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Volumn 122, Issue 18, 2005, Pages

Retention of nativelike conformation by proteins embedded in high external electric fields

Author keywords

[No Author keywords available]

Indexed keywords

EXTERNAL ELECTRIC FIELDS; FIELD-INDUCED CONFORMATIONAL ALTERNATION; INTERELECTRODE; PROTEIN IMMOBILIZATION;

EID: 18844396418     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.1902903     Document Type: Article
Times cited : (11)

References (21)
  • 15
    • 33645941402 scopus 로고
    • The MEP of azurin from Pseudomonas aeruginosa was computed on the x-ray oxidized protein structure at pH 5.5 (molecule A in the PDB file 4azu. http://pdb.gmd.de). The University of Houston Brownian Dynamics (UHBD) software [Ref.], which was employed for the calculation, solves the Poisson equation for the charge distribution that characterizes the protein residues in the protonation state that depends on the pH. The OPLS [W. L. Jorgensen and J. Tirado-Rives, J. Am. Chem. Soc. 110, 1657 (1988)] nonbonded parameter sets for atomic charges and radii were assigned to the protein residues [Ref.]. In particular, the histidines (His35, His83, His46, His117) were considered protonated, with a proton on each N atom of the pentagonal ring, as pertinent for the acidic pH. The electric field has then been obtained by performing the numerical spatial gradient on the computational grid. Obviously, such a model is not meant to calculate accurate values for the intraprotein electric field, but only to estimate its order of magnitude. This is fully satisfactory for the kind of comparisons that we would like to perform in the present work.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657
    • Jorgensen, W.L.1    Tirado-Rives, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.