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Volumn 126, Issue 23, 2004, Pages 7238-7243

Enhanced hairpin stability through loop design: The case of the protein G B1 domain hairpin

Author keywords

[No Author keywords available]

Indexed keywords

COULOMB BLOCKADE; HYDROPHOBICITY; MELTING; STRUCTURE (COMPOSITION);

EID: 2942562092     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0379520     Document Type: Article
Times cited : (165)

References (50)
  • 6
    • 2942542185 scopus 로고    scopus 로고
    • note
    • 2O data range was 55 ± (vide infra and Supporting Information), with a fold population estimate of 30% at 298 K.
  • 34
    • 2942522088 scopus 로고    scopus 로고
    • note
    • 12 mutants (GB1m1 and HP5A).
  • 39
    • 2942542184 scopus 로고    scopus 로고
    • note
    • 37 that cannot form hairpin structures.
  • 45
    • 2942575424 scopus 로고    scopus 로고
    • note
    • There are some exceptions to the CSDs predicted by Figure 1; these are attributed to ring current shifts that are in the opposite direction of the diamagnetic anisotropy effects due to backbone amide units.
  • 47
    • 2942575425 scopus 로고    scopus 로고
    • note
    • 7 assumed a significantly larger fold population, we suggest that the conclusions may need to be reevaluated in light of the present study. In addition, GB1p should no longer be viewed as the model for folding simulations of β hairpins as there are many better-folded β-hairpin structures available.
  • 49
    • 2942600680 scopus 로고    scopus 로고
    • note
    • Derived from the fraction folded values for GB1p and GB1m2 at 25 °C.
  • 50
    • 2942545368 scopus 로고    scopus 로고
    • note
    • Derived from the fraction folded values for GB1m2 and GB1m3 at 37 °C; the higher temperature was selected since the calculated folded fraction of GB1m3 is less influenced by the choice of the 100% folded shift values at this temperature.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.