메뉴 건너뛰기




Volumn 49, Issue 1, 2002, Pages 95-103

Effects of a helix substitution on the folding mechanism of bovine α-lactalbumin

Author keywords

lactalbumin; Chimera; Molten globule; Non native interaction; Protein folding

Indexed keywords

ALPHA LACTALBUMIN; AMINO ACID; GUANIDINE; LYSOZYME;

EID: 0036782097     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10185     Document Type: Article
Times cited : (6)

References (58)
  • 1
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 4
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 10
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 16
    • 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
  • 18
    • 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) Nat Struct Biol , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 32
    • 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
  • 34
    • 0029245364 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction
    • (1995) Mol Biotechnol , vol.3 , pp. 1-7
    • Barik, S.1
  • 37
    • 0015438810 scopus 로고
    • The preparation of guanidine hydrochloride
    • Hirs CH, Timasheff SN, editors. New York and London: Academic Press
    • (1972) Methods in enzymology , vol.26 , pp. 43-50
    • Nozaki, Y.1
  • 38
    • 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
  • 39
    • 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
  • 48
    • 0034141812 scopus 로고    scopus 로고
    • Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of non-native structure in the denatured state
    • (2000) Proteins , vol.38 , pp. 189-196
    • Demarest, S.J.1    Raleigh, D.P.2
  • 50
    • 0033153245 scopus 로고    scopus 로고
    • Local interactions drive the formation of non-native structure in the denatured state of human α-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution
    • (1999) Biochemistry , vol.38 , pp. 7380-7387
    • Demarest, S.J.1    Hua, Y.2    Raleigh, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.