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Volumn 42, Issue 2, 2001, Pages 237-242

A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin

Author keywords

lactalbumin; Denatured state; Hydrophobic interactions; Molten globule; Protein folding

Indexed keywords

ALPHA LACTALBUMIN;

EID: 0035254984     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20010201)42:2<237::AID-PROT110>3.0.CO;2-B     Document Type: Conference Paper
Times cited : (22)

References (24)
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    • Proline scanning mutagenesis study of a molten globule reveals non-cooperative formation of a protein's overall topology
    • (1996) Nat Struct Biol , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 10
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • (1996) FASEB J , vol.10 , pp. 102-108
    • Kuwajima, K.1
  • 14
  • 15
    • 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
  • 20
    • 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
  • 24


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.