메뉴 건너뛰기




Volumn 11, Issue 2, 2002, Pages 381-389

Contributions of folding cores to the thermostabilities of two ribonucleases H

Author keywords

Chimera; Folding core; Heat capacity; Ribonuclease H; Stability curves; Thermodynamic stability of proteins

Indexed keywords

RIBONUCLEASE H;

EID: 0036147997     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.38602     Document Type: Article
Times cited : (27)

References (26)
  • 11
    • 0033596902 scopus 로고    scopus 로고
    • A thermodynamic comparison of mesophilic and thermophilic ribonucleases H
    • (1999) Biochemistry , vol.38 , pp. 3831-3836
  • 25
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 26
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.