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Volumn 105, Issue 4, 2001, Pages 867-879

Study of the opsin shift of bacteriorhodopsin: insight from QM/MM calculations with electronic polarization effects of the protein environment

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; AMINO ACIDS; BAND STRUCTURE; CHROMOPHORES; ELECTRONIC STRUCTURE; ELECTROSTATICS; GROUND STATE; POLARIZATION; QUANTUM THEORY;

EID: 0034818544     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp0032863     Document Type: Article
Times cited : (82)

References (60)
  • 23
    • 0001491955 scopus 로고    scopus 로고
    • See for reviews: (a) Gao, J. Acc. Chem. Res. 1996, 29, 298.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 298
    • Gao, J.1
  • 38
    • 0004205195 scopus 로고    scopus 로고
    • Fujitsu Ltd.: Tkyo, Japan
    • Stewart, J. J. P. MOPAC2000; Fujitsu Ltd.: Tkyo, Japan, 1999.
    • (1999) MOPAC2000
    • Stewart, J.J.P.1
  • 56
    • 33645899533 scopus 로고    scopus 로고
    • note
    • If one adopts atom-centered polarizable dipole approximation, the Fock matrix elements involving dipole-electron interactions must be evaluated. In refs 18 and 43, these integrals were approximately evaluated after expansion of the dipole into a set of six point charges.
  • 60
    • 33645924294 scopus 로고    scopus 로고
    • note
    • In all the bR structures which we examined so far (refs 30 and 48-50), there are seven aromatic residues (W86A, W138A, W182A, W189A, Y83A, Y185A, and F208A) surrounding the chromophore and no significant difference in their side chain orientations. Therefore, the use of the structures other than 2BRD would not affect the main conclusion of this study, insisting the dominant role of these residues in causing the opsin shift of bR.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.