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Volumn 125, Issue 31, 2003, Pages 9280-9281

Effect of catenation on protein folding stability

Author keywords

[No Author keywords available]

Indexed keywords

CATENANE; DIMER; PROTEIN;

EID: 0042709601     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0355978     Document Type: Article
Times cited : (37)

References (15)
  • 8
    • 0042017011 scopus 로고    scopus 로고
    • note
    • Topologically it is not possible to pass from an interlocked to an uninterlocked configuration. However, physically the fictitious intermediate state is a special case of the unfolded state, where all interactions between the two circular chains are turned off.
  • 9
    • 0043018841 scopus 로고    scopus 로고
    • note
    • u (r) was approximated by a Gaussian distribution.
  • 11
    • 0042517825 scopus 로고    scopus 로고
    • note
    • lin on denaturant concentration. However, this difference may arise primarily from the different interactions with the denaturant by the catenated and dimeric variants in the unfolded state.
  • 12
    • 0042017010 scopus 로고    scopus 로고
    • note
    • cycl B were found to be 1.55, 2.13, 2.35, 2.47, 2.51, and 2.49, respectively. On the other hand, assuming that a and b scale with the lengths of the circular chains, C were predicted to be 0.14, 0.12, 0.10, 0.09, 0.08, and 0.07 M. respectively.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.