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Volumn 298, Issue 5, 2000, Pages 985-995

Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human α-lactalbumin

Author keywords

Chimera; Cooperativity; Molten globule; Protein folding; Lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CHIMERIC PROTEIN; GUANIDINE;

EID: 0034685617     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3705     Document Type: Article
Times cited : (34)

References (70)
  • 23
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 25
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 29
    • 0029112554 scopus 로고
    • Intrinsic stability of individual α-helices modulates structure and stability of the apomyoglobin molten globule form
    • (1995) J. Mol. Biol. , vol.252 , pp. 122-132
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 33
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 42
  • 47
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 51
    • 0030585408 scopus 로고    scopus 로고
    • Crystal structures of guinea-pig, goat and bovine α-lactalbumin: Highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
    • (1996) Structure , vol.4 , pp. 691-703
    • Pike, A.C.W.1    Brew, K.2    Acharya, K.R.3
  • 54
    • 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
  • 57
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method: 1. Unfolding of phenylmethanesulfonyl α-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.