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Volumn 31, Issue 6, 1998, Pages 343-350

Protein Charge Ladders, Capillary Electrophoresis, and the Role of Electrostatics in Biomolecular Recognition

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EID: 0000524420     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar970255q     Document Type: Article
Times cited : (42)

References (32)
  • 5
    • 0027919775 scopus 로고
    • Lehn, J.-M. Science 1993, 260, 1762-1763.
    • (1993) Science , vol.260 , pp. 1762-1763
    • Lehn, J.-M.1
  • 26
    • 85033920559 scopus 로고    scopus 로고
    • note
    • Assuming equal reactivities of the ∈-amino groups, the number of regioisomers in the nth rung of a charge ladder is given by the binomial coefficient N!/n!(N - n)!, where N is the total number of ∈-amino groups on the protein.
  • 28
    • 85033926509 scopus 로고    scopus 로고
    • note
    • The resolution of the peaks is not sufficient to investigate the behavior of each rung of the charge ladder in detail. The broadening of the middle rungs of the ladder may indicate heterogeneity in the interaction of the protein derivatives with the ligand.
  • 29
    • 85033921811 scopus 로고    scopus 로고
    • note
    • If a Lys ∈-amino group is part of the active site, or involved in a specific interaction that aids in the formation of structure (e.g., a salt bridge), then acetylation of this group may disrupt the conformation and/or binding properties of the protein.
  • 31
    • 85033935738 scopus 로고    scopus 로고
    • note
    • Separations were performed at 25 °C on a 47 cm silica capillary (40 cm from inlet to detector; i.d. 50 μm) using a running buffer of 25 mM Tris-192 mM Gly (pH 8.4). Detection was at 214 nm.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.