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Volumn 101, Issue 13, 1997, Pages 2352-2365

Rate of intrachain diffusion of unfolded cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; CARBON MONOXIDE; CHEMICAL BONDS; DIFFUSION; PHOTOLYSIS; POLYPEPTIDES; SOLVENTS;

EID: 0031095826     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9622997     Document Type: Article
Times cited : (114)

References (72)
  • 31
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    • Personal communication
    • Luck, S. D.; Roder, H. Personal communication.
    • Luck, S.D.1    Roder, H.2
  • 39
    • 5544303297 scopus 로고    scopus 로고
    • Personal communication
    • (b) Schejter, A. Personal communication.
    • Schejter, A.1
  • 43
    • 5544299745 scopus 로고    scopus 로고
    • note
    • The heme-CO recombination rate may differ slightly between samples, owing to the difficulty of preparing two independent samples with identical CO saturation.
  • 44
    • 5544244215 scopus 로고    scopus 로고
    • note
    • The BuNC complex of the heme peptide, although readily photolyzeable, proved inconvenient to work with. When prepared with excess BuNC, heme peptide samples exhibit multicomponent absorption spectra immediately after photolysis, indicating the presence of an extra, unidentified heme complex in addition to the expected deoxyheme and methionine (or histidine) complexes. This other complex is absent at very low BuNC concentrations. We concluded that BuNC can displace his 18 as the proximal heme ligand, resulting in formation of the dibutyl isocyanide heme complex. To avoid forming this complex, it was necessary to work at very low BuNC concentrations (e.g. 35 μM BuNC, 100 μM heme peptide), which reduced the photolysis signal and gave a poorer signal-to-noise ratio. For this reason, we eventually used CO instead of BuNC as the photolyzeable ligand in our experiment.
  • 46
    • 85087190919 scopus 로고    scopus 로고
    • note
    • 3 of the heme-methionine data, Figure 8. This process most likely indicates partial aggregation of the unliganded peptide molecules prior to rebinding of the CO.
  • 51
    • 0014364651 scopus 로고
    • G2 measurements for a variety of proteins unfolded in 6 M GuHCl; these results, based on viscosity data, were generally consistent with random coil statistics. Gottfried et al. suggest that the disagreement may reflect long-range intrachain interactions, possibly unique to the unfolded BPTI molecule, that persist even under strongly unfolding conditions.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121
    • Tanford, C.1
  • 56
    • 5544250654 scopus 로고    scopus 로고
    • note
    • This upper limit to the heme-ligand photolysis rate was estimated in previous photodissociation studies that used the same instrument.
  • 63
    • 5544296917 scopus 로고    scopus 로고
    • note
    • 0 would worsen it considerably. We do not understand the origin of the discrepancy in our calculation of the loop formation time from eqs 8 and 9 and that given in ref 8.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.