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Volumn 125, Issue 38, 2003, Pages 11500-11501

Triple-helix propensity of hydroxyproline and fluoroproline: Comparison of host-guest and repeating tripeptide collagen models

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; FLUOROPROLINE; HYDROXYPROLINE; PEPTIDE; PROLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0141757465     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja036673+     Document Type: Article
Times cited : (83)

References (30)
  • 2
    • 0001765479 scopus 로고
    • Ramachandran, G. N., Ed.; Academic Press: New York
    • (b) Ramachandran, G. N. In Treatise on Collagen; Ramachandran, G. N., Ed.; Academic Press: New York, 1964; pp 103-183.
    • (1964) Treatise on Collagen , pp. 103-183
    • Ramachandran, G.N.1
  • 24
    • 0141827587 scopus 로고    scopus 로고
    • note
    • 10 were obtained from Peptide International.
  • 25
    • 0141827586 scopus 로고    scopus 로고
    • note
    • m determination did not exceed ±0.5 °C.
  • 26
    • 0141604534 scopus 로고    scopus 로고
    • note
    • The host-guest peptides are designated by the three-letter amino acid sequence of its guest Gly-Xaa-Yaa triplet.
  • 27
    • 0141492917 scopus 로고    scopus 로고
    • note
    • Differential scanning calorimetry (DSC) experiments were performed on a Nano-DSC II (Calorimetry Sciences Corp., model 6100) instrument at scan rates 0.05-1.0 °C/min. The peptide concentration was 1.0 mg/mL in PBS, pH 7.0. Calorimetric enthalpy values obtained by temperature integration of excess heat capacity experimental data were independent of the scanning rate within the experimental error of ±10 kJ/mol.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.