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Volumn 69, Issue 2 1, 2004, Pages

Model study of protein unfolding by interfaces

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; CRYSTAL LATTICES; ENERGY GAP; FREE ENERGY; GROUND STATE; HYDROPHOBICITY; MATHEMATICAL MODELS; THERMODYNAMIC STABILITY;

EID: 37649026588     PISSN: 1063651X     EISSN: None     Source Type: Journal    
DOI: 10.1103/PhysRevE.69.021907     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 33645086008 scopus 로고    scopus 로고
    • note
    • Even though the term "surface" is used in most experimental and theoretical papers, we will here use the more correct term "interface" instead, leaving the former term to denote the protein surface.
  • 24
    • 33645074030 scopus 로고    scopus 로고
    • note
    • Kandori et al., measured the saturated adsorbed amount for lysozyme and bovine serum albumin as a function of the degree of hydrophobicity of the interface. The interface in this case is initially pure calcium hydroxyapatite (hydrophilic), but becomes more hydrophobic as oleyl phosphate molecules are adsorbed on it [23]. The work focused on the adsorbed amount of protein and did not study the conformational changes.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.