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Volumn 48, Issue 7, 2009, Pages 1271-1274

Self-assembly of one- And two-dimensional hemoprotein systems by polymerization through heme-heme pocket interactions

Author keywords

Cytochrome b562; Heme proteins; Protein modifications; Self assembly; Supramolecular chemistry

Indexed keywords

MACROMOLECULES; POLYMERS; PORPHYRINS; PROTEINS; SELF ASSEMBLY; SUPRAMOLECULAR CHEMISTRY; TWO DIMENSIONAL;

EID: 60149083374     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200804006     Document Type: Article
Times cited : (72)

References (33)
  • 7
    • 34547186405 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2007, 46, 5510-5514.
    • (2007) Angew. Chem. Int. Ed , vol.46 , pp. 5510-5514
  • 10
    • 0142119372 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2003, 42, 4640-4643.
    • (2003) Angew. Chem. Int. Ed , vol.42 , pp. 4640-4643
  • 12
    • 84890574176 scopus 로고    scopus 로고
    • Eds, C. A. Mirkin, C. M. Niemeyer, Wiley-VCH, Weinheim
    • M. G. Ryadnov, D. N. Woolfson in Nanobiotechnology II (Eds.: C. A. Mirkin, C. M. Niemeyer), Wiley-VCH, Weinheim, 2007, pp. 17-38.
    • (2007) Nanobiotechnology II , pp. 17-38
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 16
    • 60149096708 scopus 로고    scopus 로고
    • 562.
    • 562.
  • 25
    • 60149105588 scopus 로고    scopus 로고
    • 562(H63C) was confirmed by ESITOF mass spectrometry (see the Supporting Information).
    • 562(H63C) was confirmed by ESITOF mass spectrometry (see the Supporting Information).
  • 28
    • 60149097612 scopus 로고    scopus 로고
    • 562(H63C) protein was well-immobilized on the hydrophobic HOPG substrate, but it does not form fibers on hydrophilic mica under the same conditions.
    • 562(H63C) protein was well-immobilized on the hydrophobic HOPG substrate, but it does not form fibers on hydrophilic mica under the same conditions.
  • 29
    • 60149101659 scopus 로고    scopus 로고
    • 562 (PDB ID: 1QPU).
    • 562 (PDB ID: 1QPU).
  • 30
    • 60149093022 scopus 로고    scopus 로고
    • [28,29] Stepwise addition of up to 0.33 equivalents of a stock solution of 3 (in DMSO/0.1m KOH 1:1) into an apo-myoglobin solution in 0.1m phosphate buffer at pH 7 gave a mixture of the reconstituted myoglobin monomer, dimer, and trimer. The trimer was identified as a major product (54.3 kDa) and was isolated by SEC with an elution of 14.8 mL (see the Supporting Information).
    • [28,29] Stepwise addition of up to 0.33 equivalents of a stock solution of 3 (in DMSO/0.1m KOH 1:1) into an apo-myoglobin solution in 0.1m phosphate buffer at pH 7 gave a mixture of the reconstituted myoglobin monomer, dimer, and trimer. The trimer was identified as a major product (54.3 kDa) and was isolated by SEC with an elution volume of 14.8 mL (see the Supporting Information).
  • 33
    • 60149105890 scopus 로고    scopus 로고
    • [12]
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.