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Volumn 318, Issue 2, 2002, Pages 571-582

pH-dependent stability and folding kinetics of a protein with an unusual α-β topology: The C-terminal domain of the ribosomal protein L9

Author keywords

Linkage relationship; pH dependent folding; Protein folding; Protein stability; Ribosomal protein L9

Indexed keywords

HISTIDINE; RIBOSOME PROTEIN; RIBOSOME PROTEIN L9; UNCLASSIFIED DRUG;

EID: 0036302125     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00015-3     Document Type: Article
Times cited : (39)

References (39)
  • 7
    • 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
  • 15
    • 0033551039 scopus 로고    scopus 로고
    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state: Differentiation between local and nonlocal interactions
    • (1999) Biochemistry , vol.38 , pp. 4896-4903
    • Kuhlman, B.1    Luisi, D.L.2    Young, P.3    Raleigh, D.P.4
  • 16
    • 0033612227 scopus 로고    scopus 로고
    • Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9
    • (1999) J. Mol. Biol. , vol.289 , pp. 167-174
    • Luisi, D.L.1    Kuhlman, B.2    Sideras, K.3    Evans, P.A.4    Raleigh, D.P.5
  • 17
    • 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
  • 21
    • 0034712675 scopus 로고    scopus 로고
    • pH jump studies of the folding of the multidomain ribosomal protein L9: The structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain
    • (2000) Biochemistry , vol.39 , pp. 4955-4962
    • Sato, S.1    Luisi, D.L.2    Raleigh, D.P.3
  • 34
    • 0035929243 scopus 로고    scopus 로고
    • 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
    • (2001) J. Mol. Biol. , vol.312 , pp. 569-577
    • Sato, S.1    Xiang, S.2    Raleigh, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.