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Volumn 334, Issue 6055, 2011, Pages 512-516

The complex folding network of single calmodulin molecules

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALMODULIN; HELIX LOOP HELIX PROTEIN; UBIQUITIN;

EID: 80055087629     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1207598     Document Type: Article
Times cited : (332)

References (36)
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    • M. T. Woodside et al., Science 314, 1001 (2006).
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    • Woodside, M.T.1
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    • 79959830883 scopus 로고    scopus 로고
    • M. B. Borgia et al., Nature 474, 662 (2011).
    • (2011) Nature , vol.474 , pp. 662
    • Borgia, M.B.1
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    • Materials and methods are available as supporting material on
    • Materials and methods are available as supporting material on Science Online.
    • Science Online
  • 29
    • 84922705459 scopus 로고    scopus 로고
    • note
    • At a pretension of 11 pN, the expected length difference from the fully folded state to the fully unfolded state of calmodulin is 19.3 nm, if one assumes a persistence length of 0.5 nm and a contour length gain of 0.365 nm per amino acid residue.
  • 31
  • 35
    • 84922752827 scopus 로고    scopus 로고
    • note
    • -1. This may be explained by considering that, in all those transitions, binding of calcium ions dominates the folding process.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.