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Volumn 312, Issue 3, 2001, Pages 569-577

On the relationship between protein stability and folding kinetics: A comparative study of the n-terminal domains of rnase hi, e. coli and Bacillus stearothermophilus l9

Author keywords

Contact order; Protein folding; Protein stability; Ribosomal protein L9

Indexed keywords

BACTERIAL PROTEIN; RIBOSOME PROTEIN;

EID: 0035929243     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4968     Document Type: Article
Times cited : (13)

References (34)
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    • Principles that govern the folding of protein chains
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 5
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 15
  • 18
    • 0033849085 scopus 로고    scopus 로고
    • The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding
    • (2000) Protein Sci. , vol.9 , pp. 1601-1603
    • Sato, S.1    Sayid, C.J.2    Raleigh, D.P.3
  • 19
    • 0034674156 scopus 로고    scopus 로고
    • pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state for folding
    • (2000) J. Mol. Biol. , vol.299 , pp. 1091-1100
    • Luisi, D.L.1    Raleigh, D.P.2
  • 20
    • 0033588313 scopus 로고    scopus 로고
    • NMR Structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9
    • (1999) J. Mol. Biol. , vol.291 , pp. 661-669
    • Evans, S.P.1    Bycroft, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.