the force field used here is suitable for determination of the conformations of the peptide, which is very flexible.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.