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Volumn 310, Issue 2, 2001, Pages 471-484

Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin

Author keywords

Cold denaturation; Hydrogen deuterium exchange; NMR; Small angle X ray scattering; lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN; DEUTERIUM; HYDROGEN; UREA;

EID: 0035816223     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4777     Document Type: Article
Times cited : (37)

References (60)
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  • 9
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    • The thermodynamics of protein denaturation. II. The denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures
    • (1966) J. Am. Chem. Soc. , vol.89 , pp. 4826-4838
    • Brandts, J.F.1    Hunt, L.2
  • 17
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    • Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates
    • (1997) Biochemistry , vol.36 , pp. 14375-14383
    • Nash, D.1    Jonas, J.2
  • 28
    • 0014226043 scopus 로고
    • Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°
    • (1968) Biochemistry , vol.7 , pp. 198-208
    • Pace, N.C.1    Tanford, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.