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Volumn 113, Issue 7, 2009, Pages 2143-2150

Interaction of bovine serum albumin with dipolar molecules: Fluorescence and molecular docking studies

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; BINDING ENERGY; BINDING SITES; BODY FLUIDS; CHARGE TRANSFER; DOCKING; FLEXIBLE STRUCTURES; HYDROPHOBICITY; ION EXCHANGE; MOLECULES; SULFUR COMPOUNDS;

EID: 65249136509     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp808611b     Document Type: Article
Times cited : (134)

References (81)
  • 12
    • 0003476266 scopus 로고
    • Lakowicz, J. R, Ed, Plenum Press: New York
    • (a) Topics in Fluorescence Spectroscopy; Lakowicz, J. R., Ed.; Plenum Press: New York, 1994; Vol 4.
    • (1994) Topics in Fluorescence Spectroscopy , vol.4
  • 15
    • 0003476266 scopus 로고
    • Lakowicz, J. R, Ed, Plenum Press: New York
    • (b) Topics in Fluorescence Spectroscopy; Lakowicz, J. R., Ed.; Plenum Press: New York, 1994; Vol 2.
    • (1994) Topics in Fluorescence Spectroscopy , vol.2
  • 23
    • 84906396634 scopus 로고    scopus 로고
    • A preliminary study reveals complex time-dependent anisotropy profiles for some probe molecules in human serum albumin as well. These results will be published at a later stage
    • A preliminary study reveals complex time-dependent anisotropy profiles for some probe molecules in human serum albumin as well. These results will be published at a later stage.
  • 64
    • 84906371913 scopus 로고    scopus 로고
    • Refer to Figure S1 of the Supporting Information provided.
    • Refer to Figure S1 of the Supporting Information provided.
  • 67
    • 84906357456 scopus 로고    scopus 로고
    • Figure S2 of the Supporting Information shows 88% homology in the sequences of the BSA model and 1A06 (HSA).
    • Figure S2 of the Supporting Information shows 88% homology in the sequences of the BSA model and 1A06 (HSA).
  • 76
    • 84906396631 scopus 로고    scopus 로고
    • Figure S3 of the Supporting Information shows the structural overlay of the BSA model and 1A06.
    • Figure S3 of the Supporting Information shows the structural overlay of the BSA model and 1A06.
  • 77
    • 84906411071 scopus 로고    scopus 로고
    • Figure S4 of the Supporting Information provides the structural validation of BSA model.
    • Figure S4 of the Supporting Information provides the structural validation of BSA model.
  • 78
    • 84906396632 scopus 로고    scopus 로고
    • The docking energies of the molecules (in kcal/mol) obtained from AutoDock are-8.02 (C102),-8.25 (C153),-7.26 (C120),-7.04 (C152),- 6.83 (C1),-7.70 (HNBD),-7.99 (MNBD),-8.24 (4NBD),-9.13 (6NBD), and-8.51 (7NBD).
    • The docking energies of the molecules (in kcal/mol) obtained from AutoDock are-8.02 (C102),-8.25 (C153),-7.26 (C120),-7.04 (C152),- 6.83 (C1),-7.70 (HNBD),-7.99 (MNBD),-8.24 (4NBD),-9.13 (6NBD), and-8.51 (7NBD).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.