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Volumn 13, Issue 39, 2011, Pages 17689-17695

How does trimethylamine N-oxide counteract the denaturing activity of urea?

Author keywords

[No Author keywords available]

Indexed keywords

METHYLAMINE; PROTEIN; TRIMETHYLOXAMINE; UREA;

EID: 80053486881     PISSN: 14639076     EISSN: None     Source Type: Journal    
DOI: 10.1039/c1cp22176k     Document Type: Article
Times cited : (55)

References (93)
  • 28
    • 0026189147 scopus 로고
    • B. Lee Biopolymers 1991 31 993 1008
    • (1991) Biopolymers , vol.31 , pp. 993-1008
    • Lee, B.1
  • 38
    • 0035950781 scopus 로고    scopus 로고
    • a(intra), could not be able to counterbalance its magnitude (i.e., several of the strong interactions of charged side chains with water cannot be adequately replaced in the interior of a globular fold), and so a native globular conformation would be less stable thermodynamically than the unfolded ones. This should be the case of natively unfolded proteins
    • G. Graziano B. Lee J. Phys. Chem. B 2001 105 10367 10372
    • (2001) J. Phys. Chem. B , vol.105 , pp. 10367-10372
    • Graziano, G.1    Lee, B.2
  • 66
    • 26944481188 scopus 로고    scopus 로고
    • D. Chandler Nature 2005 437 640 647
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.